/
testParserPdbAnisou.js
644 lines (638 loc) · 49.6 KB
/
testParserPdbAnisou.js
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viewer = $3Dmol.createViewer("#gldiv");
var data = $("#pdbData").val();
//console.log(data);
viewer.setBackgroundColor(0xffffff);
viewer.addModel(data, "pdb");
viewer.zoomTo();
viewer.render();
var model = viewer.getModel();
var atoms = model.selectedAtoms();
var html = "";
for (var i = 0; i < atoms.length; i++) {
var a = atoms[i];
if ("uMat" in a) {
html += a.serial + " " + JSON.stringify(a["uMat"]) + "<br/>";
}
}
$("#loadAnisouResultDiv").html(html);
console.log(atoms[0]);
/* @data
HEADER ISOMERASE 25-FEB-14 4POC
TITLE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE WILD TYPE HUMAN ENZYME.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TIM, TRIOSE-PHOSPHATE ISOMERASE;
COMPND 5 EC: 5.3.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TPI, TPI1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+RILP;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PLC3
KEYWDS TIM ALPHA/BETA BARREL, TIM BARREL, ISOMERASE, GLYCOLYTIC
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.AMRICH,A.A.ASLAM,A.HEROUX,A.P.VANDEMARK
REVDAT 1 14-JAN-15 4POC 0
JRNL AUTH B.P.ROLAND,C.G.AMRICH,C.J.KAMMERER,K.A.STUCHUL,S.B.LARSEN,
JRNL AUTH 2 S.RODE,A.A.ASLAM,A.HEROUX,R.WETZEL,A.P.VANDEMARK,
JRNL AUTH 3 M.J.PALLADINO
JRNL TITL TRIOSEPHOSPHATE ISOMERASE I170V ALTERS CATALYTIC SITE,
JRNL TITL 2 ENHANCES STABILITY AND INDUCES PATHOLOGY IN A DROSOPHILA
JRNL TITL 3 MODEL OF TPI DEFICIENCY.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1852 61 2015
JRNL REFN ISSN 0006-3002
JRNL PMID 25463631
JRNL DOI 10.1016/J.BBADIS.2014.10.010
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 52340
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 2695
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.5840 - 4.2713 0.99 2859 153 0.1558 0.1716
REMARK 3 2 4.2713 - 3.3906 0.99 2793 145 0.1393 0.1563
REMARK 3 3 3.3906 - 2.9620 0.99 2783 154 0.1523 0.1960
REMARK 3 4 2.9620 - 2.6913 1.00 2816 150 0.1524 0.1852
REMARK 3 5 2.6913 - 2.4984 1.00 2771 163 0.1530 0.2025
REMARK 3 6 2.4984 - 2.3511 1.00 2784 145 0.1501 0.2088
REMARK 3 7 2.3511 - 2.2333 1.00 2826 121 0.1433 0.1765
REMARK 3 8 2.2333 - 2.1361 1.00 2763 164 0.1438 0.1789
REMARK 3 9 2.1361 - 2.0539 1.00 2766 167 0.1609 0.2152
REMARK 3 10 2.0539 - 1.9830 1.00 2773 165 0.1594 0.1842
REMARK 3 11 1.9830 - 1.9210 1.00 2766 137 0.1560 0.2126
REMARK 3 12 1.9210 - 1.8661 1.00 2797 146 0.1530 0.2058
REMARK 3 13 1.8661 - 1.8170 1.00 2788 142 0.1592 0.2306
REMARK 3 14 1.8170 - 1.7726 1.00 2782 137 0.1706 0.2331
REMARK 3 15 1.7726 - 1.7323 1.00 2766 156 0.1737 0.2026
REMARK 3 16 1.7323 - 1.6955 0.91 2479 144 0.1808 0.2305
REMARK 3 17 1.6955 - 1.6615 0.76 2097 134 0.1960 0.2225
REMARK 3 18 1.6615 - 1.6302 0.64 1747 104 0.2237 0.2766
REMARK 3 19 1.6302 - 1.6011 0.53 1489 68 0.2425 0.3406
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 3792
REMARK 3 ANGLE : 0.962 5137
REMARK 3 CHIRALITY : 0.052 581
REMARK 3 PLANARITY : 0.004 665
REMARK 3 DIHEDRAL : 15.111 1374
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4POC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB085018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI-111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52380
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.44200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2JK2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG 2000 MME, 0.05 KBR, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 24.42550
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 Gly A -5
REMARK 465 ASP A -4
REMARK 465 Ile A -3
REMARK 465 Thr A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 Ala A 1
REMARK 465 PRO A 2
REMARK 465 Gly B -5
REMARK 465 ASP B -4
REMARK 465 Ile B -3
REMARK 465 Thr B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 Ala B 1
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 LYS A 13 -149.26 54.18
REMARK 500 VAL A 196 -79.68 -121.56
REMARK 500 LYS A 247 69.58 -101.29
REMARK 500 LYS B 13 -144.72 50.47
REMARK 500 LYS B 32 78.16 52.07
REMARK 500 VAL B 196 -79.01 -115.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 302 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 223 O
REMARK 620 2 VAL B 226 O 82.2
REMARK 620 3 Ala B 221 O 86.3 89.8
REMARK 620 4 HOH B 440 O 76.1 158.4 89.6
REMARK 620 5 HOH B 462 O 130.6 60.1 64.6 137.5
REMARK 620 6 HOH B 503 O 144.2 129.8 106.5 70.8 84.3
REMARK 620 7 HOH B 493 O 114.5 75.3 151.8 113.0 87.2 68.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 301 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 226 O
REMARK 620 2 GLN A 223 O 82.4
REMARK 620 3 Ala A 221 O 94.1 82.8
REMARK 620 4 HOH A 519 O 75.0 121.7 150.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 174 O
REMARK 620 2 HOH A 497 O 125.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BR B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4POD RELATED DB: PDB
REMARK 900 STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE I170V MUTANT HUMAN
REMARK 900 ENZYME.
DBREF 4POC A 0 248 UNP P60174 TPIS_HUMAN 38 286
DBREF 4POC B 0 248 UNP P60174 TPIS_HUMAN 38 286
SEQADV 4POC Gly A -5 UNP P60174 EXPRESSION TAG
SEQADV 4POC ASP A -4 UNP P60174 EXPRESSION TAG
SEQADV 4POC Ile A -3 UNP P60174 EXPRESSION TAG
SEQADV 4POC Thr A -2 UNP P60174 EXPRESSION TAG
SEQADV 4POC HIS A -1 UNP P60174 EXPRESSION TAG
SEQADV 4POC Gly B -5 UNP P60174 EXPRESSION TAG
SEQADV 4POC ASP B -4 UNP P60174 EXPRESSION TAG
SEQADV 4POC Ile B -3 UNP P60174 EXPRESSION TAG
SEQADV 4POC Thr B -2 UNP P60174 EXPRESSION TAG
SEQADV 4POC HIS B -1 UNP P60174 EXPRESSION TAG
SEQRES 1 A 254 Gly ASP Ile Thr HIS MET Ala PRO SER ARG LYS Phe PHE
SEQRES 2 A 254 VAL Gly GLY ASN TRP LYS MET ASN Gly ARG LYS GLN SER
SEQRES 3 A 254 LEU Gly Glu LEU Ile Gly Thr LEU ASN Ala ALA LYS VAL
SEQRES 4 A 254 PRO Ala ASP Thr Glu VAL VAL CYS Ala PRO PRO Thr Ala
SEQRES 5 A 254 TYR Ile ASP Phe Ala ARG GLN LYS LEU ASP PRO LYS Ile
SEQRES 6 A 254 Ala VAL Ala ALA GLN ASN CYS TYR LYS VAL Thr ASN Gly
SEQRES 7 A 254 Ala Phe Thr Gly Glu Ile SER PRO Gly MET Ile LYS ASP
SEQRES 8 A 254 CYS Gly Ala Thr TRP VAL VAL LEU Gly HIS SER Glu ARG
SEQRES 9 A 254 ARG HIS VAL Phe Gly Glu SER ASP Glu LEU Ile Gly GLN
SEQRES 10 A 254 LYS VAL Ala HIS Ala LEU Ala Glu Gly LEU Gly VAL Ile
SEQRES 11 A 254 Ala CYS Ile Gly Glu LYS LEU ASP Glu ARG Glu Ala Gly
SEQRES 12 A 254 Ile Thr Glu LYS VAL VAL Phe Glu GLN Thr LYS VAL Ile
SEQRES 13 A 254 Ala ASP ASN VAL LYS ASP TRP SER LYS VAL VAL LEU Ala
SEQRES 14 A 254 TYR Glu PRO VAL TRP Ala Ile Gly Thr Gly LYS Thr Ala
SEQRES 15 A 254 Thr PRO GLN GLN Ala GLN Glu VAL HIS Glu LYS LEU ARG
SEQRES 16 A 254 Gly TRP LEU LYS SER ASN VAL SER ASP Ala VAL Ala GLN
SEQRES 17 A 254 SER Thr ARG Ile ILE TYR Gly GLY SER VAL Thr Gly Ala
SEQRES 18 A 254 Thr CYS LYS Glu LEU Ala SER GLN PRO ASP VAL ASP Gly
SEQRES 19 A 254 Phe LEU VAL Gly GLY Ala SER LEU LYS PRO Glu Phe VAL
SEQRES 20 A 254 ASP Ile ILE ASN Ala LYS GLN
SEQRES 1 B 254 Gly ASP Ile Thr HIS MET Ala PRO SER ARG LYS Phe PHE
SEQRES 2 B 254 VAL Gly GLY ASN TRP LYS MET ASN Gly ARG LYS GLN SER
SEQRES 3 B 254 LEU Gly Glu LEU Ile Gly Thr LEU ASN Ala ALA LYS VAL
SEQRES 4 B 254 PRO Ala ASP Thr Glu VAL VAL CYS Ala PRO PRO Thr Ala
SEQRES 5 B 254 TYR Ile ASP Phe Ala ARG GLN LYS LEU ASP PRO LYS Ile
SEQRES 6 B 254 Ala VAL Ala ALA GLN ASN CYS TYR LYS VAL Thr ASN Gly
SEQRES 7 B 254 Ala Phe Thr Gly Glu Ile SER PRO Gly MET Ile LYS ASP
SEQRES 8 B 254 CYS Gly Ala Thr TRP VAL VAL LEU Gly HIS SER Glu ARG
SEQRES 9 B 254 ARG HIS VAL Phe Gly Glu SER ASP Glu LEU Ile Gly GLN
SEQRES 10 B 254 LYS VAL Ala HIS Ala LEU Ala Glu Gly LEU Gly VAL Ile
SEQRES 11 B 254 Ala CYS Ile Gly Glu LYS LEU ASP Glu ARG Glu Ala Gly
SEQRES 12 B 254 Ile Thr Glu LYS VAL VAL Phe Glu GLN Thr LYS VAL Ile
SEQRES 13 B 254 Ala ASP ASN VAL LYS ASP TRP SER LYS VAL VAL LEU Ala
SEQRES 14 B 254 TYR Glu PRO VAL TRP Ala Ile Gly Thr Gly LYS Thr Ala
SEQRES 15 B 254 Thr PRO GLN GLN Ala GLN Glu VAL HIS Glu LYS LEU ARG
SEQRES 16 B 254 Gly TRP LEU LYS SER ASN VAL SER ASP Ala VAL Ala GLN
SEQRES 17 B 254 SER Thr ARG Ile ILE TYR Gly GLY SER VAL Thr Gly Ala
SEQRES 18 B 254 Thr CYS LYS Glu LEU Ala SER GLN PRO ASP VAL ASP Gly
SEQRES 19 B 254 Phe LEU VAL Gly GLY Ala SER LEU LYS PRO Glu Phe VAL
SEQRES 20 B 254 ASP Ile ILE ASN Ala LYS GLN
HET K A 301 1
HET NA A 302 1
HET BR A 303 1
HET PO4 B 301 5
HET K B 302 1
HET BR B 303 1
HETNAM K POTASSIUM ION
HETNAM NA SODIUM ION
HETNAM BR BROMIDE ION
HETNAM PO4 PHOSPHATE ION
FORMUL 3 K 2(K 1+)
FORMUL 4 NA NA 1+
FORMUL 5 BR 2(BR 1-)
FORMUL 6 PO4 O4 P 3-
FORMUL 9 HOH *327(H2 O)
HELIX 1 1 ARG A 17 Ala A 31 1 15
HELIX 2 2 PRO A 44 Ala A 46 5 3
HELIX 3 3 TYR A 47 LEU A 55 1 9
HELIX 4 4 SER A 79 CYS A 86 1 8
HELIX 5 5 HIS A 95 VAL A 101 1 7
HELIX 6 6 SER A 105 Glu A 119 1 15
HELIX 7 7 LYS A 130 Ala A 136 1 7
HELIX 8 8 Ile A 138 ASP A 152 1 15
HELIX 9 9 ASP A 156 SER A 158 5 3
HELIX 10 10 PRO A 166 Ile A 170 5 5
HELIX 11 11 Thr A 177 VAL A 196 1 20
HELIX 12 12 SER A 197 Thr A 204 1 8
HELIX 13 13 Thr A 216 SER A 222 1 7
HELIX 14 14 Gly A 232 PRO A 238 5 7
HELIX 15 15 Glu A 239 ASN A 245 1 7
HELIX 16 16 ARG B 17 Ala B 31 1 15
HELIX 17 17 PRO B 44 Ala B 46 5 3
HELIX 18 18 TYR B 47 LEU B 55 1 9
HELIX 19 19 SER B 79 CYS B 86 1 8
HELIX 20 20 HIS B 95 VAL B 101 1 7
HELIX 21 21 SER B 105 Glu B 119 1 15
HELIX 22 22 LYS B 130 Gly B 137 1 8
HELIX 23 23 Ile B 138 ASP B 152 1 15
HELIX 24 24 ASP B 156 SER B 158 5 3
HELIX 25 25 PRO B 166 Ile B 170 5 5
HELIX 26 26 Thr B 177 VAL B 196 1 20
HELIX 27 27 SER B 197 Thr B 204 1 8
HELIX 28 28 Thr B 216 SER B 222 1 7
HELIX 29 29 Gly B 232 LYS B 237 5 6
HELIX 30 30 PRO B 238 ASN B 245 1 8
SHEET 1 A 9 Phe A 6 ASN A 11 0
SHEET 2 A 9 Thr A 37 Ala A 42 1 O Ala A 42 N Gly A 10
SHEET 3 A 9 Ala A 60 Ala A 63 1 O Ala A 62 N CYS A 41
SHEET 4 A 9 TRP A 90 LEU A 93 1 O VAL A 92 N Ala A 63
SHEET 5 A 9 Gly A 122 Ile A 127 1 O CYS A 126 N LEU A 93
SHEET 6 A 9 VAL A 160 TYR A 164 1 O VAL A 161 N Ala A 125
SHEET 7 A 9 Ile A 206 TYR A 208 1 O Ile A 207 N LEU A 162
SHEET 8 A 9 Gly A 228 VAL A 231 1 O Gly A 228 N TYR A 208
SHEET 9 A 9 Phe A 6 ASN A 11 1 N Gly A 9 O VAL A 231
SHEET 1 B 9 Phe B 6 ASN B 11 0
SHEET 2 B 9 Thr B 37 Ala B 42 1 O Ala B 42 N Gly B 10
SHEET 3 B 9 Ala B 60 Ala B 63 1 O Ala B 62 N CYS B 41
SHEET 4 B 9 TRP B 90 LEU B 93 1 O VAL B 92 N Ala B 63
SHEET 5 B 9 Gly B 122 Ile B 127 1 O CYS B 126 N LEU B 93
SHEET 6 B 9 VAL B 160 TYR B 164 1 O Ala B 163 N Ala B 125
SHEET 7 B 9 Ile B 206 Gly B 209 1 O Ile B 207 N TYR B 164
SHEET 8 B 9 Gly B 228 VAL B 231 1 O Gly B 228 N TYR B 208
SHEET 9 B 9 Phe B 6 ASN B 11 1 N Gly B 9 O VAL B 231
LINK O GLN B 223 K K B 302 1555 1555 2.61
LINK O VAL A 226 K K A 301 1555 1555 2.62
LINK O GLN A 223 K K A 301 1555 1555 2.64
LINK O VAL B 226 K K B 302 1555 1555 2.71
LINK O Ala A 221 K K A 301 1555 1555 2.82
LINK O Ala B 221 K K B 302 1555 1555 2.83
LINK O LYS A 174 NA NA A 302 1555 1555 2.93
LINK K K B 302 O HOH B 440 1555 1555 2.74
LINK K K B 302 O HOH B 462 1555 1555 2.77
LINK K K B 302 O HOH B 503 1555 1555 2.79
LINK K K B 302 O HOH B 493 1555 1555 2.85
LINK K K A 301 O HOH A 519 1555 1555 2.92
LINK NA NA A 302 O HOH A 497 1555 1555 3.14
SITE 1 AC1 4 Ala A 221 GLN A 223 VAL A 226 HOH A 519
SITE 1 AC2 6 Ala A 169 Gly A 171 Thr A 172 Gly A 173
SITE 2 AC2 6 LYS A 174 HOH B 444
SITE 1 AC3 3 ASN A 71 Thr A 175 HOH A 557
SITE 1 AC4 13 LYS B 13 Ala B 169 Ile B 170 Gly B 171
SITE 2 AC4 13 Gly B 210 SER B 211 Gly B 232 Gly B 233
SITE 3 AC4 13 BR B 303 HOH B 409 HOH B 411 HOH B 477
SITE 4 AC4 13 HOH B 481
SITE 1 AC5 7 Ala B 221 GLN B 223 VAL B 226 HOH B 440
SITE 2 AC5 7 HOH B 462 HOH B 493 HOH B 503
SITE 1 AC6 4 ASN B 11 HIS B 95 Glu B 165 PO4 B 301
CRYST1 47.920 48.851 93.966 90.00 103.66 90.00 P 1 21 1 4
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 0.020868 0.000000 0.005072 0.00000
SCALE2 0.000000 0.020470 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010952 0.00000
ATOM 1073 N Ala A 73 9.852 9.388 28.674 1.00 26.13 N
ANISOU 1073 N Ala A 73 3187 3304 3438 390 -712 -860 N
ATOM 1074 CA Ala A 73 10.962 9.067 29.557 1.00 25.93 C
ANISOU 1074 CA Ala A 73 2965 3468 3419 300 -938 -709 C
ATOM 1075 C Ala A 73 11.092 7.560 29.682 1.00 27.19 C
ANISOU 1075 C Ala A 73 3217 3692 3420 450 -771 -594 C
ATOM 1076 O Ala A 73 10.783 6.978 30.727 1.00 29.60 O
ANISOU 1076 O Ala A 73 3747 3949 3550 530 -699 -804 O
ATOM 1077 CB Ala A 73 10.741 9.706 30.925 1.00 26.85 C
ANISOU 1077 CB Ala A 73 2975 3659 3569 115 -1011 -679 C
ATOM 1078 H Ala A 73 9.118 9.542 29.094 1.00 31.36 H
ATOM 1079 HA Ala A 73 11.785 9.418 29.183 1.00 31.11 H
ATOM 1080 HB1 Ala A 73 11.488 9.482 31.501 1.00 32.22 H
ATOM 1081 HB2 Ala A 73 10.680 10.668 30.818 1.00 32.22 H
ATOM 1082 HB3 Ala A 73 9.916 9.362 31.303 1.00 32.22 H
ATOM 1083 N Phe A 74 11.541 6.937 28.596 1.00 26.02 N
ANISOU 1083 N Phe A 74 3013 3549 3325 220 -783 -519 N
ATOM 1084 CA Phe A 74 11.684 5.491 28.529 1.00 23.58 C
ANISOU 1084 CA Phe A 74 2538 3259 3163 400 -909 -535 C
ATOM 1085 C Phe A 74 13.062 5.158 27.985 1.00 22.97 C
ANISOU 1085 C Phe A 74 2654 3206 2866 446 -1019 -492 C
ATOM 1086 O Phe A 74 13.235 4.752 26.840 1.00 22.87 O
ANISOU 1086 O Phe A 74 2461 3347 2880 464 -1067 -622 O
ATOM 1087 CB Phe A 74 10.536 4.898 27.709 1.00 23.69 C
ANISOU 1087 CB Phe A 74 2385 3266 3349 44 -925 -612 C
ATOM 1088 CG Phe A 74 9.192 5.238 28.276 1.00 26.78 C
ANISOU 1088 CG Phe A 74 2950 3708 3519 -253 -681 -667 C
ATOM 1089 CD1 Phe A 74 8.744 4.627 29.435 1.00 28.21 C
ANISOU 1089 CD1 Phe A 74 2891 4302 3527 -118 -736 -454 C
ATOM 1090 CD2 Phe A 74 8.401 6.207 27.690 1.00 27.10 C
ANISOU 1090 CD2 Phe A 74 2757 3955 3586 -200 -833 -682 C
ATOM 1091 CE1 Phe A 74 7.522 4.958 29.978 1.00 28.51 C
ANISOU 1091 CE1 Phe A 74 2755 4529 3549 -356 -867 -479 C
ATOM 1092 CE2 Phe A 74 7.179 6.543 28.235 1.00 26.68 C
ANISOU 1092 CE2 Phe A 74 2453 4046 3637 -223 -889 -579 C
ATOM 1093 CZ Phe A 74 6.745 5.920 29.383 1.00 27.06 C
ANISOU 1093 CZ Phe A 74 2345 4262 3675 -367 -908 -636 C
ATOM 1094 H Phe A 74 11.773 7.340 27.873 1.00 31.23 H
ATOM 1095 HA Phe A 74 11.625 5.128 29.426 1.00 28.30 H
ATOM 1096 HB2 Phe A 74 10.579 5.247 26.805 1.00 28.42 H
ATOM 1097 HB3 Phe A 74 10.622 3.932 27.697 1.00 28.42 H
ATOM 1098 HD1 Phe A 74 9.270 3.980 29.846 1.00 33.86 H
ATOM 1099 HD2 Phe A 74 8.694 6.635 26.918 1.00 32.53 H
ATOM 1100 HE1 Phe A 74 7.227 4.536 30.753 1.00 34.22 H
ATOM 1101 HE2 Phe A 74 6.650 7.190 27.828 1.00 32.01 H
ATOM 1102 HZ Phe A 74 5.917 6.138 29.745 1.00 32.47 H
ATOM 1103 N Thr A 75 14.045 5.370 28.854 1.00 21.37 N
ANISOU 1103 N Thr A 75 2545 2922 2651 219 -1096 -676 N
ATOM 1104 CA Thr A 75 15.434 5.077 28.564 1.00 21.59 C
ANISOU 1104 CA Thr A 75 2697 3009 2499 40 -1041 -447 C
ATOM 1105 C Thr A 75 15.532 3.673 27.995 1.00 21.56 C
ANISOU 1105 C Thr A 75 3028 2693 2469 -68 -922 -280 C
ATOM 1106 O Thr A 75 14.984 2.730 28.570 1.00 22.34 O
ANISOU 1106 O Thr A 75 3232 2894 2362 -134 -1005 6 O
ATOM 1107 CB Thr A 75 16.261 5.184 29.859 1.00 22.01 C
ANISOU 1107 CB Thr A 75 2774 3073 2515 -75 -940 -516 C
ATOM 1108 OG1 Thr A 75 16.178 6.525 30.361 1.00 22.88 O
ANISOU 1108 OG1 Thr A 75 2669 3181 2844 -67 -999 -341 O
ATOM 1109 CG2 Thr A 75 17.711 4.840 29.627 1.00 23.32 C
ANISOU 1109 CG2 Thr A 75 3048 3329 2483 3 -620 -527 C
ATOM 1110 H Thr A 75 13.923 5.693 29.641 1.00 25.64 H
ATOM 1111 HA Thr A 75 15.779 5.708 27.913 1.00 25.91 H
ATOM 1112 HB Thr A 75 15.904 4.571 30.520 1.00 26.41 H
ATOM 1113 HG1 Thr A 75 15.378 6.721 30.525 1.00 27.46 H
ATOM 1114 HG21 Thr A 75 18.206 4.916 30.458 1.00 27.98 H
ATOM 1115 HG22 Thr A 75 17.787 3.932 29.297 1.00 27.98 H
ATOM 1116 HG23 Thr A 75 18.095 5.447 28.975 1.00 27.98 H
ATOM 1117 N Gly A 76 16.183 3.555 26.839 1.00 20.82 N
ANISOU 1117 N Gly A 76 2890 2528 2493 -283 -948 -386 N
ATOM 1118 CA Gly A 76 16.417 2.267 26.209 1.00 21.52 C
ANISOU 1118 CA Gly A 76 2887 2716 2573 -135 -945 -319 C
ATOM 1119 C Gly A 76 15.364 1.827 25.199 1.00 20.76 C
ANISOU 1119 C Gly A 76 2473 2795 2620 -136 -996 -443 C
ATOM 1120 O Gly A 76 15.506 0.767 24.588 1.00 21.88 O
ANISOU 1120 O Gly A 76 2407 3199 2709 319 -996 -497 O
ATOM 1121 H Gly A 76 16.502 4.220 26.397 1.00 24.98 H
ATOM 1122 HA2 Gly A 76 17.272 2.294 25.752 1.00 25.82 H
ATOM 1123 HA3 Gly A 76 16.468 1.587 26.898 1.00 25.82 H
ATOM 1124 N Glu A 77 14.314 2.627 25.017 1.00 20.38 N
ANISOU 1124 N Glu A 77 2274 2789 2680 -29 -932 -370 N
ATOM 1125 CA Glu A 77 13.250 2.296 24.058 1.00 20.85 C
ANISOU 1125 CA Glu A 77 2267 2914 2741 308 -1152 -278 C
ATOM 1126 C Glu A 77 13.303 3.173 22.816 1.00 21.36 C
ANISOU 1126 C Glu A 77 2608 2655 2851 356 -1201 -248 C
ATOM 1127 O Glu A 77 13.968 4.209 22.802 1.00 21.76 O
ANISOU 1127 O Glu A 77 2862 2658 2750 27 -1328 -180 O
ATOM 1128 CB Glu A 77 11.868 2.470 24.701 1.00 23.44 C
ANISOU 1128 CB Glu A 77 2710 3344 2854 261 -929 -377 C
ATOM 1129 CG Glu A 77 11.656 1.620 25.940 1.00 24.69 C
ANISOU 1129 CG Glu A 77 2767 3655 2958 130 -836 -321 C
ATOM 1130 CD Glu A 77 11.643 0.145 25.620 1.00 25.80 C
ANISOU 1130 CD Glu A 77 3031 3781 2990 -166 -930 -288 C
ATOM 1131 OE1 Glu A 77 10.846 -0.259 24.739 1.00 27.63 O
ANISOU 1131 OE1 Glu A 77 3536 3791 3173 -241 -928 -217 O
ATOM 1132 OE2 Glu A 77 12.427 -0.609 26.239 1.00 25.79 O
ANISOU 1132 OE2 Glu A 77 3043 3826 2932 0 -929 -323 O
ATOM 1133 H Glu A 77 14.191 3.369 25.434 1.00 24.45 H
ATOM 1134 HA Glu A 77 13.344 1.370 23.782 1.00 25.02 H
ATOM 1135 HB2 Glu A 77 11.758 3.399 24.956 1.00 28.13 H
ATOM 1136 HB3 Glu A 77 11.190 2.224 24.053 1.00 28.13 H
ATOM 1137 HG2 Glu A 77 12.376 1.786 26.567 1.00 29.62 H
ATOM 1138 HG3 Glu A 77 10.803 1.849 26.341 1.00 29.62 H
ATOM 1139 N Ile A 78 12.606 2.735 21.770 1.00 20.06 N
ANISOU 1139 N Ile A 78 2488 2313 2820 599 -1487 -220 N
ATOM 1140 CA Ile A 78 12.384 3.553 20.579 1.00 20.59 C
ANISOU 1140 CA Ile A 78 2436 2494 2895 297 -1526 -263 C
ATOM 1141 C Ile A 78 10.902 3.545 20.209 1.00 22.20 C
ANISOU 1141 C Ile A 78 2601 2819 3016 402 -1357 -200 C
ATOM 1142 O Ile A 78 10.180 2.608 20.539 1.00 23.69 O
ANISOU 1142 O Ile A 78 2405 3421 3177 660 -1010 -242 O
ATOM 1143 CB Ile A 78 13.219 3.068 19.369 1.00 23.39 C
ANISOU 1143 CB Ile A 78 2838 2890 3159 600 -954 -141 C
ATOM 1144 CG1 Ile A 78 12.812 1.654 18.927 1.00 23.81 C
ANISOU 1144 CG1 Ile A 78 2646 3145 3256 564 -1052 -550 C
ATOM 1145 CG2 Ile A 78 14.721 3.134 19.690 1.00 22.80 C
ANISOU 1145 CG2 Ile A 78 2890 2822 2950 835 -1169 224 C
ATOM 1146 CD1 Ile A 78 13.346 1.276 17.558 1.00 24.35 C
ANISOU 1146 CD1 Ile A 78 2771 3262 3219 453 -1424 -569 C
ATOM 1147 H Ile A 78 12.247 1.955 21.724 1.00 24.07 H
ATOM 1148 HA Ile A 78 12.640 4.468 20.773 1.00 24.71 H
ATOM 1149 HB Ile A 78 13.047 3.671 18.629 1.00 28.07 H
ATOM 1150 HG12 Ile A 78 13.156 1.013 19.569 1.00 28.58 H
ATOM 1151 HG13 Ile A 78 11.844 1.601 18.895 1.00 28.58 H
ATOM 1152 HG21 Ile A 78 15.222 2.826 18.919 1.00 27.36 H
ATOM 1153 HG22 Ile A 78 14.959 4.052 19.895 1.00 27.36 H
ATOM 1154 HG23 Ile A 78 14.905 2.565 20.454 1.00 27.36 H
ATOM 1155 HD11 Ile A 78 13.053 0.377 17.343 1.00 29.22 H
ATOM 1156 HD12 Ile A 78 13.002 1.903 16.902 1.00 29.22 H
ATOM 1157 HD13 Ile A 78 14.315 1.314 17.577 1.00 29.22 H
MASTER 310 0 6 30 18 0 11 6 4056 2 22 40
END */