HEADER TRANSFERASE 31-MAY-05 1ZUH TITLE STRUCTURAL BASIS FOR SHIKIMATE-BINDING SPECIFICITY OF TITLE 2 HELICOBACTER PYLORI SHIKIMATE KINASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SHIKIMATE KINASE; COMPND 3 CHAIN: A; COMPND 4 EC: 2.7.1.71; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI 26695; SOURCE 3 ORGANISM_TAXID: 85962; SOURCE 4 STRAIN: 26695; SOURCE 5 GENE: AROK; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE30 KEYWDS ALPHA-BETA PROTEIN, TRANSFERASE EXPDTA X-RAY DIFFRACTION AUTHOR W.C.CHENG,Y.N.CHANG,W.C.WANG REVDAT 2 24-FEB-09 1ZUH 1 VERSN REVDAT 1 31-MAY-06 1ZUH 0 JRNL AUTH W.C.CHENG,Y.N.CHANG,W.C.WANG JRNL TITL STRUCTURAL BASIS FOR SHIKIMATE-BINDING SPECIFICITY JRNL TITL 2 OF HELICOBACTER PYLORI SHIKIMATE KINASE JRNL REF J.BACTERIOL. V. 187 8156 2005 JRNL REFN ISSN 0021-9193 JRNL PMID 16291688 JRNL DOI 10.1128/JB.187.23.8156-8163.2005 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 16283 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 867 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.79 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1167 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2240 REMARK 3 BIN FREE R VALUE SET COUNT : 61 REMARK 3 BIN FREE R VALUE : 0.2540 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1198 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 165 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.55 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.07000 REMARK 3 B22 (A**2) : 0.07000 REMARK 3 B33 (A**2) : -0.14000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.136 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.630 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1211 ; 0.021 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1620 ; 1.992 ; 1.984 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 149 ; 6.494 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 188 ; 0.322 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 871 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 588 ; 0.240 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 103 ; 0.202 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 37 ; 0.409 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.140 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 741 ; 1.233 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1185 ; 2.353 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 470 ; 3.638 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 435 ; 5.914 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ZUH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-05. REMARK 100 THE RCSB ID CODE IS RCSB033132. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-JUL-04 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL12B2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17190 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790 REMARK 200 RESOLUTION RANGE LOW (A) : 67.420 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 11.600 REMARK 200 R MERGE (I) : 0.04300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.9 REMARK 200 DATA REDUNDANCY IN SHELL : 11.00 REMARK 200 R MERGE FOR SHELL (I) : 0.39500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1VIA REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE,PEG 8000, SODIUM REMARK 280 ACETATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 47.24700 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 47.24700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.64950 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 47.24700 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 47.24700 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 19.64950 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 47.24700 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.24700 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 19.64950 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 47.24700 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.24700 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 19.64950 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 319 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 HIS A -1 REMARK 465 HIS A 0 REMARK 465 MET A 1 REMARK 465 LYS A 111 REMARK 465 GLU A 112 REMARK 465 ARG A 113 REMARK 465 GLU A 114 REMARK 465 LYS A 115 REMARK 465 ARG A 116 REMARK 465 PRO A 117 REMARK 465 LEU A 118 REMARK 465 ILE A 161 REMARK 465 ALA A 162 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 163 O HOH A 327 1.64 REMARK 500 O LYS A 106 O ASN A 109 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD1 ASN A 120 C PHE A 160 3545 1.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 31 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES REMARK 500 ASP A 33 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES REMARK 500 ARG A 57 NE - CZ - NH1 ANGL. DEV. = 6.9 DEGREES REMARK 500 ARG A 57 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 ASP A 65 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES REMARK 500 ASP A 100 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 109 99.97 -68.04 REMARK 500 ASN A 120 -19.07 74.36 REMARK 500 ASN A 121 -75.79 8.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 266 DISTANCE = 5.03 ANGSTROMS DBREF 1ZUH A 1 162 UNP P56073 AROK_HELPY 1 162 SEQADV 1ZUH HIS A -5 UNP P56073 EXPRESSION TAG SEQADV 1ZUH HIS A -4 UNP P56073 EXPRESSION TAG SEQADV 1ZUH HIS A -3 UNP P56073 EXPRESSION TAG SEQADV 1ZUH HIS A -2 UNP P56073 EXPRESSION TAG SEQADV 1ZUH HIS A -1 UNP P56073 EXPRESSION TAG SEQADV 1ZUH HIS A 0 UNP P56073 EXPRESSION TAG SEQRES 1 A 168 HIS HIS HIS HIS HIS HIS MET GLN HIS LEU VAL LEU ILE SEQRES 2 A 168 GLY PHE MET GLY SER GLY LYS SER SER LEU ALA GLN GLU SEQRES 3 A 168 LEU GLY LEU ALA LEU LYS LEU GLU VAL LEU ASP THR ASP SEQRES 4 A 168 MET ILE ILE SER GLU ARG VAL GLY LEU SER VAL ARG GLU SEQRES 5 A 168 ILE PHE GLU GLU LEU GLY GLU ASP ASN PHE ARG MET PHE SEQRES 6 A 168 GLU LYS ASN LEU ILE ASP GLU LEU LYS THR LEU LYS THR SEQRES 7 A 168 PRO HIS VAL ILE SER THR GLY GLY GLY ILE VAL MET HIS SEQRES 8 A 168 GLU ASN LEU LYS GLY LEU GLY THR THR PHE TYR LEU LYS SEQRES 9 A 168 MET ASP PHE GLU THR LEU ILE LYS ARG LEU ASN GLN LYS SEQRES 10 A 168 GLU ARG GLU LYS ARG PRO LEU LEU ASN ASN LEU THR GLN SEQRES 11 A 168 ALA LYS GLU LEU PHE GLU LYS ARG GLN ALA LEU TYR GLU SEQRES 12 A 168 LYS ASN ALA SER PHE ILE ILE ASP ALA ARG GLY GLY LEU SEQRES 13 A 168 ASN ASN SER LEU LYS GLN VAL LEU GLN PHE ILE ALA FORMUL 2 HOH *165(H2 O) HELIX 1 1 GLY A 13 LYS A 26 1 14 HELIX 2 2 THR A 32 GLY A 41 1 10 HELIX 3 3 SER A 43 LEU A 51 1 9 HELIX 4 4 GLY A 52 THR A 69 1 18 HELIX 5 5 GLY A 79 LYS A 89 5 11 HELIX 6 6 ASP A 100 ASN A 109 1 10 HELIX 7 7 LEU A 122 ASN A 139 1 18 HELIX 8 8 GLY A 149 PHE A 160 1 12 SHEET 1 A 5 VAL A 29 ASP A 31 0 SHEET 2 A 5 VAL A 75 SER A 77 1 O VAL A 75 N LEU A 30 SHEET 3 A 5 HIS A 3 ILE A 7 1 N LEU A 4 O ILE A 76 SHEET 4 A 5 GLY A 92 LYS A 98 1 O PHE A 95 N VAL A 5 SHEET 5 A 5 PHE A 142 ASP A 145 1 O ILE A 144 N TYR A 96 CRYST1 94.494 94.494 39.299 90.00 90.00 90.00 P 42 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010583 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010583 0.000000 0.00000 SCALE3 0.000000 0.000000 0.025446 0.00000 ATOM 1 N GLN A 2 49.203 19.782 8.894 1.00 32.18 N ATOM 2 CA GLN A 2 48.877 21.106 8.325 1.00 31.18 C ATOM 3 C GLN A 2 47.373 21.490 8.223 1.00 28.11 C ATOM 4 O GLN A 2 47.080 22.633 8.526 1.00 26.42 O ATOM 5 CB GLN A 2 49.807 21.524 7.174 1.00 33.09 C ATOM 6 CG GLN A 2 49.589 22.914 6.557 1.00 38.49 C ATOM 7 CD GLN A 2 50.610 24.001 6.983 1.00 44.81 C ATOM 8 OE1 GLN A 2 51.729 23.698 7.404 1.00 47.07 O ATOM 9 NE2 GLN A 2 50.198 25.268 6.879 1.00 44.09 N ATOM 10 N HIS A 3 46.426 20.567 7.919 1.00 24.84 N ATOM 11 CA HIS A 3 45.025 20.830 8.354 1.00 20.69 C ATOM 12 C HIS A 3 45.020 21.080 9.861 1.00 19.90 C ATOM 13 O HIS A 3 45.858 20.540 10.566 1.00 19.75 O ATOM 14 CB HIS A 3 44.119 19.603 8.135 1.00 19.47 C ATOM 15 CG HIS A 3 43.898 19.263 6.691 1.00 19.63 C ATOM 16 ND1 HIS A 3 43.566 20.219 5.748 1.00 24.18 N ATOM 17 CD2 HIS A 3 43.878 18.071 6.050 1.00 21.77 C ATOM 18 CE1 HIS A 3 43.382 19.629 4.574 1.00 27.27 C ATOM 19 NE2 HIS A 3 43.564 18.326 4.729 1.00 25.20 N ATOM 20 N LEU A 4 44.054 21.867 10.339 1.00 18.67 N ATOM 21 CA LEU A 4 43.872 22.138 11.761 1.00 17.98 C ATOM 22 C LEU A 4 42.560 21.410 12.098 1.00 18.39 C ATOM 23 O LEU A 4 41.490 21.810 11.662 1.00 18.90 O ATOM 24 CB LEU A 4 43.781 23.643 12.063 1.00 17.66 C ATOM 25 CG LEU A 4 44.945 24.521 11.603 1.00 19.52 C ATOM 26 CD1 LEU A 4 44.737 25.975 12.159 1.00 21.17 C ATOM 27 CD2 LEU A 4 46.239 23.961 12.183 1.00 23.29 C ATOM 28 N VAL A 5 42.667 20.342 12.875 1.00 17.75 N ATOM 29 CA VAL A 5 41.523 19.461 13.137 1.00 15.97 C ATOM 30 C VAL A 5 41.053 19.643 14.566 1.00 15.01 C ATOM 31 O VAL A 5 41.867 19.470 15.486 1.00 15.70 O ATOM 32 CB VAL A 5 41.983 17.998 12.951 1.00 14.56 C ATOM 33 CG1 VAL A 5 40.796 16.999 13.129 1.00 15.92 C ATOM 34 CG2 VAL A 5 42.570 17.817 11.583 1.00 16.78 C ATOM 35 N LEU A 6 39.759 19.972 14.777 1.00 13.75 N ATOM 36 CA LEU A 6 39.239 20.145 16.110 1.00 15.03 C ATOM 37 C LEU A 6 38.491 18.902 16.544 1.00 14.32 C ATOM 38 O LEU A 6 37.606 18.467 15.833 1.00 16.19 O ATOM 39 CB LEU A 6 38.287 21.368 16.163 1.00 14.72 C ATOM 40 CG LEU A 6 38.897 22.676 15.654 1.00 19.88 C ATOM 41 CD1 LEU A 6 37.875 23.760 15.859 1.00 19.50 C ATOM 42 CD2 LEU A 6 40.239 23.021 16.322 1.00 19.24 C ATOM 43 N ILE A 7 38.880 18.315 17.686 1.00 14.33 N ATOM 44 CA ILE A 7 38.207 17.141 18.218 1.00 14.29 C ATOM 45 C ILE A 7 37.678 17.423 19.624 1.00 14.90 C ATOM 46 O ILE A 7 38.179 18.332 20.291 1.00 15.53 O ATOM 47 CB ILE A 7 39.148 15.892 18.274 1.00 13.70 C ATOM 48 CG1 ILE A 7 40.356 16.057 19.231 1.00 15.10 C ATOM 49 CG2 ILE A 7 39.600 15.477 16.781 1.00 16.54 C ATOM 50 CD1 ILE A 7 41.179 14.787 19.288 1.00 17.49 C ATOM 51 N GLY A 8 36.700 16.613 20.016 1.00 15.61 N ATOM 52 CA GLY A 8 36.129 16.700 21.368 1.00 17.86 C ATOM 53 C GLY A 8 34.650 16.386 21.389 1.00 18.08 C ATOM 54 O GLY A 8 34.058 16.021 20.375 1.00 18.60 O ATOM 55 N PHE A 9 34.021 16.541 22.556 1.00 17.83 N ATOM 56 CA PHE A 9 32.600 16.245 22.684 1.00 19.78 C ATOM 57 C PHE A 9 31.713 17.215 21.938 1.00 20.36 C ATOM 58 O PHE A 9 32.046 18.371 21.813 1.00 19.82 O ATOM 59 CB PHE A 9 32.212 16.309 24.172 1.00 19.67 C ATOM 60 CG PHE A 9 32.883 15.269 24.985 1.00 19.99 C ATOM 61 CD1 PHE A 9 34.036 15.580 25.731 1.00 19.93 C ATOM 62 CD2 PHE A 9 32.379 13.963 25.007 1.00 20.70 C ATOM 63 CE1 PHE A 9 34.638 14.607 26.518 1.00 16.96 C ATOM 64 CE2 PHE A 9 33.007 12.980 25.767 1.00 21.12 C ATOM 65 CZ PHE A 9 34.124 13.289 26.514 1.00 22.12 C ATOM 66 N MET A 10 30.579 16.710 21.471 1.00 22.38 N ATOM 67 CA MET A 10 29.524 17.565 20.950 1.00 25.93 C ATOM 68 C MET A 10 29.163 18.530 22.084 1.00 25.97 C ATOM 69 O MET A 10 29.116 18.120 23.250 1.00 26.24 O ATOM 70 CB MET A 10 28.314 16.720 20.518 1.00 26.75 C ATOM 71 CG MET A 10 27.337 17.482 19.640 1.00 32.83 C ATOM 72 SD MET A 10 25.643 16.820 19.894 1.00 45.21 S ATOM 73 CE MET A 10 25.051 18.055 21.029 1.00 41.77 C ATOM 74 N GLY A 11 28.991 19.808 21.725 1.00 26.60 N ATOM 75 CA GLY A 11 28.672 20.876 22.656 1.00 27.40 C ATOM 76 C GLY A 11 29.864 21.558 23.275 1.00 26.38 C ATOM 77 O GLY A 11 29.683 22.450 24.114 1.00 28.23 O ATOM 78 N SER A 12 31.097 21.169 22.905 1.00 25.07 N ATOM 79 CA SER A 12 32.270 21.800 23.484 1.00 24.23 C ATOM 80 C SER A 12 32.575 23.149 22.840 1.00 24.51 C ATOM 81 O SER A 12 33.332 23.915 23.393 1.00 27.60 O ATOM 82 CB SER A 12 33.519 20.893 23.439 1.00 23.23 C ATOM 83 OG SER A 12 33.841 20.483 22.111 1.00 25.75 O ATOM 84 N GLY A 13 32.020 23.435 21.654 1.00 22.81 N ATOM 85 CA GLY A 13 32.341 24.665 20.957 1.00 21.44 C ATOM 86 C GLY A 13 33.131 24.530 19.665 1.00 21.04 C ATOM 87 O GLY A 13 33.703 25.516 19.160 1.00 19.83 O ATOM 88 N LYS A 14 33.182 23.299 19.142 1.00 21.28 N ATOM 89 CA LYS A 14 34.037 23.037 17.992 1.00 20.39 C ATOM 90 C LYS A 14 33.633 23.846 16.770 1.00 20.39 C ATOM 91 O LYS A 14 34.485 24.467 16.136 1.00 19.32 O ATOM 92 CB LYS A 14 34.045 21.553 17.625 1.00 21.03 C ATOM 93 CG LYS A 14 34.725 20.642 18.730 1.00 21.38 C ATOM 94 CD LYS A 14 34.589 19.143 18.413 1.00 19.30 C ATOM 95 CE LYS A 14 33.129 18.693 18.368 1.00 16.55 C ATOM 96 NZ LYS A 14 32.954 17.208 18.314 1.00 18.89 N ATOM 97 N SER A 15 32.345 23.816 16.419 1.00 21.31 N ATOM 98 CA SER A 15 31.919 24.495 15.197 1.00 22.52 C ATOM 99 C SER A 15 32.213 25.987 15.208 1.00 22.25 C ATOM 100 O SER A 15 32.696 26.550 14.218 1.00 22.53 O ATOM 101 CB SER A 15 30.409 24.336 14.988 1.00 24.40 C ATOM 102 OG SER A 15 30.054 23.016 15.046 1.00 30.61 O ATOM 103 N SER A 16 31.905 26.629 16.321 1.00 21.83 N ATOM 104 CA SER A 16 32.101 28.051 16.463 1.00 23.18 C ATOM 105 C SER A 16 33.599 28.368 16.403 1.00 21.79 C ATOM 106 O SER A 16 34.022 29.316 15.748 1.00 21.86 O ATOM 107 CB SER A 16 31.501 28.532 17.776 1.00 23.92 C ATOM 108 OG SER A 16 30.099 28.658 17.540 1.00 30.76 O ATOM 109 N LEU A 17 34.411 27.533 17.055 1.00 19.87 N ATOM 110 CA LEU A 17 35.840 27.789 17.050 1.00 19.00 C ATOM 111 C LEU A 17 36.408 27.595 15.652 1.00 19.63 C ATOM 112 O LEU A 17 37.243 28.377 15.162 1.00 18.82 O ATOM 113 CB LEU A 17 36.567 26.911 18.121 1.00 17.23 C ATOM 114 CG LEU A 17 38.092 27.052 18.154 1.00 19.70 C ATOM 115 CD1 LEU A 17 38.517 28.489 18.509 1.00 19.52 C ATOM 116 CD2 LEU A 17 38.721 26.038 19.145 1.00 17.14 C ATOM 117 N ALA A 18 35.901 26.584 14.964 1.00 19.13 N ATOM 118 CA ALA A 18 36.374 26.341 13.591 1.00 19.57 C ATOM 119 C ALA A 18 36.121 27.557 12.671 1.00 20.36 C ATOM 120 O ALA A 18 37.014 27.966 11.929 1.00 20.11 O ATOM 121 CB ALA A 18 35.761 25.052 13.001 1.00 19.28 C ATOM 122 N GLN A 19 34.909 28.098 12.754 1.00 20.27 N ATOM 123 CA GLN A 19 34.539 29.288 11.969 1.00 21.67 C ATOM 124 C GLN A 19 35.488 30.442 12.251 1.00 21.30 C ATOM 125 O GLN A 19 36.006 31.058 11.303 1.00 22.43 O ATOM 126 CB GLN A 19 33.078 29.707 12.219 1.00 21.44 C ATOM 127 CG GLN A 19 32.754 31.085 11.593 1.00 27.43 C ATOM 128 CD GLN A 19 31.278 31.536 11.722 1.00 32.53 C ATOM 129 OE1 GLN A 19 30.727 32.108 10.775 1.00 36.81 O ATOM 130 NE2 GLN A 19 30.661 31.304 12.885 1.00 34.79 N ATOM 131 N GLU A 20 35.737 30.729 13.533 1.00 20.42 N ATOM 132 CA GLU A 20 36.671 31.793 13.916 1.00 21.23 C ATOM 133 C GLU A 20 38.102 31.587 13.482 1.00 20.91 C ATOM 134 O GLU A 20 38.814 32.528 13.096 1.00 20.15 O ATOM 135 CB GLU A 20 36.626 32.042 15.419 1.00 21.72 C ATOM 136 CG GLU A 20 35.303 32.631 15.858 1.00 23.07 C ATOM 137 CD GLU A 20 35.067 34.051 15.340 1.00 27.16 C ATOM 138 OE1 GLU A 20 36.022 34.829 15.104 1.00 27.82 O ATOM 139 OE2 GLU A 20 33.900 34.380 15.152 1.00 30.34 O ATOM 140 N LEU A 21 38.556 30.342 13.618 1.00 20.69 N ATOM 141 CA LEU A 21 39.866 29.965 13.171 1.00 21.59 C ATOM 142 C LEU A 21 40.050 30.177 11.694 1.00 21.40 C ATOM 143 O LEU A 21 41.088 30.691 11.282 1.00 22.83 O ATOM 144 CB LEU A 21 40.169 28.480 13.493 1.00 21.23 C ATOM 145 CG LEU A 21 41.051 28.226 14.708 1.00 25.49 C ATOM 146 CD1 LEU A 21 41.296 26.676 14.745 1.00 25.73 C ATOM 147 CD2 LEU A 21 42.397 29.001 14.692 1.00 24.81 C ATOM 148 N GLY A 22 39.060 29.770 10.919 1.00 21.46 N ATOM 149 CA GLY A 22 39.056 29.960 9.478 1.00 21.64 C ATOM 150 C GLY A 22 39.185 31.431 9.079 1.00 23.35 C ATOM 151 O GLY A 22 39.921 31.794 8.168 1.00 23.89 O ATOM 152 N LEU A 23 38.494 32.285 9.814 1.00 23.42 N ATOM 153 CA LEU A 23 38.541 33.707 9.555 1.00 24.74 C ATOM 154 C LEU A 23 39.911 34.277 9.920 1.00 24.97 C ATOM 155 O LEU A 23 40.480 35.094 9.190 1.00 25.20 O ATOM 156 CB LEU A 23 37.421 34.379 10.373 1.00 25.00 C ATOM 157 CG LEU A 23 36.007 34.209 9.856 1.00 25.65 C ATOM 158 CD1 LEU A 23 35.029 34.880 10.867 1.00 27.86 C ATOM 159 CD2 LEU A 23 35.837 34.826 8.441 1.00 29.47 C ATOM 160 N ALA A 24 40.477 33.811 11.030 1.00 25.44 N ATOM 161 CA ALA A 24 41.708 34.364 11.545 1.00 25.79 C ATOM 162 C ALA A 24 42.883 34.003 10.667 1.00 26.55 C ATOM 163 O ALA A 24 43.830 34.784 10.565 1.00 27.33 O ATOM 164 CB ALA A 24 41.946 33.944 12.981 1.00 25.74 C ATOM 165 N LEU A 25 42.803 32.840 10.020 1.00 25.01 N ATOM 166 CA LEU A 25 43.889 32.278 9.241 1.00 25.29 C ATOM 167 C LEU A 25 43.647 32.316 7.727 1.00 26.42 C ATOM 168 O LEU A 25 44.513 31.944 6.950 1.00 26.29 O ATOM 169 CB LEU A 25 44.172 30.843 9.716 1.00 25.21 C ATOM 170 CG LEU A 25 44.693 30.734 11.146 1.00 24.03 C ATOM 171 CD1 LEU A 25 44.670 29.267 11.588 1.00 28.98 C ATOM 172 CD2 LEU A 25 46.114 31.378 11.392 1.00 26.17 C ATOM 173 N LYS A 26 42.485 32.808 7.316 1.00 27.21 N ATOM 174 CA LYS A 26 42.074 32.790 5.910 1.00 28.81 C ATOM 175 C LYS A 26 42.050 31.372 5.346 1.00 28.61 C ATOM 176 O LYS A 26 42.557 31.120 4.235 1.00 29.34 O ATOM 177 CB LYS A 26 42.955 33.764 5.082 1.00 30.81 C ATOM 178 CG LYS A 26 42.695 35.224 5.489 1.00 35.29 C ATOM 179 CD LYS A 26 43.773 36.214 5.024 1.00 42.86 C ATOM 180 CE LYS A 26 43.699 37.517 5.836 1.00 46.25 C ATOM 181 NZ LYS A 26 43.365 38.693 4.960 1.00 49.83 N ATOM 182 N LEU A 27 41.465 30.452 6.128 1.00 26.26 N ATOM 183 CA LEU A 27 41.329 29.049 5.740 1.00 25.85 C ATOM 184 C LEU A 27 39.873 28.664 5.572 1.00 25.52 C ATOM 185 O LEU A 27 39.001 29.164 6.300 1.00 26.74 O ATOM 186 CB LEU A 27 42.030 28.128 6.770 1.00 24.90 C ATOM 187 CG LEU A 27 43.570 28.194 6.863 1.00 27.57 C ATOM 188 CD1 LEU A 27 44.079 27.230 7.942 1.00 26.88 C ATOM 189 CD2 LEU A 27 44.370 28.011 5.523 1.00 27.98 C ATOM 190 N GLU A 28 39.606 27.832 4.570 1.00 24.82 N ATOM 191 CA GLU A 28 38.311 27.214 4.392 1.00 25.80 C ATOM 192 C GLU A 28 38.026 26.229 5.539 1.00 23.83 C ATOM 193 O GLU A 28 38.959 25.645 6.092 1.00 23.30 O ATOM 194 CB GLU A 28 38.267 26.400 3.123 1.00 26.51 C ATOM 195 CG GLU A 28 36.875 26.295 2.547 1.00 35.90 C ATOM 196 CD GLU A 28 36.677 27.387 1.503 1.00 44.83 C ATOM 197 OE1 GLU A 28 37.154 27.193 0.348 1.00 48.48 O ATOM 198 OE2 GLU A 28 36.100 28.448 1.861 1.00 46.50 O ATOM 199 N VAL A 29 36.748 26.088 5.864 1.00 22.67 N ATOM 200 CA VAL A 29 36.327 25.303 7.023 1.00 22.72 C ATOM 201 C VAL A 29 35.463 24.160 6.530 1.00 22.93 C ATOM 202 O VAL A 29 34.608 24.345 5.631 1.00 23.90 O ATOM 203 CB VAL A 29 35.546 26.168 8.069 1.00 22.50 C ATOM 204 CG1 VAL A 29 35.098 25.324 9.272 1.00 25.85 C ATOM 205 CG2 VAL A 29 36.359 27.432 8.525 1.00 23.22 C ATOM 206 N LEU A 30 35.716 22.964 7.062 1.00 20.17 N ATOM 207 CA LEU A 30 34.950 21.771 6.769 1.00 21.47 C ATOM 208 C LEU A 30 34.434 21.208 8.085 1.00 20.98 C ATOM 209 O LEU A 30 35.053 21.435 9.161 1.00 22.04 O ATOM 210 CB LEU A 30 35.817 20.702 6.064 1.00 20.64 C ATOM 211 CG LEU A 30 36.611 21.081 4.804 1.00 23.68 C ATOM 212 CD1 LEU A 30 37.518 19.935 4.448 1.00 25.13 C ATOM 213 CD2 LEU A 30 35.650 21.309 3.669 1.00 29.04 C ATOM 214 N ASP A 31 33.293 20.545 7.978 1.00 20.29 N ATOM 215 CA ASP A 31 32.709 19.823 9.061 1.00 20.00 C ATOM 216 C ASP A 31 32.373 18.385 8.566 1.00 19.70 C ATOM 217 O ASP A 31 31.519 18.206 7.689 1.00 19.21 O ATOM 218 CB ASP A 31 31.450 20.602 9.517 1.00 21.02 C ATOM 219 CG ASP A 31 30.731 19.959 10.674 1.00 26.30 C ATOM 220 OD1 ASP A 31 30.449 20.702 11.650 1.00 33.34 O ATOM 221 OD2 ASP A 31 30.356 18.776 10.717 1.00 24.76 O ATOM 222 N THR A 32 32.995 17.383 9.194 1.00 18.24 N ATOM 223 CA THR A 32 32.865 15.980 8.753 1.00 17.11 C ATOM 224 C THR A 32 31.447 15.458 8.880 1.00 17.09 C ATOM 225 O THR A 32 30.918 14.827 7.925 1.00 15.95 O ATOM 226 CB THR A 32 33.873 15.007 9.430 1.00 17.08 C ATOM 227 OG1 THR A 32 33.772 15.091 10.875 1.00 15.81 O ATOM 228 CG2 THR A 32 35.342 15.345 9.056 1.00 17.99 C ATOM 229 N ASP A 33 30.759 15.739 9.990 1.00 16.36 N ATOM 230 CA ASP A 33 29.362 15.293 10.053 1.00 18.56 C ATOM 231 C ASP A 33 28.515 15.919 8.939 1.00 18.93 C ATOM 232 O ASP A 33 27.647 15.228 8.350 1.00 19.35 O ATOM 233 CB ASP A 33 28.704 15.697 11.375 1.00 19.03 C ATOM 234 CG ASP A 33 29.064 14.799 12.532 1.00 20.69 C ATOM 235 OD1 ASP A 33 29.704 13.738 12.441 1.00 19.13 O ATOM 236 OD2 ASP A 33 28.703 15.143 13.665 1.00 25.23 O ATOM 237 N MET A 34 28.698 17.211 8.688 1.00 19.51 N ATOM 238 CA MET A 34 27.876 17.842 7.628 1.00 21.67 C ATOM 239 C MET A 34 28.205 17.336 6.239 1.00 21.35 C ATOM 240 O MET A 34 27.300 17.242 5.378 1.00 20.52 O ATOM 241 CB MET A 34 28.008 19.366 7.601 1.00 24.44 C ATOM 242 CG MET A 34 26.761 20.111 6.949 1.00 33.49 C ATOM 243 SD MET A 34 25.650 19.314 5.595 1.00 49.32 S ATOM 244 CE MET A 34 24.879 20.864 4.853 1.00 48.38 C ATOM 245 N ILE A 35 29.478 17.050 5.997 1.00 19.53 N ATOM 246 CA ILE A 35 29.891 16.507 4.661 1.00 20.02 C ATOM 247 C ILE A 35 29.201 15.145 4.431 1.00 19.94 C ATOM 248 O ILE A 35 28.576 14.920 3.354 1.00 20.87 O ATOM 249 CB ILE A 35 31.441 16.350 4.600 1.00 19.37 C ATOM 250 CG1 ILE A 35 32.079 17.746 4.526 1.00 21.28 C ATOM 251 CG2 ILE A 35 31.856 15.484 3.349 1.00 21.08 C ATOM 252 CD1 ILE A 35 33.537 17.744 4.889 1.00 23.31 C ATOM 253 N ILE A 36 29.256 14.272 5.451 1.00 19.50 N ATOM 254 CA ILE A 36 28.607 12.961 5.367 1.00 20.00 C ATOM 255 C ILE A 36 27.095 13.122 5.167 1.00 21.81 C ATOM 256 O ILE A 36 26.508 12.507 4.270 1.00 21.13 O ATOM 257 CB ILE A 36 28.919 12.082 6.611 1.00 20.74 C ATOM 258 CG1 ILE A 36 30.458 11.843 6.766 1.00 19.73 C ATOM 259 CG2 ILE A 36 28.050 10.777 6.537 1.00 20.81 C ATOM 260 CD1 ILE A 36 30.888 11.298 8.194 1.00 21.72 C ATOM 261 N SER A 37 26.483 13.969 5.989 1.00 21.38 N ATOM 262 CA SER A 37 25.068 14.248 5.871 1.00 25.31 C ATOM 263 C SER A 37 24.717 14.699 4.436 1.00 25.90 C ATOM 264 O SER A 37 23.691 14.277 3.871 1.00 26.50 O ATOM 265 CB SER A 37 24.706 15.372 6.848 1.00 24.78 C ATOM 266 OG SER A 37 23.310 15.628 6.795 1.00 31.45 O ATOM 267 N GLU A 38 25.531 15.586 3.877 1.00 27.53 N ATOM 268 CA GLU A 38 25.250 16.104 2.535 1.00 31.64 C ATOM 269 C GLU A 38 25.427 15.062 1.436 1.00 32.20 C ATOM 270 O GLU A 38 24.734 15.131 0.411 1.00 33.86 O ATOM 271 CB GLU A 38 26.137 17.277 2.198 1.00 32.59 C ATOM 272 CG GLU A 38 25.422 18.595 2.330 1.00 39.36 C ATOM 273 CD GLU A 38 26.023 19.661 1.449 1.00 46.62 C ATOM 274 OE1 GLU A 38 25.947 19.518 0.202 1.00 49.60 O ATOM 275 OE2 GLU A 38 26.582 20.638 2.001 1.00 49.49 O ATOM 276 N ARG A 39 26.368 14.140 1.625 1.00 31.19 N ATOM 277 CA ARG A 39 26.610 13.088 0.645 1.00 31.40 C ATOM 278 C ARG A 39 25.424 12.094 0.619 1.00 31.58 C ATOM 279 O ARG A 39 25.019 11.624 -0.444 1.00 30.71 O ATOM 280 CB ARG A 39 27.894 12.331 0.960 1.00 31.74 C ATOM 281 CG ARG A 39 29.153 13.158 0.868 1.00 34.89 C ATOM 282 CD ARG A 39 29.892 13.038 -0.462 1.00 37.55 C ATOM 283 NE ARG A 39 30.936 14.053 -0.603 1.00 40.17 N ATOM 284 CZ ARG A 39 32.214 13.891 -0.222 1.00 42.53 C ATOM 285 NH1 ARG A 39 32.604 12.763 0.362 1.00 39.12 N ATOM 286 NH2 ARG A 39 33.108 14.867 -0.423 1.00 42.62 N ATOM 287 N VAL A 40 24.886 11.785 1.792 1.00 30.76 N ATOM 288 CA VAL A 40 23.846 10.769 1.934 1.00 30.62 C ATOM 289 C VAL A 40 22.437 11.348 1.795 1.00 31.50 C ATOM 290 O VAL A 40 21.492 10.604 1.516 1.00 30.50 O ATOM 291 CB VAL A 40 23.944 10.065 3.319 1.00 32.40 C ATOM 292 CG1 VAL A 40 22.778 9.068 3.518 1.00 33.44 C ATOM 293 CG2 VAL A 40 25.278 9.329 3.469 1.00 30.76 C ATOM 294 N GLY A 41 22.296 12.649 2.049 1.00 30.81 N ATOM 295 CA GLY A 41 21.014 13.346 1.974 1.00 32.30 C ATOM 296 C GLY A 41 20.107 13.104 3.163 1.00 32.85 C ATOM 297 O GLY A 41 18.875 13.232 3.061 1.00 33.87 O ATOM 298 N LEU A 42 20.700 12.757 4.299 1.00 31.70 N ATOM 299 CA LEU A 42 19.947 12.477 5.509 1.00 30.92 C ATOM 300 C LEU A 42 20.711 13.115 6.619 1.00 30.74 C ATOM 301 O LEU A 42 21.934 13.224 6.537 1.00 28.08 O ATOM 302 CB LEU A 42 19.895 10.981 5.791 1.00 31.79 C ATOM 303 CG LEU A 42 19.166 10.038 4.831 1.00 32.02 C ATOM 304 CD1 LEU A 42 19.311 8.609 5.348 1.00 30.16 C ATOM 305 CD2 LEU A 42 17.705 10.426 4.786 1.00 35.52 C ATOM 306 N SER A 43 20.014 13.498 7.684 1.00 29.99 N ATOM 307 CA SER A 43 20.716 14.056 8.832 1.00 29.92 C ATOM 308 C SER A 43 21.484 12.949 9.571 1.00 29.33 C ATOM 309 O SER A 43 21.181 11.769 9.451 1.00 29.75 O ATOM 310 CB SER A 43 19.720 14.736 9.770 1.00 29.85 C ATOM 311 OG SER A 43 19.087 13.772 10.601 1.00 31.72 O ATOM 312 N VAL A 44 22.489 13.337 10.352 1.00 28.87 N ATOM 313 CA VAL A 44 23.225 12.365 11.119 1.00 28.99 C ATOM 314 C VAL A 44 22.290 11.434 11.888 1.00 29.55 C ATOM 315 O VAL A 44 22.477 10.230 11.876 1.00 27.63 O ATOM 316 CB VAL A 44 24.299 13.029 12.032 1.00 29.24 C ATOM 317 CG1 VAL A 44 24.945 11.991 12.929 1.00 29.00 C ATOM 318 CG2 VAL A 44 25.362 13.739 11.169 1.00 30.49 C ATOM 319 N ARG A 45 21.256 11.978 12.545 1.00 30.30 N ATOM 320 CA ARG A 45 20.359 11.108 13.303 1.00 32.05 C ATOM 321 C ARG A 45 19.567 10.197 12.355 1.00 31.39 C ATOM 322 O ARG A 45 19.335 9.038 12.654 1.00 31.89 O ATOM 323 CB ARG A 45 19.430 11.915 14.219 1.00 32.87 C ATOM 324 CG ARG A 45 18.759 11.071 15.321 1.00 38.49 C ATOM 325 CD ARG A 45 17.295 11.378 15.530 1.00 46.94 C ATOM 326 NE ARG A 45 16.575 11.325 14.255 1.00 53.17 N ATOM 327 CZ ARG A 45 15.253 11.436 14.105 1.00 56.65 C ATOM 328 NH1 ARG A 45 14.725 11.369 12.876 1.00 56.75 N ATOM 329 NH2 ARG A 45 14.456 11.609 15.167 1.00 57.34 N ATOM 330 N GLU A 46 19.167 10.710 11.205 1.00 31.83 N ATOM 331 CA GLU A 46 18.457 9.845 10.242 1.00 32.34 C ATOM 332 C GLU A 46 19.392 8.755 9.723 1.00 31.23 C ATOM 333 O GLU A 46 18.973 7.600 9.489 1.00 30.68 O ATOM 334 CB GLU A 46 17.936 10.634 9.068 1.00 32.58 C ATOM 335 CG GLU A 46 16.881 11.676 9.380 1.00 36.80 C ATOM 336 CD GLU A 46 16.470 12.440 8.125 1.00 40.93 C ATOM 337 OE1 GLU A 46 15.360 12.156 7.643 1.00 46.88 O ATOM 338 OE2 GLU A 46 17.224 13.310 7.617 1.00 38.11 O ATOM 339 N ILE A 47 20.653 9.113 9.524 1.00 29.68 N ATOM 340 CA ILE A 47 21.612 8.102 9.098 1.00 27.47 C ATOM 341 C ILE A 47 21.676 6.983 10.132 1.00 28.50 C ATOM 342 O ILE A 47 21.620 5.801 9.770 1.00 28.99 O ATOM 343 CB ILE A 47 23.047 8.677 8.785 1.00 27.31 C ATOM 344 CG1 ILE A 47 22.984 9.662 7.612 1.00 25.24 C ATOM 345 CG2 ILE A 47 23.985 7.505 8.511 1.00 26.35 C ATOM 346 CD1 ILE A 47 24.250 10.565 7.368 1.00 25.01 C ATOM 347 N PHE A 48 21.805 7.332 11.409 1.00 27.90 N ATOM 348 CA PHE A 48 21.929 6.304 12.443 1.00 30.13 C ATOM 349 C PHE A 48 20.636 5.456 12.516 1.00 30.50 C ATOM 350 O PHE A 48 20.686 4.236 12.721 1.00 31.60 O ATOM 351 CB PHE A 48 22.193 6.938 13.801 1.00 29.58 C ATOM 352 CG PHE A 48 23.660 7.164 14.102 1.00 31.58 C ATOM 353 CD1 PHE A 48 24.373 8.161 13.435 1.00 30.03 C ATOM 354 CD2 PHE A 48 24.314 6.395 15.068 1.00 32.39 C ATOM 355 CE1 PHE A 48 25.690 8.402 13.720 1.00 30.09 C ATOM 356 CE2 PHE A 48 25.668 6.629 15.373 1.00 30.30 C ATOM 357 CZ PHE A 48 26.358 7.620 14.690 1.00 30.09 C ATOM 358 N GLU A 49 19.501 6.112 12.296 1.00 32.24 N ATOM 359 CA GLU A 49 18.200 5.444 12.394 1.00 34.21 C ATOM 360 C GLU A 49 17.906 4.557 11.183 1.00 33.96 C ATOM 361 O GLU A 49 17.453 3.415 11.335 1.00 34.92 O ATOM 362 CB GLU A 49 17.093 6.480 12.551 1.00 34.66 C ATOM 363 CG GLU A 49 17.019 7.048 13.958 1.00 39.91 C ATOM 364 CD GLU A 49 15.897 8.052 14.096 1.00 46.17 C ATOM 365 OE1 GLU A 49 15.352 8.491 13.042 1.00 48.03 O ATOM 366 OE2 GLU A 49 15.600 8.425 15.252 1.00 48.16 O ATOM 367 N GLU A 50 18.164 5.104 10.003 1.00 33.43 N ATOM 368 CA GLU A 50 17.811 4.491 8.741 1.00 33.41 C ATOM 369 C GLU A 50 18.901 3.514 8.280 1.00 33.01 C ATOM 370 O GLU A 50 18.601 2.406 7.818 1.00 31.42 O ATOM 371 CB GLU A 50 17.671 5.586 7.700 1.00 33.91 C ATOM 372 CG GLU A 50 16.336 5.798 6.995 1.00 40.27 C ATOM 373 CD GLU A 50 15.096 5.525 7.826 1.00 46.63 C ATOM 374 OE1 GLU A 50 14.494 6.517 8.292 1.00 50.71 O ATOM 375 OE2 GLU A 50 14.698 4.331 7.968 1.00 46.18 O ATOM 376 N LEU A 51 20.170 3.926 8.391 1.00 31.07 N ATOM 377 CA LEU A 51 21.279 3.166 7.765 1.00 30.15 C ATOM 378 C LEU A 51 22.164 2.449 8.755 1.00 29.16 C ATOM 379 O LEU A 51 22.883 1.548 8.361 1.00 29.93 O ATOM 380 CB LEU A 51 22.166 4.071 6.887 1.00 29.86 C ATOM 381 CG LEU A 51 21.623 5.016 5.821 1.00 32.72 C ATOM 382 CD1 LEU A 51 22.736 5.416 4.827 1.00 36.57 C ATOM 383 CD2 LEU A 51 20.418 4.463 5.077 1.00 34.09 C ATOM 384 N GLY A 52 22.131 2.870 10.024 1.00 27.35 N ATOM 385 CA GLY A 52 22.842 2.218 11.117 1.00 26.88 C ATOM 386 C GLY A 52 24.203 2.848 11.367 1.00 26.35 C ATOM 387 O GLY A 52 24.802 3.413 10.447 1.00 26.19 O ATOM 388 N GLU A 53 24.686 2.746 12.603 1.00 26.59 N ATOM 389 CA GLU A 53 25.996 3.281 12.934 1.00 25.73 C ATOM 390 C GLU A 53 27.164 2.687 12.122 1.00 25.87 C ATOM 391 O GLU A 53 28.122 3.376 11.799 1.00 23.07 O ATOM 392 CB GLU A 53 26.271 3.102 14.416 1.00 26.00 C ATOM 393 CG GLU A 53 27.582 3.749 14.825 1.00 26.56 C ATOM 394 CD GLU A 53 27.713 3.901 16.329 1.00 31.39 C ATOM 395 OE1 GLU A 53 28.735 4.445 16.775 1.00 33.22 O ATOM 396 OE2 GLU A 53 26.806 3.457 17.044 1.00 31.61 O ATOM 397 N ASP A 54 27.086 1.397 11.795 1.00 25.85 N ATOM 398 CA ASP A 54 28.143 0.763 10.993 1.00 25.24 C ATOM 399 C ASP A 54 28.399 1.542 9.705 1.00 23.14 C ATOM 400 O ASP A 54 29.571 1.752 9.293 1.00 21.44 O ATOM 401 CB ASP A 54 27.692 -0.649 10.565 1.00 26.30 C ATOM 402 CG ASP A 54 28.127 -1.717 11.504 1.00 31.55 C ATOM 403 OD1 ASP A 54 28.683 -1.410 12.567 1.00 35.06 O ATOM 404 OD2 ASP A 54 27.912 -2.938 11.256 1.00 34.92 O ATOM 405 N ASN A 55 27.321 1.898 9.023 1.00 21.00 N ATOM 406 CA ASN A 55 27.455 2.696 7.818 1.00 20.36 C ATOM 407 C ASN A 55 28.015 4.077 8.119 1.00 21.26 C ATOM 408 O ASN A 55 28.900 4.553 7.435 1.00 19.94 O ATOM 409 CB ASN A 55 26.158 2.822 7.072 1.00 21.09 C ATOM 410 CG ASN A 55 25.915 1.611 6.173 1.00 21.15 C ATOM 411 OD1 ASN A 55 26.747 1.304 5.303 1.00 19.70 O ATOM 412 ND2 ASN A 55 24.770 0.945 6.360 1.00 22.19 N ATOM 413 N PHE A 56 27.440 4.728 9.122 1.00 19.50 N ATOM 414 CA PHE A 56 27.970 6.056 9.498 1.00 18.95 C ATOM 415 C PHE A 56 29.484 6.017 9.755 1.00 18.66 C ATOM 416 O PHE A 56 30.224 6.860 9.185 1.00 18.66 O ATOM 417 CB PHE A 56 27.207 6.681 10.697 1.00 19.04 C ATOM 418 CG PHE A 56 27.691 8.075 10.983 1.00 19.67 C ATOM 419 CD1 PHE A 56 28.675 8.290 11.923 1.00 20.11 C ATOM 420 CD2 PHE A 56 27.253 9.141 10.202 1.00 19.25 C ATOM 421 CE1 PHE A 56 29.199 9.607 12.139 1.00 23.44 C ATOM 422 CE2 PHE A 56 27.758 10.445 10.408 1.00 22.05 C ATOM 423 CZ PHE A 56 28.737 10.659 11.385 1.00 23.05 C ATOM 424 N ARG A 57 29.951 5.031 10.539 1.00 17.96 N ATOM 425 CA ARG A 57 31.368 4.948 10.895 1.00 19.41 C ATOM 426 C ARG A 57 32.219 4.654 9.656 1.00 19.63 C ATOM 427 O ARG A 57 33.344 5.146 9.505 1.00 17.76 O ATOM 428 CB ARG A 57 31.608 3.826 11.885 1.00 20.66 C ATOM 429 CG ARG A 57 31.293 4.010 13.374 1.00 26.27 C ATOM 430 CD ARG A 57 30.281 5.004 13.854 1.00 35.12 C ATOM 431 NE ARG A 57 30.853 6.315 14.075 1.00 35.58 N ATOM 432 CZ ARG A 57 30.649 7.205 15.095 1.00 31.53 C ATOM 433 NH1 ARG A 57 29.951 7.006 16.208 1.00 34.91 N ATOM 434 NH2 ARG A 57 31.238 8.372 14.957 1.00 22.65 N ATOM 435 N MET A 58 31.679 3.820 8.778 1.00 19.66 N ATOM 436 CA MET A 58 32.424 3.526 7.550 1.00 18.75 C ATOM 437 C MET A 58 32.534 4.782 6.675 1.00 18.77 C ATOM 438 O MET A 58 33.597 5.022 6.090 1.00 19.11 O ATOM 439 CB MET A 58 31.790 2.350 6.783 1.00 19.80 C ATOM 440 CG MET A 58 32.532 2.048 5.528 1.00 18.22 C ATOM 441 SD MET A 58 31.739 0.653 4.611 1.00 23.21 S ATOM 442 CE MET A 58 30.212 1.542 4.002 1.00 18.43 C ATOM 443 N PHE A 59 31.440 5.545 6.529 1.00 18.75 N ATOM 444 CA PHE A 59 31.499 6.815 5.820 1.00 18.56 C ATOM 445 C PHE A 59 32.524 7.766 6.436 1.00 18.38 C ATOM 446 O PHE A 59 33.284 8.433 5.717 1.00 17.46 O ATOM 447 CB PHE A 59 30.155 7.514 5.806 1.00 18.17 C ATOM 448 CG PHE A 59 29.030 6.681 5.178 1.00 19.64 C ATOM 449 CD1 PHE A 59 27.705 6.929 5.546 1.00 22.63 C ATOM 450 CD2 PHE A 59 29.309 5.652 4.245 1.00 19.74 C ATOM 451 CE1 PHE A 59 26.663 6.155 4.991 1.00 23.43 C ATOM 452 CE2 PHE A 59 28.283 4.855 3.703 1.00 22.48 C ATOM 453 CZ PHE A 59 26.943 5.105 4.086 1.00 25.08 C ATOM 454 N GLU A 60 32.533 7.810 7.768 1.00 18.51 N ATOM 455 CA GLU A 60 33.486 8.697 8.503 1.00 17.76 C ATOM 456 C GLU A 60 34.930 8.310 8.239 1.00 18.25 C ATOM 457 O GLU A 60 35.805 9.158 7.965 1.00 16.90 O ATOM 458 CB GLU A 60 33.226 8.552 10.004 1.00 18.61 C ATOM 459 CG GLU A 60 33.607 9.751 10.809 1.00 19.49 C ATOM 460 CD GLU A 60 33.113 9.640 12.268 1.00 19.91 C ATOM 461 OE1 GLU A 60 32.997 8.515 12.809 1.00 20.85 O ATOM 462 OE2 GLU A 60 32.798 10.685 12.849 1.00 22.52 O ATOM 463 N LYS A 61 35.211 7.008 8.347 1.00 19.12 N ATOM 464 CA LYS A 61 36.581 6.494 8.118 1.00 19.94 C ATOM 465 C LYS A 61 37.045 6.837 6.736 1.00 18.61 C ATOM 466 O LYS A 61 38.178 7.278 6.521 1.00 18.42 O ATOM 467 CB LYS A 61 36.613 4.956 8.222 1.00 22.21 C ATOM 468 CG LYS A 61 36.489 4.426 9.632 1.00 29.19 C ATOM 469 CD LYS A 61 36.885 2.938 9.797 1.00 35.87 C ATOM 470 CE LYS A 61 37.972 2.808 10.884 1.00 39.27 C ATOM 471 NZ LYS A 61 37.428 2.474 12.215 1.00 35.41 N ATOM 472 N ASN A 62 36.186 6.590 5.753 1.00 18.01 N ATOM 473 CA ASN A 62 36.580 6.866 4.384 1.00 18.43 C ATOM 474 C ASN A 62 36.764 8.362 4.111 1.00 18.53 C ATOM 475 O ASN A 62 37.630 8.776 3.318 1.00 17.12 O ATOM 476 CB ASN A 62 35.535 6.286 3.430 1.00 18.35 C ATOM 477 CG ASN A 62 35.543 4.753 3.408 1.00 19.99 C ATOM 478 OD1 ASN A 62 36.549 4.122 3.770 1.00 19.98 O ATOM 479 ND2 ASN A 62 34.422 4.138 2.914 1.00 20.15 N ATOM 480 N LEU A 63 35.930 9.180 4.762 1.00 16.65 N ATOM 481 CA LEU A 63 36.025 10.639 4.589 1.00 16.59 C ATOM 482 C LEU A 63 37.357 11.133 5.165 1.00 16.62 C ATOM 483 O LEU A 63 38.021 12.008 4.562 1.00 16.57 O ATOM 484 CB LEU A 63 34.878 11.378 5.301 1.00 16.28 C ATOM 485 CG LEU A 63 34.971 12.932 5.207 1.00 17.80 C ATOM 486 CD1 LEU A 63 34.986 13.427 3.720 1.00 15.42 C ATOM 487 CD2 LEU A 63 33.758 13.527 5.975 1.00 15.22 C ATOM 488 N ILE A 64 37.752 10.583 6.313 1.00 16.03 N ATOM 489 CA ILE A 64 39.118 10.891 6.820 1.00 17.20 C ATOM 490 C ILE A 64 40.196 10.659 5.747 1.00 17.67 C ATOM 491 O ILE A 64 41.036 11.548 5.502 1.00 17.77 O ATOM 492 CB ILE A 64 39.447 10.087 8.048 1.00 17.53 C ATOM 493 CG1 ILE A 64 38.567 10.600 9.232 1.00 16.31 C ATOM 494 CG2 ILE A 64 40.931 10.254 8.465 1.00 19.27 C ATOM 495 CD1 ILE A 64 38.599 9.679 10.396 1.00 20.16 C ATOM 496 N ASP A 65 40.158 9.495 5.112 1.00 18.76 N ATOM 497 CA ASP A 65 41.103 9.226 4.008 1.00 20.91 C ATOM 498 C ASP A 65 41.021 10.233 2.869 1.00 21.05 C ATOM 499 O ASP A 65 42.048 10.706 2.357 1.00 21.02 O ATOM 500 CB ASP A 65 40.925 7.797 3.489 1.00 21.07 C ATOM 501 CG ASP A 65 41.416 6.789 4.471 1.00 23.94 C ATOM 502 OD1 ASP A 65 42.217 7.170 5.353 1.00 26.98 O ATOM 503 OD2 ASP A 65 41.085 5.595 4.475 1.00 25.07 O ATOM 504 N GLU A 66 39.803 10.545 2.473 1.00 22.04 N ATOM 505 CA GLU A 66 39.559 11.515 1.438 1.00 22.46 C ATOM 506 C GLU A 66 40.151 12.889 1.796 1.00 22.32 C ATOM 507 O GLU A 66 40.769 13.526 0.972 1.00 22.98 O ATOM 508 CB GLU A 66 38.072 11.642 1.195 1.00 23.10 C ATOM 509 CG GLU A 66 37.745 12.532 0.000 1.00 26.34 C ATOM 510 CD GLU A 66 36.262 12.843 -0.150 1.00 31.15 C ATOM 511 OE1 GLU A 66 35.940 13.909 -0.716 1.00 32.91 O ATOM 512 OE2 GLU A 66 35.419 12.026 0.242 1.00 28.45 O ATOM 513 N LEU A 67 39.986 13.344 3.044 1.00 21.87 N ATOM 514 CA LEU A 67 40.495 14.672 3.362 1.00 21.61 C ATOM 515 C LEU A 67 42.032 14.722 3.410 1.00 21.31 C ATOM 516 O LEU A 67 42.625 15.791 3.219 1.00 22.71 O ATOM 517 CB LEU A 67 39.827 15.204 4.647 1.00 20.64 C ATOM 518 CG LEU A 67 38.304 15.326 4.541 1.00 21.07 C ATOM 519 CD1 LEU A 67 37.710 15.788 5.871 1.00 22.23 C ATOM 520 CD2 LEU A 67 37.807 16.263 3.434 1.00 22.16 C ATOM 521 N LYS A 68 42.665 13.588 3.682 1.00 21.84 N ATOM 522 CA LYS A 68 44.150 13.493 3.664 1.00 23.82 C ATOM 523 C LYS A 68 44.710 13.805 2.288 1.00 26.45 C ATOM 524 O LYS A 68 45.872 14.276 2.177 1.00 27.60 O ATOM 525 CB LYS A 68 44.596 12.118 4.113 1.00 23.20 C ATOM 526 CG LYS A 68 44.504 11.906 5.620 1.00 23.14 C ATOM 527 CD LYS A 68 44.930 10.529 6.016 1.00 24.24 C ATOM 528 CE LYS A 68 44.962 10.395 7.555 1.00 24.06 C ATOM 529 NZ LYS A 68 45.614 9.180 8.085 1.00 29.08 N ATOM 530 N THR A 69 43.860 13.695 1.273 1.00 27.93 N ATOM 531 CA THR A 69 44.250 14.026 -0.135 1.00 29.78 C ATOM 532 C THR A 69 44.163 15.503 -0.486 1.00 31.23 C ATOM 533 O THR A 69 44.704 15.901 -1.530 1.00 32.23 O ATOM 534 CB THR A 69 43.503 13.169 -1.255 1.00 28.40 C ATOM 535 OG1 THR A 69 42.115 13.517 -1.317 1.00 30.51 O ATOM 536 CG2 THR A 69 43.501 11.700 -0.932 1.00 29.82 C ATOM 537 N LEU A 70 43.502 16.323 0.341 1.00 31.01 N ATOM 538 CA LEU A 70 43.428 17.768 0.067 1.00 33.04 C ATOM 539 C LEU A 70 44.820 18.360 0.268 1.00 33.84 C ATOM 540 O LEU A 70 45.500 18.071 1.243 1.00 35.93 O ATOM 541 CB LEU A 70 42.382 18.524 0.932 1.00 32.03 C ATOM 542 CG LEU A 70 40.865 18.341 0.813 1.00 33.18 C ATOM 543 CD1 LEU A 70 40.127 19.089 1.929 1.00 31.20 C ATOM 544 CD2 LEU A 70 40.281 18.750 -0.569 1.00 34.00 C ATOM 545 N LYS A 71 45.212 19.185 -0.681 1.00 34.66 N ATOM 546 CA LYS A 71 46.528 19.809 -0.764 1.00 36.00 C ATOM 547 C LYS A 71 46.577 21.089 0.092 1.00 34.71 C ATOM 548 O LYS A 71 47.591 21.407 0.701 1.00 35.84 O ATOM 549 CB LYS A 71 46.790 20.154 -2.251 1.00 37.04 C ATOM 550 CG LYS A 71 45.586 20.900 -3.010 1.00 39.43 C ATOM 551 CD LYS A 71 44.181 20.210 -2.796 1.00 41.53 C ATOM 552 CE LYS A 71 42.987 21.000 -3.324 1.00 41.61 C ATOM 553 NZ LYS A 71 42.269 21.817 -2.319 1.00 40.78 N ATOM 554 N THR A 72 45.475 21.829 0.089 1.00 32.64 N ATOM 555 CA THR A 72 45.380 23.112 0.786 1.00 31.08 C ATOM 556 C THR A 72 44.938 22.821 2.240 1.00 28.21 C ATOM 557 O THR A 72 44.047 22.030 2.436 1.00 27.11 O ATOM 558 CB THR A 72 44.381 24.006 0.019 1.00 31.45 C ATOM 559 OG1 THR A 72 44.831 24.096 -1.350 1.00 34.44 O ATOM 560 CG2 THR A 72 44.458 25.443 0.452 1.00 33.21 C ATOM 561 N PRO A 73 45.589 23.437 3.226 1.00 27.66 N ATOM 562 CA PRO A 73 45.163 23.313 4.628 1.00 25.90 C ATOM 563 C PRO A 73 43.740 23.830 4.850 1.00 24.12 C ATOM 564 O PRO A 73 43.392 24.885 4.364 1.00 23.89 O ATOM 565 CB PRO A 73 46.187 24.182 5.390 1.00 26.56 C ATOM 566 CG PRO A 73 47.401 24.270 4.438 1.00 30.01 C ATOM 567 CD PRO A 73 46.793 24.293 3.074 1.00 27.65 C ATOM 568 N HIS A 74 42.925 23.081 5.597 1.00 21.73 N ATOM 569 CA HIS A 74 41.589 23.493 5.917 1.00 20.78 C ATOM 570 C HIS A 74 41.506 23.436 7.468 1.00 18.44 C ATOM 571 O HIS A 74 42.301 22.760 8.101 1.00 19.43 O ATOM 572 CB HIS A 74 40.556 22.532 5.302 1.00 20.27 C ATOM 573 CG HIS A 74 40.415 22.661 3.805 1.00 23.41 C ATOM 574 ND1 HIS A 74 39.247 23.060 3.195 1.00 30.46 N ATOM 575 CD2 HIS A 74 41.282 22.391 2.811 1.00 22.99 C ATOM 576 CE1 HIS A 74 39.416 23.078 1.880 1.00 25.40 C ATOM 577 NE2 HIS A 74 40.637 22.655 1.622 1.00 28.76 N ATOM 578 N VAL A 75 40.618 24.236 8.035 1.00 19.58 N ATOM 579 CA VAL A 75 40.111 23.964 9.397 1.00 19.04 C ATOM 580 C VAL A 75 38.995 22.920 9.323 1.00 18.70 C ATOM 581 O VAL A 75 38.007 23.089 8.562 1.00 20.12 O ATOM 582 CB VAL A 75 39.594 25.240 10.075 1.00 19.80 C ATOM 583 CG1 VAL A 75 39.152 24.937 11.518 1.00 22.05 C ATOM 584 CG2 VAL A 75 40.650 26.333 10.033 1.00 19.70 C ATOM 585 N ILE A 76 39.143 21.839 10.094 1.00 17.62 N ATOM 586 CA ILE A 76 38.198 20.721 10.035 1.00 18.15 C ATOM 587 C ILE A 76 37.567 20.507 11.407 1.00 17.50 C ATOM 588 O ILE A 76 38.307 20.109 12.298 1.00 18.64 O ATOM 589 CB ILE A 76 38.905 19.410 9.543 1.00 17.98 C ATOM 590 CG1 ILE A 76 39.601 19.679 8.199 1.00 19.18 C ATOM 591 CG2 ILE A 76 37.865 18.288 9.433 1.00 18.49 C ATOM 592 CD1 ILE A 76 40.414 18.446 7.579 1.00 20.00 C ATOM 593 N SER A 77 36.243 20.702 11.597 1.00 18.14 N ATOM 594 CA SER A 77 35.610 20.220 12.852 1.00 19.38 C ATOM 595 C SER A 77 35.004 18.854 12.620 1.00 18.64 C ATOM 596 O SER A 77 34.636 18.505 11.506 1.00 18.96 O ATOM 597 CB SER A 77 34.520 21.149 13.494 1.00 21.80 C ATOM 598 OG SER A 77 33.657 21.586 12.473 1.00 28.35 O ATOM 599 N THR A 78 34.901 18.070 13.692 1.00 17.95 N ATOM 600 CA THR A 78 34.710 16.651 13.568 1.00 18.15 C ATOM 601 C THR A 78 33.640 16.236 14.566 1.00 18.70 C ATOM 602 O THR A 78 33.342 16.977 15.490 1.00 20.16 O ATOM 603 CB THR A 78 36.023 16.073 13.896 1.00 19.39 C ATOM 604 OG1 THR A 78 36.430 16.060 15.232 1.00 10.43 O ATOM 605 CG2 THR A 78 37.024 16.011 12.853 1.00 23.90 C ATOM 606 N GLY A 79 33.014 15.082 14.311 1.00 18.94 N ATOM 607 CA GLY A 79 31.993 14.529 15.190 1.00 18.07 C ATOM 608 C GLY A 79 32.649 13.906 16.420 1.00 17.37 C ATOM 609 O GLY A 79 33.820 13.549 16.404 1.00 17.10 O ATOM 610 N GLY A 80 31.882 13.799 17.503 1.00 17.73 N ATOM 611 CA GLY A 80 32.405 13.274 18.772 1.00 18.00 C ATOM 612 C GLY A 80 33.023 11.889 18.713 1.00 19.59 C ATOM 613 O GLY A 80 34.002 11.594 19.416 1.00 20.10 O ATOM 614 N GLY A 81 32.482 11.022 17.857 1.00 18.65 N ATOM 615 CA GLY A 81 33.027 9.681 17.734 1.00 19.97 C ATOM 616 C GLY A 81 34.195 9.466 16.776 1.00 20.74 C ATOM 617 O GLY A 81 34.677 8.314 16.616 1.00 21.51 O ATOM 618 N ILE A 82 34.677 10.528 16.142 1.00 18.82 N ATOM 619 CA ILE A 82 35.681 10.378 15.109 1.00 19.47 C ATOM 620 C ILE A 82 37.007 9.737 15.603 1.00 19.54 C ATOM 621 O ILE A 82 37.759 9.128 14.818 1.00 19.01 O ATOM 622 CB ILE A 82 35.925 11.698 14.396 1.00 19.95 C ATOM 623 CG1 ILE A 82 36.492 11.407 12.963 1.00 21.02 C ATOM 624 CG2 ILE A 82 36.892 12.593 15.234 1.00 21.17 C ATOM 625 CD1 ILE A 82 36.399 12.554 12.023 1.00 22.10 C ATOM 626 N VAL A 83 37.265 9.860 16.897 1.00 18.97 N ATOM 627 CA VAL A 83 38.510 9.348 17.455 1.00 21.35 C ATOM 628 C VAL A 83 38.504 7.821 17.539 1.00 21.98 C ATOM 629 O VAL A 83 39.541 7.265 17.853 1.00 22.71 O ATOM 630 CB VAL A 83 38.858 9.965 18.851 1.00 21.52 C ATOM 631 CG1 VAL A 83 39.404 11.378 18.674 1.00 22.67 C ATOM 632 CG2 VAL A 83 37.650 9.921 19.756 1.00 20.66 C ATOM 633 N MET A 84 37.372 7.157 17.276 1.00 22.92 N ATOM 634 CA MET A 84 37.374 5.701 17.158 1.00 25.16 C ATOM 635 C MET A 84 38.224 5.185 15.963 1.00 25.06 C ATOM 636 O MET A 84 38.635 4.007 15.940 1.00 26.37 O ATOM 637 CB MET A 84 35.945 5.151 17.110 1.00 26.85 C ATOM 638 CG MET A 84 35.333 5.137 15.744 1.00 30.39 C ATOM 639 SD MET A 84 33.839 4.135 15.689 1.00 43.18 S ATOM 640 CE MET A 84 34.353 2.668 14.866 1.00 39.81 C ATOM 641 N HIS A 85 38.524 6.053 15.005 1.00 23.20 N ATOM 642 CA HIS A 85 39.233 5.627 13.810 1.00 23.10 C ATOM 643 C HIS A 85 40.748 5.729 13.908 1.00 24.26 C ATOM 644 O HIS A 85 41.304 6.813 14.201 1.00 22.53 O ATOM 645 CB HIS A 85 38.730 6.383 12.567 1.00 22.37 C ATOM 646 CG HIS A 85 37.244 6.372 12.449 1.00 22.80 C ATOM 647 ND1 HIS A 85 36.532 5.201 12.310 1.00 24.26 N ATOM 648 CD2 HIS A 85 36.322 7.366 12.572 1.00 18.94 C ATOM 649 CE1 HIS A 85 35.239 5.476 12.301 1.00 25.29 C ATOM 650 NE2 HIS A 85 35.084 6.779 12.469 1.00 20.63 N ATOM 651 N GLU A 86 41.411 4.595 13.637 1.00 24.22 N ATOM 652 CA GLU A 86 42.875 4.570 13.708 1.00 27.18 C ATOM 653 C GLU A 86 43.543 5.513 12.677 1.00 26.15 C ATOM 654 O GLU A 86 44.649 6.039 12.906 1.00 26.04 O ATOM 655 CB GLU A 86 43.395 3.111 13.689 1.00 28.61 C ATOM 656 CG GLU A 86 44.439 2.767 12.646 1.00 36.84 C ATOM 657 CD GLU A 86 44.504 1.262 12.414 1.00 45.93 C ATOM 658 OE1 GLU A 86 43.813 0.787 11.476 1.00 49.71 O ATOM 659 OE2 GLU A 86 45.228 0.556 13.177 1.00 47.76 O ATOM 660 N ASN A 87 42.828 5.798 11.594 1.00 24.19 N ATOM 661 CA ASN A 87 43.341 6.645 10.532 1.00 24.62 C ATOM 662 C ASN A 87 43.206 8.138 10.778 1.00 23.42 C ATOM 663 O ASN A 87 43.672 8.914 9.977 1.00 23.22 O ATOM 664 CB ASN A 87 42.797 6.220 9.135 1.00 25.34 C ATOM 665 CG ASN A 87 41.288 6.484 8.953 1.00 26.64 C ATOM 666 OD1 ASN A 87 40.806 6.823 7.855 1.00 28.21 O ATOM 667 ND2 ASN A 87 40.552 6.323 10.018 1.00 27.18 N ATOM 668 N LEU A 88 42.544 8.541 11.872 1.00 22.74 N ATOM 669 CA LEU A 88 42.402 9.967 12.199 1.00 24.45 C ATOM 670 C LEU A 88 43.791 10.577 12.447 1.00 25.53 C ATOM 671 O LEU A 88 44.073 11.721 12.062 1.00 24.61 O ATOM 672 CB LEU A 88 41.503 10.138 13.436 1.00 23.51 C ATOM 673 CG LEU A 88 40.757 11.479 13.767 1.00 28.73 C ATOM 674 CD1 LEU A 88 40.906 11.885 15.215 1.00 27.16 C ATOM 675 CD2 LEU A 88 40.913 12.652 12.836 1.00 27.41 C ATOM 676 N LYS A 89 44.660 9.777 13.071 1.00 27.50 N ATOM 677 CA LYS A 89 46.087 10.120 13.212 1.00 29.09 C ATOM 678 C LYS A 89 46.719 10.413 11.856 1.00 27.50 C ATOM 679 O LYS A 89 46.729 9.578 10.905 1.00 28.08 O ATOM 680 CB LYS A 89 46.849 9.003 13.958 1.00 29.53 C ATOM 681 CG LYS A 89 48.304 9.362 14.337 1.00 35.70 C ATOM 682 CD LYS A 89 49.177 8.090 14.517 1.00 37.05 C ATOM 683 CE LYS A 89 50.615 8.449 14.950 1.00 42.45 C ATOM 684 NZ LYS A 89 50.718 9.094 16.340 1.00 43.74 N ATOM 685 N GLY A 90 47.306 11.593 11.772 1.00 27.41 N ATOM 686 CA GLY A 90 47.914 12.057 10.541 1.00 24.45 C ATOM 687 C GLY A 90 47.020 12.907 9.655 1.00 22.06 C ATOM 688 O GLY A 90 47.504 13.462 8.675 1.00 22.85 O ATOM 689 N LEU A 91 45.749 13.066 9.989 1.00 20.55 N ATOM 690 CA LEU A 91 44.907 13.937 9.189 1.00 19.09 C ATOM 691 C LEU A 91 45.449 15.383 9.224 1.00 18.84 C ATOM 692 O LEU A 91 45.557 16.062 8.182 1.00 20.30 O ATOM 693 CB LEU A 91 43.440 13.896 9.673 1.00 18.31 C ATOM 694 CG LEU A 91 42.465 14.848 8.970 1.00 19.65 C ATOM 695 CD1 LEU A 91 42.494 14.635 7.390 1.00 19.80 C ATOM 696 CD2 LEU A 91 41.019 14.691 9.492 1.00 19.75 C ATOM 697 N GLY A 92 45.824 15.818 10.424 1.00 18.28 N ATOM 698 CA GLY A 92 46.410 17.133 10.597 1.00 17.14 C ATOM 699 C GLY A 92 46.833 17.345 12.037 1.00 18.59 C ATOM 700 O GLY A 92 46.943 16.404 12.846 1.00 18.27 O ATOM 701 N THR A 93 47.067 18.619 12.356 1.00 18.66 N ATOM 702 CA THR A 93 47.412 18.978 13.719 1.00 19.35 C ATOM 703 C THR A 93 46.118 18.939 14.519 1.00 18.71 C ATOM 704 O THR A 93 45.155 19.611 14.137 1.00 20.40 O ATOM 705 CB THR A 93 47.951 20.386 13.743 1.00 19.32 C ATOM 706 OG1 THR A 93 49.084 20.480 12.867 1.00 22.24 O ATOM 707 CG2 THR A 93 48.474 20.722 15.204 1.00 19.04 C ATOM 708 N THR A 94 46.059 18.175 15.590 1.00 18.28 N ATOM 709 CA THR A 94 44.739 17.942 16.183 1.00 20.27 C ATOM 710 C THR A 94 44.623 18.642 17.549 1.00 18.91 C ATOM 711 O THR A 94 45.493 18.479 18.355 1.00 18.70 O ATOM 712 CB THR A 94 44.556 16.438 16.304 1.00 22.11 C ATOM 713 OG1 THR A 94 44.547 15.875 14.973 1.00 27.09 O ATOM 714 CG2 THR A 94 43.210 16.111 16.795 1.00 24.37 C ATOM 715 N PHE A 95 43.513 19.361 17.790 1.00 18.63 N ATOM 716 CA PHE A 95 43.335 20.191 18.971 1.00 18.14 C ATOM 717 C PHE A 95 42.148 19.589 19.691 1.00 18.18 C ATOM 718 O PHE A 95 41.038 19.544 19.126 1.00 17.39 O ATOM 719 CB PHE A 95 43.015 21.604 18.499 1.00 17.82 C ATOM 720 CG PHE A 95 44.162 22.258 17.819 1.00 18.39 C ATOM 721 CD1 PHE A 95 44.339 22.149 16.413 1.00 19.69 C ATOM 722 CD2 PHE A 95 45.055 22.992 18.564 1.00 15.97 C ATOM 723 CE1 PHE A 95 45.409 22.773 15.806 1.00 18.58 C ATOM 724 CE2 PHE A 95 46.129 23.622 17.950 1.00 18.64 C ATOM 725 CZ PHE A 95 46.307 23.503 16.584 1.00 17.38 C ATOM 726 N TYR A 96 42.376 19.077 20.911 1.00 16.77 N ATOM 727 CA TYR A 96 41.267 18.643 21.757 1.00 16.40 C ATOM 728 C TYR A 96 40.702 19.841 22.525 1.00 15.67 C ATOM 729 O TYR A 96 41.412 20.487 23.288 1.00 15.55 O ATOM 730 CB TYR A 96 41.745 17.543 22.741 1.00 16.72 C ATOM 731 CG TYR A 96 40.769 17.157 23.832 1.00 16.68 C ATOM 732 CD1 TYR A 96 41.226 16.797 25.090 1.00 19.77 C ATOM 733 CD2 TYR A 96 39.367 17.145 23.616 1.00 18.13 C ATOM 734 CE1 TYR A 96 40.356 16.405 26.096 1.00 22.41 C ATOM 735 CE2 TYR A 96 38.486 16.781 24.624 1.00 19.31 C ATOM 736 CZ TYR A 96 39.000 16.398 25.889 1.00 22.02 C ATOM 737 OH TYR A 96 38.122 16.020 26.916 1.00 21.98 O ATOM 738 N LEU A 97 39.463 20.219 22.218 1.00 14.47 N ATOM 739 CA LEU A 97 38.823 21.341 22.916 1.00 16.96 C ATOM 740 C LEU A 97 38.297 20.821 24.254 1.00 17.20 C ATOM 741 O LEU A 97 37.189 20.299 24.346 1.00 17.61 O ATOM 742 CB LEU A 97 37.658 21.875 22.033 1.00 17.68 C ATOM 743 CG LEU A 97 36.991 23.176 22.476 1.00 20.64 C ATOM 744 CD1 LEU A 97 38.057 24.354 22.663 1.00 22.93 C ATOM 745 CD2 LEU A 97 35.913 23.521 21.407 1.00 21.43 C ATOM 746 N LYS A 98 39.111 20.942 25.305 1.00 17.71 N ATOM 747 CA LYS A 98 38.873 20.232 26.576 1.00 17.17 C ATOM 748 C LYS A 98 38.021 21.071 27.523 1.00 19.37 C ATOM 749 O LYS A 98 38.413 22.171 27.921 1.00 19.52 O ATOM 750 CB LYS A 98 40.217 19.882 27.246 1.00 17.40 C ATOM 751 CG LYS A 98 40.073 19.073 28.581 1.00 16.56 C ATOM 752 CD LYS A 98 41.386 18.550 29.073 1.00 19.22 C ATOM 753 CE LYS A 98 41.214 17.888 30.476 1.00 22.51 C ATOM 754 NZ LYS A 98 42.506 17.143 30.749 1.00 23.64 N ATOM 755 N MET A 99 36.830 20.546 27.828 1.00 21.78 N ATOM 756 CA MET A 99 35.941 21.106 28.869 1.00 24.53 C ATOM 757 C MET A 99 35.830 20.078 29.957 1.00 25.68 C ATOM 758 O MET A 99 35.739 18.880 29.669 1.00 24.62 O ATOM 759 CB MET A 99 34.505 21.225 28.399 1.00 25.75 C ATOM 760 CG MET A 99 34.201 21.787 27.126 1.00 30.06 C ATOM 761 SD MET A 99 32.513 22.381 27.407 1.00 38.27 S ATOM 762 CE MET A 99 32.931 24.163 26.740 1.00 31.48 C ATOM 763 N ASP A 100 35.778 20.546 31.207 1.00 24.63 N ATOM 764 CA ASP A 100 35.419 19.678 32.309 1.00 25.88 C ATOM 765 C ASP A 100 33.959 19.174 32.129 1.00 23.62 C ATOM 766 O ASP A 100 33.116 19.808 31.468 1.00 23.69 O ATOM 767 CB ASP A 100 35.542 20.470 33.625 1.00 27.12 C ATOM 768 CG ASP A 100 34.678 21.705 33.624 1.00 32.65 C ATOM 769 OD1 ASP A 100 33.596 21.702 34.247 1.00 37.39 O ATOM 770 OD2 ASP A 100 34.951 22.743 32.984 1.00 41.51 O ATOM 771 N PHE A 101 33.688 18.037 32.737 1.00 22.98 N ATOM 772 CA PHE A 101 32.389 17.383 32.709 1.00 23.44 C ATOM 773 C PHE A 101 31.251 18.296 33.133 1.00 24.18 C ATOM 774 O PHE A 101 30.255 18.358 32.455 1.00 23.38 O ATOM 775 CB PHE A 101 32.438 16.137 33.599 1.00 22.56 C ATOM 776 CG PHE A 101 31.191 15.313 33.567 1.00 23.25 C ATOM 777 CD1 PHE A 101 30.366 15.238 34.700 1.00 24.65 C ATOM 778 CD2 PHE A 101 30.847 14.565 32.437 1.00 22.33 C ATOM 779 CE1 PHE A 101 29.194 14.460 34.659 1.00 24.06 C ATOM 780 CE2 PHE A 101 29.735 13.783 32.424 1.00 21.35 C ATOM 781 CZ PHE A 101 28.888 13.740 33.549 1.00 25.33 C ATOM 782 N GLU A 102 31.411 19.014 34.242 1.00 24.37 N ATOM 783 CA GLU A 102 30.266 19.783 34.743 1.00 27.76 C ATOM 784 C GLU A 102 29.870 20.927 33.792 1.00 26.64 C ATOM 785 O GLU A 102 28.695 21.149 33.571 1.00 27.49 O ATOM 786 CB GLU A 102 30.530 20.305 36.153 1.00 29.33 C ATOM 787 CG GLU A 102 30.687 19.161 37.159 1.00 34.38 C ATOM 788 CD GLU A 102 32.035 18.400 37.110 1.00 41.60 C ATOM 789 OE1 GLU A 102 32.149 17.405 37.872 1.00 45.64 O ATOM 790 OE2 GLU A 102 32.995 18.760 36.353 1.00 41.98 O ATOM 791 N THR A 103 30.866 21.590 33.218 1.00 27.15 N ATOM 792 CA THR A 103 30.627 22.627 32.202 1.00 27.78 C ATOM 793 C THR A 103 29.939 22.084 30.968 1.00 25.98 C ATOM 794 O THR A 103 29.031 22.727 30.394 1.00 25.69 O ATOM 795 CB THR A 103 31.944 23.307 31.830 1.00 28.74 C ATOM 796 OG1 THR A 103 32.519 23.820 33.036 1.00 35.54 O ATOM 797 CG2 THR A 103 31.709 24.576 31.007 1.00 29.65 C ATOM 798 N LEU A 104 30.422 20.927 30.527 1.00 24.15 N ATOM 799 CA LEU A 104 29.913 20.300 29.325 1.00 23.29 C ATOM 800 C LEU A 104 28.485 19.898 29.514 1.00 21.93 C ATOM 801 O LEU A 104 27.677 20.068 28.618 1.00 24.05 O ATOM 802 CB LEU A 104 30.766 19.051 29.013 1.00 22.60 C ATOM 803 CG LEU A 104 30.893 18.431 27.616 1.00 28.17 C ATOM 804 CD1 LEU A 104 30.620 16.902 27.555 1.00 26.74 C ATOM 805 CD2 LEU A 104 30.386 19.295 26.387 1.00 25.85 C ATOM 806 N ILE A 105 28.142 19.350 30.683 1.00 23.66 N ATOM 807 CA ILE A 105 26.759 18.959 30.938 1.00 24.19 C ATOM 808 C ILE A 105 25.863 20.202 30.953 1.00 24.31 C ATOM 809 O ILE A 105 24.777 20.187 30.397 1.00 23.92 O ATOM 810 CB ILE A 105 26.635 18.135 32.258 1.00 23.73 C ATOM 811 CG1 ILE A 105 27.208 16.725 32.039 1.00 25.90 C ATOM 812 CG2 ILE A 105 25.197 18.119 32.737 1.00 26.27 C ATOM 813 CD1 ILE A 105 26.381 15.796 31.189 1.00 28.17 C ATOM 814 N LYS A 106 26.356 21.273 31.545 1.00 27.14 N ATOM 815 CA LYS A 106 25.639 22.535 31.537 1.00 29.54 C ATOM 816 C LYS A 106 25.379 22.981 30.092 1.00 30.16 C ATOM 817 O LYS A 106 24.245 23.266 29.709 1.00 30.01 O ATOM 818 CB LYS A 106 26.437 23.572 32.338 1.00 29.93 C ATOM 819 CG LYS A 106 25.571 24.315 33.387 1.00 36.98 C ATOM 820 CD LYS A 106 26.346 25.441 34.122 1.00 38.39 C ATOM 821 CE LYS A 106 26.063 26.835 33.470 1.00 44.28 C ATOM 822 NZ LYS A 106 26.135 27.936 34.499 1.00 41.79 N ATOM 823 N ARG A 107 26.432 23.000 29.284 1.00 30.36 N ATOM 824 CA ARG A 107 26.306 23.418 27.886 1.00 30.37 C ATOM 825 C ARG A 107 25.322 22.527 27.128 1.00 30.58 C ATOM 826 O ARG A 107 24.474 23.044 26.394 1.00 31.29 O ATOM 827 CB ARG A 107 27.670 23.423 27.194 1.00 29.58 C ATOM 828 CG ARG A 107 28.556 24.634 27.397 1.00 33.40 C ATOM 829 CD ARG A 107 29.717 24.646 26.367 1.00 37.04 C ATOM 830 NE ARG A 107 29.867 25.855 25.524 1.00 43.03 N ATOM 831 CZ ARG A 107 29.641 25.901 24.203 1.00 45.19 C ATOM 832 NH1 ARG A 107 29.174 24.839 23.546 1.00 46.58 N ATOM 833 NH2 ARG A 107 29.827 27.040 23.530 1.00 50.98 N ATOM 834 N LEU A 108 25.411 21.201 27.298 1.00 30.87 N ATOM 835 CA LEU A 108 24.474 20.280 26.632 1.00 32.16 C ATOM 836 C LEU A 108 23.017 20.450 27.066 1.00 34.13 C ATOM 837 O LEU A 108 22.101 20.379 26.233 1.00 34.23 O ATOM 838 CB LEU A 108 24.884 18.815 26.842 1.00 32.02 C ATOM 839 CG LEU A 108 26.182 18.376 26.140 1.00 32.24 C ATOM 840 CD1 LEU A 108 26.573 16.981 26.627 1.00 32.09 C ATOM 841 CD2 LEU A 108 26.043 18.396 24.639 1.00 31.75 C ATOM 842 N ASN A 109 22.806 20.586 28.375 1.00 36.54 N ATOM 843 CA ASN A 109 21.545 21.083 28.908 1.00 39.09 C ATOM 844 C ASN A 109 21.582 22.529 28.439 1.00 40.97 C ATOM 845 O ASN A 109 22.286 23.345 29.032 1.00 42.82 O ATOM 846 CB ASN A 109 21.560 21.056 30.438 1.00 38.26 C ATOM 847 CG ASN A 109 21.558 19.635 31.021 1.00 39.20 C ATOM 848 OD1 ASN A 109 21.172 18.663 30.379 1.00 41.93 O ATOM 849 ND2 ASN A 109 21.993 19.529 32.255 1.00 40.56 N ATOM 850 N GLN A 110 20.899 22.876 27.368 1.00 42.61 N ATOM 851 CA GLN A 110 21.353 24.102 26.672 1.00 43.06 C ATOM 852 C GLN A 110 21.355 25.346 27.560 1.00 43.68 C ATOM 853 O GLN A 110 22.375 26.034 27.704 1.00 43.48 O ATOM 854 CB GLN A 110 20.614 24.317 25.362 1.00 43.27 C ATOM 855 CG GLN A 110 21.348 23.632 24.171 1.00 43.15 C ATOM 856 CD GLN A 110 20.568 22.471 23.551 1.00 42.00 C ATOM 857 OE1 GLN A 110 20.392 21.414 24.175 1.00 38.07 O ATOM 858 NE2 GLN A 110 20.109 22.660 22.318 1.00 41.27 N ATOM 859 N LEU A 119 18.926 9.627 40.785 1.00 55.29 N ATOM 860 CA LEU A 119 18.351 8.315 40.491 1.00 55.37 C ATOM 861 C LEU A 119 19.405 7.497 39.753 1.00 54.68 C ATOM 862 O LEU A 119 19.075 6.733 38.842 1.00 54.76 O ATOM 863 CB LEU A 119 17.070 8.446 39.636 1.00 55.81 C ATOM 864 CG LEU A 119 16.594 9.761 38.980 1.00 56.73 C ATOM 865 CD1 LEU A 119 17.444 10.206 37.759 1.00 55.89 C ATOM 866 CD2 LEU A 119 15.105 9.661 38.606 1.00 57.70 C ATOM 867 N ASN A 120 20.659 7.672 40.201 1.00 53.20 N ATOM 868 CA ASN A 120 21.934 7.407 39.477 1.00 50.89 C ATOM 869 C ASN A 120 22.358 8.409 38.358 1.00 48.25 C ATOM 870 O ASN A 120 23.551 8.507 38.053 1.00 47.04 O ATOM 871 CB ASN A 120 22.151 5.929 39.122 1.00 52.09 C ATOM 872 CG ASN A 120 21.725 5.575 37.693 1.00 55.03 C ATOM 873 OD1 ASN A 120 20.561 5.250 37.454 1.00 56.18 O ATOM 874 ND2 ASN A 120 22.675 5.617 36.742 1.00 58.03 N ATOM 875 N ASN A 121 21.381 9.187 37.866 1.00 44.91 N ATOM 876 CA ASN A 121 21.486 10.225 36.795 1.00 41.77 C ATOM 877 C ASN A 121 22.766 10.432 35.929 1.00 37.94 C ATOM 878 O ASN A 121 22.742 10.036 34.774 1.00 38.42 O ATOM 879 CB ASN A 121 20.549 11.464 37.035 1.00 42.16 C ATOM 880 CG ASN A 121 21.246 12.702 37.604 1.00 45.09 C ATOM 881 OD1 ASN A 121 22.265 12.625 38.297 1.00 49.34 O ATOM 882 ND2 ASN A 121 20.670 13.861 37.322 1.00 46.57 N ATOM 883 N LEU A 122 23.851 11.043 36.421 1.00 32.61 N ATOM 884 CA LEU A 122 24.990 11.318 35.524 1.00 29.27 C ATOM 885 C LEU A 122 26.112 10.259 35.543 1.00 26.69 C ATOM 886 O LEU A 122 27.128 10.440 34.904 1.00 23.59 O ATOM 887 CB LEU A 122 25.562 12.733 35.757 1.00 29.06 C ATOM 888 CG LEU A 122 24.509 13.837 35.575 1.00 30.67 C ATOM 889 CD1 LEU A 122 25.042 15.158 36.059 1.00 34.18 C ATOM 890 CD2 LEU A 122 24.111 13.910 34.099 1.00 33.03 C ATOM 891 N THR A 123 25.913 9.153 36.269 1.00 24.53 N ATOM 892 CA THR A 123 26.955 8.157 36.429 1.00 23.47 C ATOM 893 C THR A 123 27.430 7.567 35.116 1.00 23.98 C ATOM 894 O THR A 123 28.640 7.519 34.867 1.00 25.87 O ATOM 895 CB THR A 123 26.454 7.011 37.378 1.00 23.97 C ATOM 896 OG1 THR A 123 26.352 7.547 38.697 1.00 22.50 O ATOM 897 CG2 THR A 123 27.523 5.874 37.497 1.00 23.82 C ATOM 898 N GLN A 124 26.487 7.150 34.282 1.00 23.83 N ATOM 899 CA GLN A 124 26.794 6.551 32.985 1.00 24.81 C ATOM 900 C GLN A 124 27.408 7.605 32.035 1.00 24.57 C ATOM 901 O GLN A 124 28.399 7.336 31.372 1.00 24.66 O ATOM 902 CB GLN A 124 25.554 5.918 32.367 1.00 25.91 C ATOM 903 CG GLN A 124 24.968 4.706 33.109 1.00 28.15 C ATOM 904 CD GLN A 124 23.997 3.958 32.197 1.00 31.99 C ATOM 905 OE1 GLN A 124 23.005 4.516 31.770 1.00 34.21 O ATOM 906 NE2 GLN A 124 24.317 2.724 31.866 1.00 31.24 N ATOM 907 N ALA A 125 26.854 8.817 32.047 1.00 24.08 N ATOM 908 CA ALA A 125 27.392 9.947 31.254 1.00 23.15 C ATOM 909 C ALA A 125 28.860 10.237 31.595 1.00 22.15 C ATOM 910 O ALA A 125 29.694 10.488 30.704 1.00 22.66 O ATOM 911 CB ALA A 125 26.527 11.215 31.443 1.00 23.64 C ATOM 912 N LYS A 126 29.187 10.170 32.870 1.00 20.70 N ATOM 913 CA LYS A 126 30.544 10.414 33.356 1.00 20.32 C ATOM 914 C LYS A 126 31.496 9.274 32.958 1.00 21.85 C ATOM 915 O LYS A 126 32.660 9.531 32.607 1.00 20.87 O ATOM 916 CB LYS A 126 30.506 10.664 34.892 1.00 20.76 C ATOM 917 CG LYS A 126 31.848 10.991 35.560 1.00 22.30 C ATOM 918 CD LYS A 126 32.530 12.176 34.844 1.00 24.75 C ATOM 919 CE LYS A 126 33.402 12.958 35.807 1.00 28.62 C ATOM 920 NZ LYS A 126 34.639 12.197 36.095 1.00 31.20 N ATOM 921 N GLU A 127 31.017 8.019 32.951 1.00 22.60 N ATOM 922 CA GLU A 127 31.864 6.911 32.453 1.00 22.42 C ATOM 923 C GLU A 127 32.186 7.105 31.001 1.00 21.71 C ATOM 924 O GLU A 127 33.347 6.868 30.561 1.00 22.75 O ATOM 925 CB GLU A 127 31.158 5.548 32.537 1.00 22.61 C ATOM 926 CG GLU A 127 30.701 5.228 33.918 1.00 25.02 C ATOM 927 CD GLU A 127 29.816 3.998 33.987 1.00 28.38 C ATOM 928 OE1 GLU A 127 29.127 3.574 32.982 1.00 28.44 O ATOM 929 OE2 GLU A 127 29.804 3.462 35.098 1.00 30.36 O ATOM 930 N LEU A 128 31.172 7.493 30.242 1.00 21.69 N ATOM 931 CA LEU A 128 31.333 7.689 28.796 1.00 22.69 C ATOM 932 C LEU A 128 32.283 8.875 28.561 1.00 22.43 C ATOM 933 O LEU A 128 33.205 8.783 27.716 1.00 21.71 O ATOM 934 CB LEU A 128 29.978 7.873 28.097 1.00 24.38 C ATOM 935 CG LEU A 128 29.960 8.262 26.614 1.00 30.06 C ATOM 936 CD1 LEU A 128 30.617 7.203 25.707 1.00 34.84 C ATOM 937 CD2 LEU A 128 28.508 8.509 26.162 1.00 34.55 C ATOM 938 N PHE A 129 32.103 9.928 29.373 1.00 19.40 N ATOM 939 CA PHE A 129 33.025 11.075 29.389 1.00 19.77 C ATOM 940 C PHE A 129 34.491 10.650 29.622 1.00 20.54 C ATOM 941 O PHE A 129 35.403 11.036 28.874 1.00 18.87 O ATOM 942 CB PHE A 129 32.567 12.152 30.413 1.00 18.78 C ATOM 943 CG PHE A 129 33.486 13.357 30.467 1.00 21.51 C ATOM 944 CD1 PHE A 129 33.215 14.466 29.663 1.00 22.49 C ATOM 945 CD2 PHE A 129 34.597 13.384 31.329 1.00 20.93 C ATOM 946 CE1 PHE A 129 34.048 15.631 29.732 1.00 20.27 C ATOM 947 CE2 PHE A 129 35.465 14.522 31.364 1.00 21.25 C ATOM 948 CZ PHE A 129 35.167 15.633 30.572 1.00 20.80 C ATOM 949 N GLU A 130 34.752 9.862 30.677 1.00 19.49 N ATOM 950 CA GLU A 130 36.132 9.552 30.973 1.00 21.36 C ATOM 951 C GLU A 130 36.735 8.703 29.867 1.00 21.36 C ATOM 952 O GLU A 130 37.912 8.893 29.520 1.00 22.56 O ATOM 953 CB GLU A 130 36.289 8.847 32.339 1.00 22.74 C ATOM 954 CG GLU A 130 36.053 9.738 33.544 1.00 24.44 C ATOM 955 CD GLU A 130 37.014 10.889 33.645 1.00 27.95 C ATOM 956 OE1 GLU A 130 38.212 10.693 33.357 1.00 32.00 O ATOM 957 OE2 GLU A 130 36.569 11.985 34.031 1.00 28.04 O ATOM 958 N LYS A 131 35.970 7.762 29.325 1.00 22.64 N ATOM 959 CA LYS A 131 36.542 6.891 28.278 1.00 23.61 C ATOM 960 C LYS A 131 36.807 7.681 26.973 1.00 22.56 C ATOM 961 O LYS A 131 37.847 7.530 26.338 1.00 21.39 O ATOM 962 CB LYS A 131 35.703 5.615 28.115 1.00 25.51 C ATOM 963 CG LYS A 131 34.685 5.585 27.025 1.00 31.62 C ATOM 964 CD LYS A 131 34.233 4.115 26.785 1.00 37.33 C ATOM 965 CE LYS A 131 32.979 3.789 27.568 1.00 38.54 C ATOM 966 NZ LYS A 131 32.569 2.360 27.385 1.00 37.84 N ATOM 967 N ARG A 132 35.923 8.599 26.643 1.00 20.40 N ATOM 968 CA ARG A 132 36.092 9.334 25.386 1.00 21.15 C ATOM 969 C ARG A 132 37.198 10.372 25.579 1.00 20.47 C ATOM 970 O ARG A 132 37.968 10.610 24.662 1.00 20.24 O ATOM 971 CB ARG A 132 34.776 9.985 24.924 1.00 21.22 C ATOM 972 CG ARG A 132 33.859 9.072 24.042 1.00 26.89 C ATOM 973 CD ARG A 132 34.153 9.131 22.483 1.00 31.83 C ATOM 974 NE ARG A 132 33.342 8.114 21.779 1.00 37.49 N ATOM 975 CZ ARG A 132 32.161 8.339 21.208 1.00 39.49 C ATOM 976 NH1 ARG A 132 31.604 9.549 21.236 1.00 38.12 N ATOM 977 NH2 ARG A 132 31.515 7.338 20.605 1.00 41.06 N ATOM 978 N GLN A 133 37.307 10.968 26.771 1.00 18.74 N ATOM 979 CA GLN A 133 38.370 11.954 26.999 1.00 18.92 C ATOM 980 C GLN A 133 39.742 11.317 26.863 1.00 20.00 C ATOM 981 O GLN A 133 40.656 11.873 26.255 1.00 19.30 O ATOM 982 CB GLN A 133 38.202 12.618 28.380 1.00 19.77 C ATOM 983 CG GLN A 133 39.445 13.451 28.714 1.00 20.39 C ATOM 984 CD GLN A 133 39.149 14.483 29.757 1.00 25.48 C ATOM 985 OE1 GLN A 133 39.398 14.256 30.970 1.00 31.73 O ATOM 986 NE2 GLN A 133 38.601 15.593 29.333 1.00 22.89 N ATOM 987 N ALA A 134 39.895 10.101 27.385 1.00 20.24 N ATOM 988 CA ALA A 134 41.152 9.397 27.218 1.00 21.15 C ATOM 989 C ALA A 134 41.515 9.221 25.714 1.00 20.88 C ATOM 990 O ALA A 134 42.667 9.437 25.296 1.00 22.30 O ATOM 991 CB ALA A 134 41.080 8.019 27.990 1.00 21.44 C ATOM 992 N LEU A 135 40.531 8.893 24.883 1.00 20.37 N ATOM 993 CA LEU A 135 40.753 8.808 23.412 1.00 20.35 C ATOM 994 C LEU A 135 41.045 10.151 22.714 1.00 19.59 C ATOM 995 O LEU A 135 41.902 10.228 21.795 1.00 20.17 O ATOM 996 CB LEU A 135 39.540 8.177 22.729 1.00 20.44 C ATOM 997 CG LEU A 135 39.305 6.696 22.985 1.00 26.18 C ATOM 998 CD1 LEU A 135 38.055 6.322 22.242 1.00 28.24 C ATOM 999 CD2 LEU A 135 40.525 5.967 22.416 1.00 29.79 C ATOM 1000 N TYR A 136 40.354 11.230 23.134 1.00 17.53 N ATOM 1001 CA TYR A 136 40.729 12.557 22.631 1.00 18.11 C ATOM 1002 C TYR A 136 42.164 12.919 22.943 1.00 18.31 C ATOM 1003 O TYR A 136 42.854 13.467 22.102 1.00 17.08 O ATOM 1004 CB TYR A 136 39.822 13.662 23.189 1.00 17.18 C ATOM 1005 CG TYR A 136 38.352 13.505 22.768 1.00 17.65 C ATOM 1006 CD1 TYR A 136 37.315 13.615 23.712 1.00 16.78 C ATOM 1007 CD2 TYR A 136 38.011 13.276 21.424 1.00 18.41 C ATOM 1008 CE1 TYR A 136 36.014 13.470 23.368 1.00 19.44 C ATOM 1009 CE2 TYR A 136 36.674 13.126 21.047 1.00 18.36 C ATOM 1010 CZ TYR A 136 35.670 13.194 22.025 1.00 19.88 C ATOM 1011 OH TYR A 136 34.348 13.043 21.672 1.00 19.00 O ATOM 1012 N GLU A 137 42.606 12.648 24.180 1.00 17.65 N ATOM 1013 CA GLU A 137 43.967 12.962 24.555 1.00 19.93 C ATOM 1014 C GLU A 137 45.016 12.088 23.857 1.00 21.51 C ATOM 1015 O GLU A 137 46.089 12.587 23.533 1.00 23.43 O ATOM 1016 CB GLU A 137 44.156 13.030 26.091 1.00 19.01 C ATOM 1017 CG GLU A 137 43.274 14.175 26.658 1.00 21.11 C ATOM 1018 CD GLU A 137 43.355 14.432 28.165 1.00 28.38 C ATOM 1019 OE1 GLU A 137 44.131 13.763 28.877 1.00 30.01 O ATOM 1020 OE2 GLU A 137 42.638 15.332 28.631 1.00 26.36 O ATOM 1021 N LYS A 138 44.698 10.811 23.606 1.00 21.01 N ATOM 1022 CA LYS A 138 45.586 9.956 22.814 1.00 23.54 C ATOM 1023 C LYS A 138 45.806 10.480 21.404 1.00 23.28 C ATOM 1024 O LYS A 138 46.844 10.204 20.758 1.00 25.80 O ATOM 1025 CB LYS A 138 44.956 8.544 22.660 1.00 23.08 C ATOM 1026 CG LYS A 138 45.942 7.402 22.714 1.00 31.25 C ATOM 1027 CD LYS A 138 45.281 6.116 23.303 1.00 38.25 C ATOM 1028 CE LYS A 138 45.867 5.727 24.692 1.00 41.78 C ATOM 1029 NZ LYS A 138 46.632 4.409 24.725 1.00 45.86 N ATOM 1030 N ASN A 139 44.811 11.187 20.897 1.00 21.80 N ATOM 1031 CA ASN A 139 44.782 11.629 19.512 1.00 21.56 C ATOM 1032 C ASN A 139 45.146 13.092 19.304 1.00 22.34 C ATOM 1033 O ASN A 139 45.018 13.595 18.195 1.00 23.86 O ATOM 1034 CB ASN A 139 43.385 11.390 18.948 1.00 22.82 C ATOM 1035 CG ASN A 139 43.187 9.937 18.471 1.00 27.02 C ATOM 1036 OD1 ASN A 139 43.646 9.574 17.369 1.00 29.04 O ATOM 1037 ND2 ASN A 139 42.531 9.112 19.289 1.00 23.76 N ATOM 1038 N ALA A 140 45.558 13.797 20.349 1.00 18.50 N ATOM 1039 CA ALA A 140 45.678 15.253 20.253 1.00 18.07 C ATOM 1040 C ALA A 140 47.132 15.669 20.007 1.00 18.49 C ATOM 1041 O ALA A 140 48.031 15.118 20.630 1.00 18.66 O ATOM 1042 CB ALA A 140 45.198 15.873 21.582 1.00 17.82 C ATOM 1043 N SER A 141 47.354 16.657 19.143 1.00 17.93 N ATOM 1044 CA SER A 141 48.622 17.366 19.098 1.00 18.63 C ATOM 1045 C SER A 141 48.755 18.414 20.237 1.00 19.26 C ATOM 1046 O SER A 141 49.855 18.686 20.710 1.00 19.77 O ATOM 1047 CB SER A 141 48.737 18.078 17.754 1.00 18.91 C ATOM 1048 OG SER A 141 48.537 17.187 16.641 1.00 18.37 O ATOM 1049 N PHE A 142 47.625 19.011 20.611 1.00 18.62 N ATOM 1050 CA PHE A 142 47.528 20.070 21.612 1.00 19.39 C ATOM 1051 C PHE A 142 46.191 19.937 22.320 1.00 18.75 C ATOM 1052 O PHE A 142 45.187 19.522 21.718 1.00 19.44 O ATOM 1053 CB PHE A 142 47.572 21.422 20.931 1.00 19.42 C ATOM 1054 CG PHE A 142 48.911 21.810 20.373 1.00 23.93 C ATOM 1055 CD1 PHE A 142 49.115 21.838 18.991 1.00 24.84 C ATOM 1056 CD2 PHE A 142 49.970 22.212 21.228 1.00 26.89 C ATOM 1057 CE1 PHE A 142 50.366 22.245 18.456 1.00 27.21 C ATOM 1058 CE2 PHE A 142 51.241 22.567 20.698 1.00 25.48 C ATOM 1059 CZ PHE A 142 51.413 22.599 19.319 1.00 26.77 C ATOM 1060 N ILE A 143 46.171 20.258 23.606 1.00 17.71 N ATOM 1061 CA ILE A 143 44.951 20.306 24.366 1.00 17.26 C ATOM 1062 C ILE A 143 44.619 21.783 24.596 1.00 18.31 C ATOM 1063 O ILE A 143 45.411 22.529 25.154 1.00 18.81 O ATOM 1064 CB ILE A 143 45.138 19.615 25.761 1.00 18.79 C ATOM 1065 CG1 ILE A 143 45.489 18.146 25.570 1.00 18.13 C ATOM 1066 CG2 ILE A 143 43.862 19.818 26.625 1.00 16.68 C ATOM 1067 CD1 ILE A 143 45.764 17.358 26.883 1.00 21.07 C ATOM 1068 N ILE A 144 43.457 22.204 24.128 1.00 16.76 N ATOM 1069 CA ILE A 144 43.015 23.562 24.397 1.00 16.85 C ATOM 1070 C ILE A 144 42.156 23.541 25.684 1.00 17.08 C ATOM 1071 O ILE A 144 41.242 22.727 25.845 1.00 18.04 O ATOM 1072 CB ILE A 144 42.084 24.008 23.261 1.00 16.97 C ATOM 1073 CG1 ILE A 144 42.799 23.931 21.915 1.00 16.02 C ATOM 1074 CG2 ILE A 144 41.562 25.459 23.531 1.00 18.24 C ATOM 1075 CD1 ILE A 144 41.747 24.032 20.780 1.00 20.68 C ATOM 1076 N ASP A 145 42.416 24.468 26.582 1.00 17.99 N ATOM 1077 CA ASP A 145 41.510 24.613 27.711 1.00 19.83 C ATOM 1078 C ASP A 145 40.292 25.426 27.271 1.00 20.37 C ATOM 1079 O ASP A 145 40.386 26.642 27.075 1.00 20.41 O ATOM 1080 CB ASP A 145 42.252 25.281 28.854 1.00 21.56 C ATOM 1081 CG ASP A 145 41.440 25.364 30.117 1.00 25.48 C ATOM 1082 OD1 ASP A 145 40.198 25.244 30.099 1.00 23.67 O ATOM 1083 OD2 ASP A 145 42.009 25.540 31.219 1.00 32.61 O ATOM 1084 N ALA A 146 39.162 24.735 27.112 1.00 20.68 N ATOM 1085 CA ALA A 146 37.920 25.328 26.555 1.00 23.51 C ATOM 1086 C ALA A 146 37.093 26.077 27.581 1.00 26.13 C ATOM 1087 O ALA A 146 36.037 26.664 27.243 1.00 28.98 O ATOM 1088 CB ALA A 146 37.100 24.265 25.890 1.00 22.97 C ATOM 1089 N ARG A 147 37.557 26.082 28.826 1.00 27.18 N ATOM 1090 CA ARG A 147 36.734 26.648 29.929 1.00 30.13 C ATOM 1091 C ARG A 147 36.576 28.172 29.927 1.00 30.68 C ATOM 1092 O ARG A 147 35.604 28.677 30.502 1.00 32.92 O ATOM 1093 CB ARG A 147 37.235 26.161 31.269 1.00 29.24 C ATOM 1094 CG ARG A 147 37.063 24.655 31.360 1.00 29.69 C ATOM 1095 CD ARG A 147 37.713 24.034 32.600 1.00 26.04 C ATOM 1096 NE ARG A 147 39.150 24.208 32.624 1.00 28.96 N ATOM 1097 CZ ARG A 147 39.919 23.746 33.606 1.00 33.91 C ATOM 1098 NH1 ARG A 147 39.359 23.087 34.617 1.00 36.42 N ATOM 1099 NH2 ARG A 147 41.236 23.934 33.599 1.00 32.19 N ATOM 1100 N GLY A 148 37.502 28.884 29.288 1.00 30.70 N ATOM 1101 CA GLY A 148 37.404 30.333 29.179 1.00 30.65 C ATOM 1102 C GLY A 148 36.572 30.899 28.033 1.00 29.41 C ATOM 1103 O GLY A 148 36.535 32.127 27.882 1.00 29.27 O ATOM 1104 N GLY A 149 35.936 30.053 27.221 1.00 27.58 N ATOM 1105 CA GLY A 149 35.119 30.536 26.117 1.00 26.23 C ATOM 1106 C GLY A 149 35.879 30.599 24.810 1.00 24.90 C ATOM 1107 O GLY A 149 37.093 30.426 24.785 1.00 23.17 O ATOM 1108 N LEU A 150 35.155 30.916 23.742 1.00 23.55 N ATOM 1109 CA LEU A 150 35.679 30.856 22.374 1.00 23.06 C ATOM 1110 C LEU A 150 36.957 31.685 22.168 1.00 23.25 C ATOM 1111 O LEU A 150 37.984 31.187 21.645 1.00 19.58 O ATOM 1112 CB LEU A 150 34.560 31.317 21.413 1.00 24.42 C ATOM 1113 CG LEU A 150 34.809 31.496 19.911 1.00 27.29 C ATOM 1114 CD1 LEU A 150 35.608 32.780 19.569 1.00 29.52 C ATOM 1115 CD2 LEU A 150 35.483 30.317 19.330 1.00 31.57 C ATOM 1116 N ASN A 151 36.914 32.954 22.561 1.00 21.72 N ATOM 1117 CA ASN A 151 38.089 33.774 22.325 1.00 22.30 C ATOM 1118 C ASN A 151 39.346 33.281 23.020 1.00 21.65 C ATOM 1119 O ASN A 151 40.429 33.334 22.431 1.00 21.82 O ATOM 1120 CB ASN A 151 37.811 35.258 22.615 1.00 22.68 C ATOM 1121 CG ASN A 151 37.326 35.991 21.379 1.00 27.84 C ATOM 1122 OD1 ASN A 151 37.979 35.925 20.316 1.00 31.40 O ATOM 1123 ND2 ASN A 151 36.175 36.696 21.493 1.00 24.02 N ATOM 1124 N ASN A 152 39.194 32.783 24.240 1.00 20.00 N ATOM 1125 CA ASN A 152 40.341 32.287 24.965 1.00 20.88 C ATOM 1126 C ASN A 152 40.853 31.002 24.280 1.00 19.62 C ATOM 1127 O ASN A 152 42.050 30.804 24.176 1.00 20.30 O ATOM 1128 CB ASN A 152 39.985 32.008 26.400 1.00 20.91 C ATOM 1129 CG ASN A 152 41.215 31.647 27.223 1.00 25.80 C ATOM 1130 OD1 ASN A 152 42.154 32.428 27.321 1.00 34.43 O ATOM 1131 ND2 ASN A 152 41.213 30.461 27.784 1.00 31.69 N ATOM 1132 N SER A 153 39.925 30.184 23.764 1.00 19.44 N ATOM 1133 CA SER A 153 40.331 28.951 23.025 1.00 18.95 C ATOM 1134 C SER A 153 41.038 29.312 21.715 1.00 19.28 C ATOM 1135 O SER A 153 42.071 28.746 21.356 1.00 18.50 O ATOM 1136 CB SER A 153 39.095 28.119 22.697 1.00 19.68 C ATOM 1137 OG SER A 153 38.505 27.629 23.870 1.00 20.00 O ATOM 1138 N LEU A 154 40.494 30.311 21.015 1.00 17.96 N ATOM 1139 CA LEU A 154 41.095 30.804 19.783 1.00 20.35 C ATOM 1140 C LEU A 154 42.495 31.313 20.015 1.00 19.73 C ATOM 1141 O LEU A 154 43.423 30.983 19.271 1.00 20.03 O ATOM 1142 CB LEU A 154 40.242 31.970 19.245 1.00 21.33 C ATOM 1143 CG LEU A 154 40.138 32.372 17.768 1.00 28.28 C ATOM 1144 CD1 LEU A 154 40.066 33.877 17.524 1.00 29.73 C ATOM 1145 CD2 LEU A 154 40.986 31.588 16.780 1.00 25.08 C ATOM 1146 N LYS A 155 42.674 32.069 21.096 1.00 20.71 N ATOM 1147 CA LYS A 155 43.994 32.611 21.443 1.00 20.43 C ATOM 1148 C LYS A 155 45.036 31.500 21.655 1.00 20.66 C ATOM 1149 O LYS A 155 46.190 31.581 21.171 1.00 19.14 O ATOM 1150 CB LYS A 155 43.826 33.462 22.704 1.00 20.75 C ATOM 1151 CG LYS A 155 45.079 34.197 23.251 1.00 27.17 C ATOM 1152 CD LYS A 155 44.684 34.889 24.595 1.00 33.76 C ATOM 1153 CE LYS A 155 45.561 34.459 25.767 1.00 40.34 C ATOM 1154 NZ LYS A 155 44.894 34.699 27.116 1.00 43.18 N ATOM 1155 N GLN A 156 44.610 30.443 22.353 1.00 20.43 N ATOM 1156 CA GLN A 156 45.485 29.288 22.568 1.00 19.91 C ATOM 1157 C GLN A 156 45.911 28.634 21.242 1.00 20.34 C ATOM 1158 O GLN A 156 47.105 28.337 21.018 1.00 20.71 O ATOM 1159 CB GLN A 156 44.787 28.298 23.488 1.00 19.95 C ATOM 1160 CG GLN A 156 44.641 28.745 24.928 1.00 21.04 C ATOM 1161 CD GLN A 156 43.744 27.777 25.711 1.00 22.52 C ATOM 1162 OE1 GLN A 156 44.153 26.629 26.013 1.00 20.28 O ATOM 1163 NE2 GLN A 156 42.496 28.212 25.999 1.00 20.93 N ATOM 1164 N VAL A 157 44.950 28.424 20.346 1.00 20.23 N ATOM 1165 CA VAL A 157 45.278 27.738 19.114 1.00 20.17 C ATOM 1166 C VAL A 157 46.332 28.560 18.341 1.00 22.06 C ATOM 1167 O VAL A 157 47.359 28.020 17.861 1.00 20.82 O ATOM 1168 CB VAL A 157 44.021 27.493 18.267 1.00 19.64 C ATOM 1169 CG1 VAL A 157 44.392 27.014 16.893 1.00 19.60 C ATOM 1170 CG2 VAL A 157 43.082 26.476 18.984 1.00 18.62 C ATOM 1171 N LEU A 158 46.079 29.867 18.245 1.00 22.30 N ATOM 1172 CA LEU A 158 46.969 30.732 17.439 1.00 25.16 C ATOM 1173 C LEU A 158 48.384 30.829 18.013 1.00 26.15 C ATOM 1174 O LEU A 158 49.351 30.836 17.257 1.00 26.94 O ATOM 1175 CB LEU A 158 46.366 32.121 17.225 1.00 23.66 C ATOM 1176 CG LEU A 158 45.049 32.194 16.447 1.00 24.06 C ATOM 1177 CD1 LEU A 158 44.498 33.611 16.347 1.00 24.38 C ATOM 1178 CD2 LEU A 158 45.102 31.529 15.023 1.00 26.24 C ATOM 1179 N GLN A 159 48.478 30.888 19.342 1.00 28.18 N ATOM 1180 CA GLN A 159 49.754 30.915 20.061 1.00 30.31 C ATOM 1181 C GLN A 159 50.480 29.595 19.868 1.00 29.61 C ATOM 1182 O GLN A 159 51.704 29.587 19.615 1.00 28.69 O ATOM 1183 CB GLN A 159 49.500 31.196 21.562 1.00 31.23 C ATOM 1184 CG GLN A 159 50.676 30.945 22.526 1.00 37.46 C ATOM 1185 CD GLN A 159 50.312 31.293 23.983 1.00 45.12 C ATOM 1186 OE1 GLN A 159 51.145 31.833 24.719 1.00 48.65 O ATOM 1187 NE2 GLN A 159 49.065 30.990 24.396 1.00 46.43 N ATOM 1188 N PHE A 160 49.723 28.491 19.921 1.00 29.58 N ATOM 1189 CA PHE A 160 50.296 27.149 19.798 1.00 29.75 C ATOM 1190 C PHE A 160 50.776 26.830 18.379 1.00 30.00 C ATOM 1191 O PHE A 160 50.287 27.332 17.337 1.00 30.22 O ATOM 1192 CB PHE A 160 49.337 26.045 20.302 1.00 30.28 C ATOM 1193 CG PHE A 160 48.865 26.211 21.751 1.00 32.51 C ATOM 1194 CD1 PHE A 160 49.219 27.343 22.534 1.00 37.57 C ATOM 1195 CD2 PHE A 160 48.034 25.248 22.318 1.00 36.87 C ATOM 1196 CE1 PHE A 160 48.751 27.496 23.850 1.00 35.59 C ATOM 1197 CE2 PHE A 160 47.559 25.354 23.655 1.00 31.47 C ATOM 1198 CZ PHE A 160 47.915 26.483 24.416 1.00 37.10 C TER 1199 PHE A 160 HETATM 1200 O HOH A 163 30.005 21.911 18.964 1.00 20.77 O HETATM 1201 O HOH A 164 35.823 14.983 17.761 1.00 17.90 O HETATM 1202 O HOH A 165 32.395 13.160 12.092 1.00 20.37 O HETATM 1203 O HOH A 166 35.242 18.286 24.499 1.00 16.51 O HETATM 1204 O HOH A 167 19.112 4.918 34.236 1.00 28.35 O HETATM 1205 O HOH A 168 31.594 21.233 5.701 1.00 22.36 O HETATM 1206 O HOH A 169 30.970 4.775 37.383 1.00 26.34 O HETATM 1207 O HOH A 170 29.083 12.328 14.739 1.00 28.01 O HETATM 1208 O HOH A 171 36.829 33.829 25.778 1.00 23.03 O HETATM 1209 O HOH A 172 45.247 23.007 28.172 1.00 29.55 O HETATM 1210 O HOH A 173 30.192 16.971 17.668 1.00 26.24 O HETATM 1211 O HOH A 174 31.537 11.139 15.204 1.00 22.15 O HETATM 1212 O HOH A 175 32.124 5.941 1.979 1.00 24.86 O HETATM 1213 O HOH A 176 36.047 17.760 27.178 1.00 21.85 O HETATM 1214 O HOH A 177 34.844 9.597 1.512 1.00 27.82 O HETATM 1215 O HOH A 178 25.469 -3.981 10.132 1.00 32.44 O HETATM 1216 O HOH A 179 48.521 12.836 21.943 1.00 24.30 O HETATM 1217 O HOH A 180 44.698 9.201 27.153 1.00 30.31 O HETATM 1218 O HOH A 181 47.465 13.628 13.619 1.00 31.63 O HETATM 1219 O HOH A 182 31.462 17.365 12.564 1.00 24.81 O HETATM 1220 O HOH A 183 29.880 13.862 21.874 1.00 23.40 O HETATM 1221 O HOH A 184 32.645 9.107 3.084 1.00 22.98 O HETATM 1222 O HOH A 185 23.544 6.997 35.224 1.00 28.64 O HETATM 1223 O HOH A 186 38.759 28.841 26.718 1.00 25.43 O HETATM 1224 O HOH A 187 34.254 27.667 20.866 1.00 24.30 O HETATM 1225 O HOH A 188 30.175 25.490 18.298 1.00 28.62 O HETATM 1226 O HOH A 189 41.844 26.656 2.863 1.00 28.42 O HETATM 1227 O HOH A 190 35.209 31.005 8.734 1.00 28.06 O HETATM 1228 O HOH A 191 17.875 7.348 36.053 1.00 41.44 O HETATM 1229 O HOH A 192 38.095 17.701 31.281 1.00 32.65 O HETATM 1230 O HOH A 193 48.536 9.724 7.722 1.00 30.23 O HETATM 1231 O HOH A 194 31.801 0.491 10.395 1.00 28.06 O HETATM 1232 O HOH A 195 46.901 13.431 28.410 1.00 33.42 O HETATM 1233 O HOH A 196 30.695 7.503 36.752 1.00 25.09 O HETATM 1234 O HOH A 197 40.571 22.088 30.173 1.00 32.90 O HETATM 1235 O HOH A 198 28.660 7.538 40.186 1.00 28.63 O HETATM 1236 O HOH A 199 52.097 17.356 20.302 1.00 25.67 O HETATM 1237 O HOH A 200 29.046 14.358 17.216 1.00 33.43 O HETATM 1238 O HOH A 201 39.287 5.270 26.343 1.00 28.18 O HETATM 1239 O HOH A 202 33.567 7.695 35.985 1.00 34.96 O HETATM 1240 O HOH A 203 24.767 0.219 9.894 1.00 37.07 O HETATM 1241 O HOH A 204 29.535 9.684 18.425 1.00 41.95 O HETATM 1242 O HOH A 205 39.085 20.353 32.336 1.00 34.34 O HETATM 1243 O HOH A 206 29.227 27.465 20.825 1.00 39.62 O HETATM 1244 O HOH A 207 49.683 14.361 12.125 1.00 34.59 O HETATM 1245 O HOH A 208 21.298 14.865 13.359 1.00 33.68 O HETATM 1246 O HOH A 209 38.332 35.135 14.041 1.00 27.01 O HETATM 1247 O HOH A 210 38.236 7.651 0.772 1.00 28.48 O HETATM 1248 O HOH A 211 40.145 2.125 13.020 1.00 35.60 O HETATM 1249 O HOH A 212 33.890 24.703 2.988 1.00 36.86 O HETATM 1250 O HOH A 213 24.092 9.179 32.781 1.00 30.74 O HETATM 1251 O HOH A 214 38.395 35.913 26.419 1.00 34.19 O HETATM 1252 O HOH A 215 40.818 35.569 20.725 1.00 31.27 O HETATM 1253 O HOH A 216 34.889 28.027 4.832 1.00 32.42 O HETATM 1254 O HOH A 217 31.748 19.580 14.892 1.00 35.08 O HETATM 1255 O HOH A 218 47.976 14.540 16.116 1.00 40.11 O HETATM 1256 O HOH A 219 42.010 15.804 33.282 1.00 37.19 O HETATM 1257 O HOH A 220 34.173 6.734 0.129 1.00 35.44 O HETATM 1258 O HOH A 221 31.729 32.192 15.419 1.00 40.51 O HETATM 1259 O HOH A 222 25.536 18.366 9.922 1.00 35.67 O HETATM 1260 O HOH A 223 38.311 33.589 29.480 1.00 37.37 O HETATM 1261 O HOH A 224 35.989 16.807 34.175 1.00 32.22 O HETATM 1262 O HOH A 225 44.339 9.059 1.873 1.00 33.20 O HETATM 1263 O HOH A 226 34.888 5.142 32.195 1.00 34.42 O HETATM 1264 O HOH A 227 47.278 17.912 7.135 1.00 26.19 O HETATM 1265 O HOH A 228 32.902 29.032 8.155 1.00 36.86 O HETATM 1266 O HOH A 229 49.224 34.075 18.497 1.00 37.29 O HETATM 1267 O HOH A 230 30.201 23.409 11.489 1.00 38.82 O HETATM 1268 O HOH A 231 44.770 7.119 6.305 1.00 33.86 O HETATM 1269 O HOH A 232 43.533 7.867 15.413 1.00 30.99 O HETATM 1270 O HOH A 233 31.806 11.841 22.426 1.00 28.45 O HETATM 1271 O HOH A 234 33.569 27.765 27.503 1.00 41.42 O HETATM 1272 O HOH A 235 33.613 26.307 23.845 1.00 32.86 O HETATM 1273 O HOH A 236 33.172 0.953 12.693 1.00 38.68 O HETATM 1274 O HOH A 237 49.424 31.993 14.722 1.00 38.17 O HETATM 1275 O HOH A 238 40.873 36.071 25.505 1.00 45.72 O HETATM 1276 O HOH A 239 39.644 10.218 31.136 1.00 42.95 O HETATM 1277 O HOH A 240 18.034 21.131 24.400 1.00 41.06 O HETATM 1278 O HOH A 241 34.898 9.618 37.100 1.00 35.94 O HETATM 1279 O HOH A 242 47.125 34.024 20.528 1.00 30.48 O HETATM 1280 O HOH A 243 24.978 -0.601 12.505 1.00 38.86 O HETATM 1281 O HOH A 244 29.227 19.270 2.183 1.00 40.25 O HETATM 1282 O HOH A 245 32.170 25.915 11.636 1.00 29.61 O HETATM 1283 O HOH A 246 39.717 29.238 31.854 1.00 42.54 O HETATM 1284 O HOH A 247 45.537 35.837 19.593 1.00 39.38 O HETATM 1285 O HOH A 248 29.694 27.754 11.185 1.00 42.86 O HETATM 1286 O HOH A 249 48.419 34.858 22.611 1.00 39.53 O HETATM 1287 O HOH A 250 35.874 27.173 23.491 1.00 42.54 O HETATM 1288 O HOH A 251 27.401 18.073 14.406 1.00 46.18 O HETATM 1289 O HOH A 252 43.298 13.985 31.915 1.00 51.34 O HETATM 1290 O HOH A 253 41.333 12.108 31.217 1.00 48.26 O HETATM 1291 O HOH A 254 27.393 30.078 10.264 1.00 42.84 O HETATM 1292 O HOH A 255 29.269 16.459 1.131 1.00 45.01 O HETATM 1293 O HOH A 256 29.477 4.545 19.208 1.00 37.16 O HETATM 1294 O HOH A 257 28.529 15.328 23.874 1.00 34.36 O HETATM 1295 O HOH A 258 44.471 31.378 27.643 1.00 47.27 O HETATM 1296 O HOH A 259 30.478 2.629 30.512 1.00 44.39 O HETATM 1297 O HOH A 260 44.694 12.704 15.619 1.00 34.62 O HETATM 1298 O HOH A 261 50.454 17.702 8.543 1.00 43.56 O HETATM 1299 O HOH A 262 37.712 15.664 -1.293 1.00 45.13 O HETATM 1300 O HOH A 263 26.872 11.300 16.284 1.00 36.53 O HETATM 1301 O HOH A 264 26.121 13.522 24.642 1.00 52.52 O HETATM 1302 O HOH A 265 38.837 15.987 33.031 1.00 41.54 O HETATM 1303 O HOH A 266 36.627 18.664 0.767 1.00 40.12 O HETATM 1304 O HOH A 267 34.923 5.697 23.633 1.00 44.48 O HETATM 1305 O HOH A 268 33.376 19.304 40.554 1.00 40.39 O HETATM 1306 O HOH A 269 37.161 3.796 24.713 1.00 47.63 O HETATM 1307 O HOH A 270 48.751 24.288 9.862 1.00 36.36 O HETATM 1308 O HOH A 271 28.843 22.247 6.393 1.00 44.10 O HETATM 1309 O HOH A 272 33.345 21.991 36.725 1.00 39.48 O HETATM 1310 O HOH A 273 39.387 4.921 2.624 1.00 42.81 O HETATM 1311 O HOH A 274 15.845 5.507 36.262 1.00 49.74 O HETATM 1312 O HOH A 275 46.234 23.218 22.246 1.00 46.87 O HETATM 1313 O HOH A 276 16.597 16.567 8.701 1.00 45.09 O HETATM 1314 O HOH A 277 44.641 14.341 12.797 1.00 28.66 O HETATM 1315 O HOH A 278 24.720 30.147 35.405 1.00 43.52 O HETATM 1316 O HOH A 279 39.836 8.369 34.454 1.00 54.94 O HETATM 1317 O HOH A 280 24.164 8.558 29.830 1.00 49.89 O HETATM 1318 O HOH A 281 39.497 19.827 35.075 1.00 51.96 O HETATM 1319 O HOH A 282 28.226 20.349 -0.122 1.00 46.09 O HETATM 1320 O HOH A 283 36.867 1.657 14.744 1.00 44.44 O HETATM 1321 O HOH A 284 21.869 16.569 3.830 1.00 46.59 O HETATM 1322 O HOH A 285 15.329 14.872 10.553 1.00 49.66 O HETATM 1323 O HOH A 286 39.921 4.492 28.577 1.00 43.99 O HETATM 1324 O HOH A 287 37.139 30.872 6.465 1.00 32.03 O HETATM 1325 O HOH A 288 49.983 8.898 9.777 1.00 39.46 O HETATM 1326 O HOH A 289 42.897 29.209 29.389 1.00 47.36 O HETATM 1327 O HOH A 290 25.269 26.188 37.242 1.00 56.98 O HETATM 1328 O HOH A 291 49.397 11.467 19.985 1.00 36.67 O HETATM 1329 O HOH A 292 27.471 23.451 36.521 1.00 42.00 O HETATM 1330 O HOH A 293 32.622 5.802 17.554 1.00 46.48 O HETATM 1331 O HOH A 294 45.320 4.344 6.920 1.00 42.79 O HETATM 1332 O HOH A 295 46.314 2.617 5.116 1.00 56.97 O HETATM 1333 O HOH A 296 34.696 5.679 34.598 1.00 37.01 O HETATM 1334 O HOH A 297 46.703 10.730 1.223 1.00 41.01 O HETATM 1335 O HOH A 298 28.397 13.204 19.705 1.00 46.29 O HETATM 1336 O HOH A 299 46.939 19.244 3.872 1.00 56.55 O HETATM 1337 O HOH A 300 21.576 16.921 1.139 1.00 50.35 O HETATM 1338 O HOH A 301 43.503 17.665 -3.887 1.00 62.49 O HETATM 1339 O HOH A 302 42.734 7.990 -0.531 1.00 40.03 O HETATM 1340 O HOH A 303 38.132 33.561 5.584 1.00 39.70 O HETATM 1341 O HOH A 304 40.728 25.989 0.357 1.00 38.26 O HETATM 1342 O HOH A 305 24.946 2.262 17.416 1.00 35.17 O HETATM 1343 O HOH A 306 23.200 1.087 14.495 1.00 46.76 O HETATM 1344 O HOH A 307 26.743 20.740 35.329 1.00 32.48 O HETATM 1345 O HOH A 308 14.312 8.437 10.248 1.00 48.90 O HETATM 1346 O HOH A 309 22.933 20.429 2.097 1.00 51.11 O HETATM 1347 O HOH A 310 14.887 18.069 7.025 1.00 51.37 O HETATM 1348 O HOH A 311 30.342 5.808 22.816 1.00 56.58 O HETATM 1349 O HOH A 312 22.682 24.340 31.749 1.00 45.18 O HETATM 1350 O HOH A 313 45.716 4.070 9.484 1.00 55.62 O HETATM 1351 O HOH A 314 41.916 5.301 25.236 1.00 46.29 O HETATM 1352 O HOH A 315 48.128 11.684 25.991 1.00 50.67 O HETATM 1353 O HOH A 316 53.911 9.599 16.042 1.00 53.14 O HETATM 1354 O HOH A 317 47.015 14.959 -2.679 1.00 44.43 O HETATM 1355 O HOH A 318 41.725 20.376 -6.332 1.00 48.18 O HETATM 1356 O HOH A 319 27.054 27.054 19.649 0.50 55.53 O HETATM 1357 O HOH A 320 23.858 23.957 23.342 1.00 52.39 O HETATM 1358 O HOH A 321 49.724 26.875 15.190 1.00 42.78 O HETATM 1359 O HOH A 322 45.751 36.115 13.411 1.00 49.27 O HETATM 1360 O HOH A 323 47.693 34.898 14.168 1.00 50.26 O HETATM 1361 O HOH A 324 29.529 9.905 2.448 1.00 63.38 O HETATM 1362 O HOH A 325 48.942 6.782 23.865 1.00 45.31 O HETATM 1363 O HOH A 326 33.957 24.117 28.920 1.00 41.33 O HETATM 1364 O HOH A 327 31.315 21.284 19.735 1.00 23.85 O MASTER 364 0 0 8 5 0 0 6 1363 1 0 13 END