HEADER IMMUNE SYSTEM 25-JUN-16 5GIX
TITLE HUMAN SERUM ALBUMIN-PALMITIC ACID-FE(HN3PIT)CL2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 27-607;
COMPND 5 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: ALB, GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619,
SOURCE 6 PRO2675, UNQ696/PRO1341;
SOURCE 7 EXPRESSION_SYSTEM: PICHIA KUDRIAVZEVII;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4909
KEYWDS FERRIC COMPOUND, ANTICANCER MECHANISM, TUMOR TARGETING, THERAPEUTIC
KEYWDS 2 EFFECT, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR F.YANG,J.QI,T.WANG
REVDAT 2 08-NOV-23 5GIX 1 REMARK
REVDAT 1 19-JUL-17 5GIX 0
JRNL AUTH J.QI,Y.GOU,Y.ZHANG,K.YANG,S.CHEN,L.LIU,X.WU,T.WANG,W.ZHANG,
JRNL AUTH 2 F.YANG
JRNL TITL DEVELOPING ANTICANCER FERRIC PRODRUGS BASED ON THE N-DONOR
JRNL TITL 2 RESIDUES OF HUMAN SERUM ALBUMIN CARRIER IIA SUBDOMAIN
JRNL REF J. MED. CHEM. V. 59 7497 2016
JRNL REFN ISSN 1520-4804
JRNL PMID 27441502
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00509
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 30492
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.540
REMARK 3 FREE R VALUE TEST SET COUNT : 1994
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 27.1269 - 6.7185 0.90 1886 141 0.1553 0.2227
REMARK 3 2 6.7185 - 5.3460 0.98 2063 143 0.2087 0.2517
REMARK 3 3 5.3460 - 4.6742 0.97 2054 142 0.1815 0.2188
REMARK 3 4 4.6742 - 4.2486 0.97 2036 138 0.1806 0.2379
REMARK 3 5 4.2486 - 3.9450 0.97 2067 141 0.1884 0.2444
REMARK 3 6 3.9450 - 3.7131 0.98 2066 149 0.2130 0.3019
REMARK 3 7 3.7131 - 3.5275 0.99 2061 147 0.2225 0.2801
REMARK 3 8 3.5275 - 3.3743 0.97 2071 145 0.2431 0.3151
REMARK 3 9 3.3743 - 3.2446 0.99 2046 142 0.2504 0.2881
REMARK 3 10 3.2446 - 3.1328 0.96 2052 147 0.2667 0.3087
REMARK 3 11 3.1328 - 3.0350 0.98 2082 145 0.2675 0.3485
REMARK 3 12 3.0350 - 2.9483 0.98 2000 133 0.2627 0.3321
REMARK 3 13 2.9483 - 2.8708 0.96 2056 142 0.2715 0.2800
REMARK 3 14 2.8708 - 2.8008 0.93 1958 139 0.3055 0.4090
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 9677
REMARK 3 ANGLE : 0.668 12946
REMARK 3 CHIRALITY : 0.024 1418
REMARK 3 PLANARITY : 0.003 1666
REMARK 3 DIHEDRAL : 16.154 3718
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1382 0.2589 -1.2401
REMARK 3 T TENSOR
REMARK 3 T11: 0.2035 T22: 0.2818
REMARK 3 T33: 0.4201 T12: 0.1241
REMARK 3 T13: 0.0444 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: -0.0259 L22: 1.2767
REMARK 3 L33: 0.6405 L12: 0.1938
REMARK 3 L13: 0.0325 L23: 0.1527
REMARK 3 S TENSOR
REMARK 3 S11: 0.0247 S12: -0.0016 S13: 0.0435
REMARK 3 S21: -0.0100 S22: 0.0290 S23: -0.0179
REMARK 3 S31: -0.0758 S32: -0.0928 S33: -0.0504
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3625 -42.4950 38.5857
REMARK 3 T TENSOR
REMARK 3 T11: 0.3706 T22: 0.5186
REMARK 3 T33: 0.4626 T12: -0.0408
REMARK 3 T13: -0.0444 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: -0.2492 L22: 1.0245
REMARK 3 L33: 1.0740 L12: 0.0809
REMARK 3 L13: -0.3605 L23: 0.0417
REMARK 3 S TENSOR
REMARK 3 S11: -0.0539 S12: -0.0368 S13: -0.0302
REMARK 3 S21: -0.0072 S22: 0.1012 S23: -0.0124
REMARK 3 S31: 0.3068 S32: -0.1524 S33: 0.0109
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 5GIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1300000702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : AGILENT EOS CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30492
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: 1BJ5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, 50 MM POTASSIUM PHOSPHATE (PH
REMARK 280 7.5), 5% GLYCEROL, AND 4% DMSO., PH 7.4, EVAPORATION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 41 CG CD CE NZ
REMARK 470 LYS A 181 CE NZ
REMARK 470 ARG A 186 CZ NH1 NH2
REMARK 470 LYS A 240 CD CE NZ
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 GLU A 396 CG CD OE1 OE2
REMARK 470 LYS B 41 CG CD CE NZ
REMARK 470 LYS B 181 CE NZ
REMARK 470 ARG B 186 CZ NH1 NH2
REMARK 470 LYS B 240 CD CE NZ
REMARK 470 LYS B 389 CG CD CE NZ
REMARK 470 GLU B 396 CG CD OE1 OE2
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 OG SER B 287 O1 PLM B 603 1.27
REMARK 500 NE2 HIS A 242 FE1 6WF A 601 1.57
REMARK 500 SG CYS B 360 CB CYS B 369 2.14
REMARK 500 NZ LYS A 199 O11 6WF A 601 2.17
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 ILE A 271 -54.69 -121.87
REMARK 500 LYS A 274 40.97 -95.84
REMARK 500 PRO A 303 -176.43 -69.87
REMARK 500 VAL A 310 -58.71 -137.08
REMARK 500 ALA A 322 85.77 -166.28
REMARK 500 LEU A 481 2.98 -64.04
REMARK 500 LYS A 564 -54.15 -125.50
REMARK 500 ILE B 271 -55.94 -121.25
REMARK 500 LYS B 274 40.84 -95.79
REMARK 500 PRO B 303 -176.23 -69.62
REMARK 500 VAL B 310 -58.17 -137.58
REMARK 500 ALA B 322 86.13 -167.00
REMARK 500 LEU B 481 2.56 -64.21
REMARK 500 LYS B 564 -54.22 -125.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PLM A 602
REMARK 610 PLM A 604
REMARK 610 PLM A 606
REMARK 610 PLM B 602
REMARK 610 PLM B 604
REMARK 610 PLM B 606
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 6WF A 601 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 199 NZ
REMARK 620 2 6WF A 601 S09 59.7
REMARK 620 3 6WF A 601 O11 70.9 125.0
REMARK 620 4 6WF A 601 N15 135.3 98.0 100.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 6WF B 601 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 199 NZ
REMARK 620 2 6WF B 601 S09 70.6
REMARK 620 3 6WF B 601 O11 67.0 116.7
REMARK 620 4 6WF B 601 N15 171.3 101.6 114.9
REMARK 620 5 HIS B 242 NE2 84.1 111.7 108.3 102.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6WF A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6WF B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide CYS B 360 and CYS B
REMARK 800 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLM B 607 and LYS B
REMARK 800 351
DBREF 5GIX A 3 583 UNP P02768 ALBU_HUMAN 27 607
DBREF 5GIX B 3 583 UNP P02768 ALBU_HUMAN 27 607
SEQRES 1 A 581 HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP LEU GLY
SEQRES 2 A 581 GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA PHE ALA
SEQRES 3 A 581 GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS VAL LYS
SEQRES 4 A 581 LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR CYS VAL
SEQRES 5 A 581 ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER LEU HIS
SEQRES 6 A 581 THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA THR LEU
SEQRES 7 A 581 ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS ALA LYS
SEQRES 8 A 581 GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN HIS LYS
SEQRES 9 A 581 ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG PRO GLU
SEQRES 10 A 581 VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN GLU GLU
SEQRES 11 A 581 THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA ARG ARG
SEQRES 12 A 581 HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE PHE ALA
SEQRES 13 A 581 LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS GLN ALA
SEQRES 14 A 581 ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU ASP GLU
SEQRES 15 A 581 LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS GLN ARG
SEQRES 16 A 581 LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU ARG ALA
SEQRES 17 A 581 PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN ARG PHE
SEQRES 18 A 581 PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU VAL THR
SEQRES 19 A 581 ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS GLY ASP
SEQRES 20 A 581 LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA LYS
SEQRES 21 A 581 TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER LYS LEU
SEQRES 22 A 581 LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS SER HIS
SEQRES 23 A 581 CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO ALA ASP
SEQRES 24 A 581 LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER LYS ASP
SEQRES 25 A 581 VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL PHE LEU
SEQRES 26 A 581 GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS PRO ASP
SEQRES 27 A 581 TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS THR TYR
SEQRES 28 A 581 GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA ASP PRO
SEQRES 29 A 581 HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE LYS PRO
SEQRES 30 A 581 LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN ASN CYS
SEQRES 31 A 581 GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE GLN ASN
SEQRES 32 A 581 ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO GLN VAL
SEQRES 33 A 581 SER THR PRO THR LEU VAL GLU VAL SER ARG ASN LEU GLY
SEQRES 34 A 581 LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU ALA LYS
SEQRES 35 A 581 ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL VAL LEU
SEQRES 36 A 581 ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO VAL SER
SEQRES 37 A 581 ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU VAL ASN
SEQRES 38 A 581 ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP GLU THR
SEQRES 39 A 581 TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE THR PHE
SEQRES 40 A 581 HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU ARG GLN
SEQRES 41 A 581 ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL LYS HIS
SEQRES 42 A 581 LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA VAL MET
SEQRES 43 A 581 ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS LYS ALA
SEQRES 44 A 581 ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY LYS LYS
SEQRES 45 A 581 LEU VAL ALA ALA SER GLN ALA ALA LEU
SEQRES 1 B 581 HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP LEU GLY
SEQRES 2 B 581 GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA PHE ALA
SEQRES 3 B 581 GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS VAL LYS
SEQRES 4 B 581 LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR CYS VAL
SEQRES 5 B 581 ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER LEU HIS
SEQRES 6 B 581 THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA THR LEU
SEQRES 7 B 581 ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS ALA LYS
SEQRES 8 B 581 GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN HIS LYS
SEQRES 9 B 581 ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG PRO GLU
SEQRES 10 B 581 VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN GLU GLU
SEQRES 11 B 581 THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA ARG ARG
SEQRES 12 B 581 HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE PHE ALA
SEQRES 13 B 581 LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS GLN ALA
SEQRES 14 B 581 ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU ASP GLU
SEQRES 15 B 581 LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS GLN ARG
SEQRES 16 B 581 LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU ARG ALA
SEQRES 17 B 581 PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN ARG PHE
SEQRES 18 B 581 PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU VAL THR
SEQRES 19 B 581 ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS GLY ASP
SEQRES 20 B 581 LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU ALA LYS
SEQRES 21 B 581 TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER LYS LEU
SEQRES 22 B 581 LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS SER HIS
SEQRES 23 B 581 CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO ALA ASP
SEQRES 24 B 581 LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER LYS ASP
SEQRES 25 B 581 VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL PHE LEU
SEQRES 26 B 581 GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS PRO ASP
SEQRES 27 B 581 TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS THR TYR
SEQRES 28 B 581 GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA ASP PRO
SEQRES 29 B 581 HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE LYS PRO
SEQRES 30 B 581 LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN ASN CYS
SEQRES 31 B 581 GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE GLN ASN
SEQRES 32 B 581 ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO GLN VAL
SEQRES 33 B 581 SER THR PRO THR LEU VAL GLU VAL SER ARG ASN LEU GLY
SEQRES 34 B 581 LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU ALA LYS
SEQRES 35 B 581 ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL VAL LEU
SEQRES 36 B 581 ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO VAL SER
SEQRES 37 B 581 ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU VAL ASN
SEQRES 38 B 581 ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP GLU THR
SEQRES 39 B 581 TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE THR PHE
SEQRES 40 B 581 HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU ARG GLN
SEQRES 41 B 581 ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL LYS HIS
SEQRES 42 B 581 LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA VAL MET
SEQRES 43 B 581 ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS LYS ALA
SEQRES 44 B 581 ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY LYS LYS
SEQRES 45 B 581 LEU VAL ALA ALA SER GLN ALA ALA LEU
HET 6WF A 601 41
HET PLM A 602 13
HET PLM A 603 18
HET PLM A 604 17
HET PLM A 605 18
HET PLM A 606 17
HET PLM A 607 18
HET 6WF B 601 41
HET PLM B 602 13
HET PLM B 603 18
HET PLM B 604 17
HET PLM B 605 18
HET PLM B 606 17
HET PLM B 607 18
HETNAM 6WF 14-PIPERIDIN-1-YL-11-OXA-13$L^{3}-THIA-15,16$L^{4}-
HETNAM 2 6WF DIAZA-12$L^{3}-FERRATETRACYCLO[8.7.0.0^{2,7}.0^{12,
HETNAM 3 6WF 16}]HEPTADECA-1(10),2(7),3,5,8,13,16-HEPTAENE
HETNAM PLM PALMITIC ACID
FORMUL 3 6WF 2(C17 H18 FE N3 O S)
FORMUL 4 PLM 12(C16 H32 O2)
FORMUL 17 HOH *2(H2 O)
HELIX 1 AA1 SER A 5 GLY A 15 1 11
HELIX 2 AA2 GLY A 15 LEU A 31 1 17
HELIX 3 AA3 PRO A 35 ASP A 56 1 22
HELIX 4 AA4 SER A 65 CYS A 75 1 11
HELIX 5 AA5 THR A 79 GLY A 85 1 7
HELIX 6 AA6 GLU A 86 LYS A 93 5 8
HELIX 7 AA7 PRO A 96 HIS A 105 1 10
HELIX 8 AA8 GLU A 119 ASN A 130 1 12
HELIX 9 AA9 ASN A 130 HIS A 146 1 17
HELIX 10 AB1 TYR A 150 CYS A 169 1 20
HELIX 11 AB2 ASP A 173 GLY A 207 1 35
HELIX 12 AB3 GLY A 207 PHE A 223 1 17
HELIX 13 AB4 GLU A 227 GLY A 248 1 22
HELIX 14 AB5 ASP A 249 ASN A 267 1 19
HELIX 15 AB6 GLN A 268 ILE A 271 5 4
HELIX 16 AB7 LEU A 275 LYS A 281 1 7
HELIX 17 AB8 PRO A 282 GLU A 292 1 11
HELIX 18 AB9 LEU A 305 VAL A 310 1 6
HELIX 19 AC1 ASP A 314 ALA A 322 1 9
HELIX 20 AC2 ALA A 322 HIS A 338 1 17
HELIX 21 AC3 SER A 342 CYS A 361 1 20
HELIX 22 AC4 PRO A 366 LEU A 398 1 33
HELIX 23 AC5 GLY A 399 VAL A 415 1 17
HELIX 24 AC6 SER A 419 CYS A 438 1 20
HELIX 25 AC7 PRO A 441 THR A 467 1 27
HELIX 26 AC8 SER A 470 THR A 478 1 9
HELIX 27 AC9 ASN A 483 ALA A 490 1 8
HELIX 28 AD1 ALA A 504 THR A 508 5 5
HELIX 29 AD2 HIS A 510 THR A 515 5 6
HELIX 30 AD3 SER A 517 LYS A 536 1 20
HELIX 31 AD4 THR A 540 CYS A 559 1 20
HELIX 32 AD5 LYS A 564 LEU A 583 1 20
HELIX 33 AD6 SER B 5 GLY B 15 1 11
HELIX 34 AD7 GLY B 15 LEU B 31 1 17
HELIX 35 AD8 PRO B 35 ASP B 56 1 22
HELIX 36 AD9 SER B 65 CYS B 75 1 11
HELIX 37 AE1 THR B 79 GLY B 85 1 7
HELIX 38 AE2 GLU B 86 LYS B 93 5 8
HELIX 39 AE3 PRO B 96 HIS B 105 1 10
HELIX 40 AE4 GLU B 119 ASN B 130 1 12
HELIX 41 AE5 ASN B 130 HIS B 146 1 17
HELIX 42 AE6 TYR B 150 CYS B 169 1 20
HELIX 43 AE7 ASP B 173 PHE B 206 1 34
HELIX 44 AE8 GLY B 207 PHE B 223 1 17
HELIX 45 AE9 GLU B 227 CYS B 246 1 20
HELIX 46 AF1 ASP B 249 ASN B 267 1 19
HELIX 47 AF2 GLN B 268 ILE B 271 5 4
HELIX 48 AF3 LEU B 275 LYS B 281 1 7
HELIX 49 AF4 PRO B 282 GLU B 292 1 11
HELIX 50 AF5 LEU B 305 VAL B 310 1 6
HELIX 51 AF6 ASP B 314 ALA B 322 1 9
HELIX 52 AF7 ALA B 322 HIS B 338 1 17
HELIX 53 AF8 SER B 342 CYS B 361 1 20
HELIX 54 AF9 PRO B 366 LEU B 398 1 33
HELIX 55 AG1 GLY B 399 VAL B 415 1 17
HELIX 56 AG2 SER B 419 CYS B 438 1 20
HELIX 57 AG3 PRO B 441 THR B 467 1 27
HELIX 58 AG4 SER B 470 THR B 478 1 9
HELIX 59 AG5 ASN B 483 ALA B 490 1 8
HELIX 60 AG6 ALA B 504 THR B 508 5 5
HELIX 61 AG7 HIS B 510 THR B 515 5 6
HELIX 62 AG8 SER B 517 LYS B 536 1 20
HELIX 63 AG9 THR B 540 CYS B 559 1 20
HELIX 64 AH1 LYS B 564 LEU B 583 1 20
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.03
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.04
SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.03
SSBOND 4 CYS A 124 CYS A 169 1555 1555 2.03
SSBOND 5 CYS A 168 CYS A 177 1555 1555 2.03
SSBOND 6 CYS A 200 CYS A 246 1555 1555 2.01
SSBOND 7 CYS A 245 CYS A 253 1555 1555 2.03
SSBOND 8 CYS A 265 CYS A 279 1555 1555 2.03
SSBOND 9 CYS A 278 CYS A 289 1555 1555 2.03
SSBOND 10 CYS A 316 CYS A 361 1555 1555 2.03
SSBOND 11 CYS A 360 CYS A 369 1555 1555 2.03
SSBOND 12 CYS A 392 CYS A 438 1555 1555 2.03
SSBOND 13 CYS A 437 CYS A 448 1555 1555 2.04
SSBOND 14 CYS A 461 CYS A 477 1555 1555 2.03
SSBOND 15 CYS A 476 CYS A 487 1555 1555 2.03
SSBOND 16 CYS A 514 CYS A 559 1555 1555 2.03
SSBOND 17 CYS A 558 CYS A 567 1555 1555 2.03
SSBOND 18 CYS B 53 CYS B 62 1555 1555 2.03
SSBOND 19 CYS B 75 CYS B 91 1555 1555 1.98
SSBOND 20 CYS B 90 CYS B 101 1555 1555 2.03
SSBOND 21 CYS B 124 CYS B 169 1555 1555 2.03
SSBOND 22 CYS B 168 CYS B 177 1555 1555 2.03
SSBOND 23 CYS B 200 CYS B 246 1555 1555 2.03
SSBOND 24 CYS B 245 CYS B 253 1555 1555 2.03
SSBOND 25 CYS B 265 CYS B 279 1555 1555 2.03
SSBOND 26 CYS B 278 CYS B 289 1555 1555 2.03
SSBOND 27 CYS B 316 CYS B 361 1555 1555 2.03
SSBOND 28 CYS B 360 CYS B 369 1555 1555 2.03
SSBOND 29 CYS B 392 CYS B 438 1555 1555 2.03
SSBOND 30 CYS B 437 CYS B 448 1555 1555 2.03
SSBOND 31 CYS B 461 CYS B 477 1555 1555 2.03
SSBOND 32 CYS B 476 CYS B 487 1555 1555 2.03
SSBOND 33 CYS B 514 CYS B 559 1555 1555 2.03
SSBOND 34 CYS B 558 CYS B 567 1555 1555 2.03
LINK NE ARG A 117 O2 PLM A 602 1555 1555 1.30
LINK NZ LYS A 199 S09 6WF A 601 1555 1555 1.77
LINK CB CYS A 360 SG CYS A 369 1555 1555 1.64
LINK SG CYS A 360 CB CYS A 369 1555 1555 1.84
LINK NZ LYS B 351 O2 PLM B 607 1555 1555 1.30
LINK CB CYS B 360 SG CYS B 369 1555 1555 1.96
LINK NZ LYS A 199 FE1 6WF A 601 1555 1555 1.84
LINK NZ LYS B 199 FE1 6WF B 601 1555 1555 2.16
LINK NE2 HIS B 242 FE1 6WF B 601 1555 1555 2.16
CISPEP 1 GLU A 95 PRO A 96 0 8.03
CISPEP 2 GLU B 95 PRO B 96 0 5.96
SITE 1 AC1 7 GLN A 196 LYS A 199 CYS A 200 HIS A 242
SITE 2 AC1 7 CYS A 245 ARG A 257 ALA A 291
SITE 1 AC2 5 ARG A 117 LEU A 135 TYR A 138 LEU A 139
SITE 2 AC2 5 TYR A 161
SITE 1 AC3 9 ARG A 10 LEU A 14 LEU A 66 LEU A 69
SITE 2 AC3 9 PHE A 70 TYR A 150 ARG A 257 LEU A 283
SITE 3 AC3 9 SER A 287
SITE 1 AC4 7 SER A 342 VAL A 344 ARG A 348 LEU A 387
SITE 2 AC4 7 LEU A 453 ARG A 485 PLM A 605
SITE 1 AC5 8 ARG A 410 TYR A 411 VAL A 418 LEU A 457
SITE 2 AC5 8 LEU A 460 HIS A 464 SER A 489 PLM A 604
SITE 1 AC6 7 TYR A 401 PHE A 507 LYS A 525 ALA A 528
SITE 2 AC6 7 VAL A 547 PHE A 551 SER A 579
SITE 1 AC7 5 ARG A 209 ALA A 210 VAL A 216 ASP A 324
SITE 2 AC7 5 LYS A 351
SITE 1 AC8 8 GLN B 196 LYS B 199 CYS B 200 VAL B 241
SITE 2 AC8 8 HIS B 242 CYS B 245 ARG B 257 ALA B 291
SITE 1 AC9 6 ARG B 117 LEU B 135 TYR B 138 ALA B 158
SITE 2 AC9 6 TYR B 161 PHE B 165
SITE 1 AD1 12 ARG B 10 LEU B 14 LEU B 22 LEU B 66
SITE 2 AD1 12 LEU B 69 TYR B 150 LEU B 251 ALA B 254
SITE 3 AD1 12 ARG B 257 ALA B 258 LEU B 284 SER B 287
SITE 1 AD2 7 SER B 342 VAL B 344 ARG B 348 LEU B 387
SITE 2 AD2 7 LEU B 453 ARG B 485 PLM B 605
SITE 1 AD3 7 TYR B 411 VAL B 418 LEU B 457 LEU B 460
SITE 2 AD3 7 HIS B 464 SER B 489 PLM B 604
SITE 1 AD4 9 TYR B 401 PHE B 507 LYS B 525 ALA B 528
SITE 2 AD4 9 LEU B 532 PHE B 551 ALA B 552 SER B 579
SITE 3 AD4 9 GLN B 580
SITE 1 AD5 14 THR B 356 LEU B 357 GLU B 358 LYS B 359
SITE 2 AD5 14 CYS B 361 ALA B 362 ALA B 363 PRO B 366
SITE 3 AD5 14 HIS B 367 GLU B 368 TYR B 370 ALA B 371
SITE 4 AD5 14 LYS B 372 VAL B 373
SITE 1 AD6 10 ARG B 209 ASP B 324 LEU B 347 ARG B 348
SITE 2 AD6 10 LEU B 349 ALA B 350 THR B 352 TYR B 353
SITE 3 AD6 10 GLU B 354 THR B 355
CRYST1 38.472 94.550 96.105 104.90 89.90 100.86 P 1 2
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 0.025993 0.004989 0.001304 0.00000
SCALE2 0.000000 0.010769 0.002917 0.00000
SCALE3 0.000000 0.000000 0.010780 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
