HEADER TRANSPORT PROTEIN 26-JUL-05 2BXC
TITLE HUMAN SERUM ALBUMIN COMPLEXED WITH PHENYLBUTAZONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HUMAN SERUM ALBUMIN;
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 TISSUE: PLASMA;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS TRANSPORT PROTEIN, ALBUMIN, CARRIER PROTEIN, LIPID-BINDING, METAL-
KEYWDS 2 BINDING, DRUG-BINDING, PHENYLBUTAZONE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GHUMAN,P.A.ZUNSZAIN,I.PETITPAS,A.A.BHATTACHARYA,S.CURRY
REVDAT 5 13-DEC-23 2BXC 1 REMARK
REVDAT 4 24-JUL-19 2BXC 1 REMARK
REVDAT 3 24-FEB-09 2BXC 1 VERSN
REVDAT 2 20-DEC-06 2BXC 1 JRNL
REVDAT 1 22-SEP-05 2BXC 0
JRNL AUTH J.GHUMAN,P.A.ZUNSZAIN,I.PETITPAS,A.A.BHATTACHARYA,M.OTAGIRI,
JRNL AUTH 2 S.CURRY
JRNL TITL STRUCTURAL BASIS OF THE DRUG-BINDING SPECIFICITY OF HUMAN
JRNL TITL 2 SERUM ALBUMIN.
JRNL REF J.MOL.BIOL. V. 353 38 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16169013
JRNL DOI 10.1016/J.JMB.2005.07.075
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 677256.620
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 22248
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 SET) : 0.251
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1056
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.29
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3430
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8758
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 82.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.70000
REMARK 3 B22 (A**2) : -2.19000
REMARK 3 B33 (A**2) : 10.89000
REMARK 3 B12 (A**2) : -2.13000
REMARK 3 B13 (A**2) : 10.46000
REMARK 3 B23 (A**2) : -10.72000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.690
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.26
REMARK 3 BSOL : 76.92
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PBZ.SC.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PBZ.SC.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1290025055.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 298.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8130
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22396
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 36.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1E78
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.00
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: PQS
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: PQS
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 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 ASP A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 LYS A 4
REMARK 465 LEU A 583
REMARK 465 GLY A 584
REMARK 465 LEU A 585
REMARK 465 ASP B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 LYS B 4
REMARK 465 LEU B 583
REMARK 465 GLY B 584
REMARK 465 LEU B 585
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 12 CG CD CE NZ
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 GLU A 60 CG CD OE1 OE2
REMARK 470 LEU A 69 CG CD1 CD2
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 THR A 83 OG1 CG2
REMARK 470 TYR A 84 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 GLN A 94 CG CD OE1 NE2
REMARK 470 GLU A 95 CG CD OE1 OE2
REMARK 470 GLU A 97 CG CD OE1 OE2
REMARK 470 ASN A 111 CG OD1 ND2
REMARK 470 ARG A 114 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 115 CG CD1 CD2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LYS A 190 CD CE NZ
REMARK 470 LYS A 205 CD CE NZ
REMARK 470 ARG A 209 CD NE CZ NH1 NH2
REMARK 470 LEU A 251 CG CD1 CD2
REMARK 470 LYS A 274 CD CE NZ
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 GLU A 277 CG CD OE1 OE2
REMARK 470 GLU A 280 CG CD OE1 OE2
REMARK 470 ASP A 301 CG OD1 OD2
REMARK 470 LEU A 302 CG CD1 CD2
REMARK 470 LYS A 313 CG CD CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 359 CD CE NZ
REMARK 470 GLU A 368 CG CD OE1 OE2
REMARK 470 LYS A 378 CG CD CE NZ
REMARK 470 LYS A 389 CD CE NZ
REMARK 470 GLN A 390 CG CD OE1 NE2
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 ARG A 410 CD NE CZ NH1 NH2
REMARK 470 LYS A 436 CD CE NZ
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 PHE A 509 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 513 CG1 CG2 CD1
REMARK 470 LYS A 519 CG CD CE NZ
REMARK 470 LYS A 524 CG CD CE NZ
REMARK 470 LYS A 536 CG CD CE NZ
REMARK 470 LYS A 538 CG CD CE NZ
REMARK 470 LYS A 541 CD CE NZ
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 PHE A 551 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 554 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 556 CG CD OE1 OE2
REMARK 470 LYS A 560 CG CD CE NZ
REMARK 470 ASP A 563 CG OD1 OD2
REMARK 470 LYS A 564 CG CD CE NZ
REMARK 470 GLU A 565 CG CD OE1 OE2
REMARK 470 THR A 566 OG1 CG2
REMARK 470 PHE A 568 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 573 CG CD CE NZ
REMARK 470 LYS A 574 CG CD CE NZ
REMARK 470 GLN A 580 CG CD OE1 NE2
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 LYS B 64 CG CD CE NZ
REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2
REMARK 470 THR B 83 OG1 CG2
REMARK 470 TYR B 84 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 86 CG CD OE1 OE2
REMARK 470 MET B 87 CG SD CE
REMARK 470 GLN B 94 CG CD OE1 NE2
REMARK 470 GLU B 97 CG CD OE1 OE2
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 115 CG CD1 CD2
REMARK 470 GLU B 119 CG CD OE1 OE2
REMARK 470 HIS B 128 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 GLU B 141 CG CD OE1 OE2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 ARG B 160 CZ NH1 NH2
REMARK 470 GLU B 167 CG CD OE1 OE2
REMARK 470 GLN B 170 CG CD OE1 NE2
REMARK 470 LYS B 174 CG CD CE NZ
REMARK 470 LEU B 178 CG CD1 CD2
REMARK 470 LYS B 190 CE NZ
REMARK 470 GLU B 208 CG CD OE1 OE2
REMARK 470 ARG B 209 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 247 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 276 CG CD CE NZ
REMARK 470 GLU B 277 CG CD OE1 OE2
REMARK 470 LYS B 286 CG CD CE NZ
REMARK 470 GLU B 294 CG CD OE1 OE2
REMARK 470 GLU B 297 CG CD OE1 OE2
REMARK 470 ASP B 301 CG OD1 OD2
REMARK 470 LYS B 313 CG CD CE NZ
REMARK 470 LYS B 317 CD CE NZ
REMARK 470 LYS B 359 CE NZ
REMARK 470 LYS B 378 CD CE NZ
REMARK 470 LYS B 389 CE NZ
REMARK 470 LYS B 402 CD CE NZ
REMARK 470 LYS B 436 CD CE NZ
REMARK 470 GLU B 442 CG CD OE1 OE2
REMARK 470 LYS B 444 CE NZ
REMARK 470 LYS B 466 CG CD CE NZ
REMARK 470 PHE B 509 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS B 510 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 512 CG OD1 OD2
REMARK 470 ILE B 513 CG1 CG2 CD1
REMARK 470 LYS B 519 CG CD CE NZ
REMARK 470 LYS B 536 CG CD CE NZ
REMARK 470 PHE B 554 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 562 CG OD1 OD2
REMARK 470 GLU B 565 CG CD OE1 OE2
REMARK 470 GLU B 570 CG CD OE1 OE2
REMARK 470 LYS B 574 CG CD CE NZ
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 ALA A 511 N ILE A 513 2.16
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 CYS A 567 CA - CB - SG ANGL. DEV. = 9.6 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 GLU A 17 -75.15 -51.42
REMARK 500 LEU A 31 76.61 -109.15
REMARK 500 GLU A 57 47.26 -79.45
REMARK 500 SER A 58 0.86 -175.00
REMARK 500 ALA A 59 -101.36 -35.98
REMARK 500 GLU A 60 -85.24 -81.78
REMARK 500 CYS A 75 11.97 -65.70
REMARK 500 VAL A 77 -16.89 -140.99
REMARK 500 THR A 79 -9.86 -55.74
REMARK 500 GLN A 94 -155.29 -99.26
REMARK 500 GLU A 97 31.49 -158.86
REMARK 500 ASN A 111 41.85 -83.99
REMARK 500 GLU A 119 152.14 -47.58
REMARK 500 TYR A 138 -72.52 -46.78
REMARK 500 PRO A 147 -9.43 -49.96
REMARK 500 ALA A 171 -167.58 -77.91
REMARK 500 LEU A 178 -81.74 -71.62
REMARK 500 LEU A 179 -64.88 -11.99
REMARK 500 PHE A 223 75.36 -110.83
REMARK 500 ASN A 267 40.98 -99.34
REMARK 500 ILE A 271 -72.09 -104.85
REMARK 500 LYS A 276 -77.66 -41.64
REMARK 500 LEU A 283 -72.23 -35.75
REMARK 500 ALA A 300 -100.50 -45.07
REMARK 500 SER A 312 156.65 -47.90
REMARK 500 VAL A 315 -72.86 -44.52
REMARK 500 ALA A 322 78.29 -150.43
REMARK 500 HIS A 367 -36.32 -37.80
REMARK 500 GLN A 397 -70.65 -50.23
REMARK 500 VAL A 418 143.88 -39.10
REMARK 500 GLU A 492 -90.11 -103.84
REMARK 500 PRO A 499 130.63 -37.89
REMARK 500 PHE A 507 123.41 -178.20
REMARK 500 HIS A 510 135.79 -31.67
REMARK 500 ASP A 512 -7.29 -38.75
REMARK 500 GLU A 520 -9.19 -57.06
REMARK 500 LYS A 538 -87.28 -53.44
REMARK 500 ALA A 539 93.15 -44.81
REMARK 500 LYS A 541 -73.84 -155.66
REMARK 500 LYS A 564 173.10 -45.75
REMARK 500 GLU A 565 39.35 -61.87
REMARK 500 LEU B 31 74.23 -106.31
REMARK 500 PHE B 49 -19.91 -142.81
REMARK 500 THR B 52 1.94 -67.28
REMARK 500 VAL B 54 -96.41 -52.10
REMARK 500 GLU B 57 -109.81 -65.25
REMARK 500 SER B 58 82.94 -52.27
REMARK 500 ALA B 59 -162.96 -112.53
REMARK 500 GLU B 60 -85.98 -36.72
REMARK 500 VAL B 77 -11.07 -152.31
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P1Z A2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P1Z B2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AO6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
REMARK 900 RELATED ID: 1BJ5 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID
REMARK 900 RELATED ID: 1BKE RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN IN A COMPLEX WITH MYRISTIC ACID AND TRI-
REMARK 900 IODOBENZOIC ACID
REMARK 900 RELATED ID: 1BM0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
REMARK 900 RELATED ID: 1E78 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN
REMARK 900 RELATED ID: 1E7A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH THE GENERAL
REMARK 900 ANESTHETIC PROPOFOL
REMARK 900 RELATED ID: 1E7B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH HALOTHANE
REMARK 900 RELATED ID: 1E7C RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE GENERAL
REMARK 900 ANESTHETIC HALOTHANE
REMARK 900 RELATED ID: 1E7E RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH DECANOIC ACID
REMARK 900 RELATED ID: 1E7F RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH DODECANOIC ACID
REMARK 900 RELATED ID: 1E7G RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID
REMARK 900 RELATED ID: 1E7H RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH HEXADECANOIC ACID
REMARK 900 RELATED ID: 1E7I RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH OCTADECANOIC ACID
REMARK 900 RELATED ID: 1GNI RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-9- OCTADECENOIC ACID (OLEIC
REMARK 900 ACID)
REMARK 900 RELATED ID: 1GNJ RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH CIS-5,8 ,11,14-EICOSATETRAENOIC
REMARK 900 ACID (ARACHIDONIC ACID)
REMARK 900 RELATED ID: 1H9Z RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE R-(+)
REMARK 900 ENANTIOMER OF WARFARIN
REMARK 900 RELATED ID: 1HA2 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTIC ACID AND THE S-(-)
REMARK 900 ENANTIOMER OF WARFARIN
REMARK 900 RELATED ID: 1HK1 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-
REMARK 900 THYRONINE)
REMARK 900 RELATED ID: 1HK2 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'
REMARK 900 -TETRAIODO-L- THYRONINE)
REMARK 900 RELATED ID: 1HK3 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'
REMARK 900 -TETRAIODO-L- THYRONINE)
REMARK 900 RELATED ID: 1HK4 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH THYROXINE (3,3',5,5'-TETRAIODO-L-
REMARK 900 THYRONINE) AND MYRISTIC ACID (TETRADECANOIC ACID)
REMARK 900 RELATED ID: 1HK5 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN MUTANT R218H COMPLEXED WITH THYROXINE (3,3',5,5'
REMARK 900 -TETRAIODO-L- THYRONINE) AND MYRISTIC ACID (TETRADECANOIC ACID)
REMARK 900 RELATED ID: 1N5U RELATED DB: PDB
REMARK 900 X-RAY STUDY OF HUMAN SERUM ALBUMIN COMPLEXED WITH HEME
REMARK 900 RELATED ID: 1O9X RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH TETRADECANOIC ACID (MYRISTIC
REMARK 900 ACID) AND HEMIN
REMARK 900 RELATED ID: 1TF0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GA MODULE COMPLEXED WITH HUMANSERUM ALBUMIN
REMARK 900 RELATED ID: 1UOR RELATED DB: PDB
REMARK 900 X-RAY STUDY OF RECOMBINANT HUMAN SERUM ALBUMIN. PHASES DETERMINED
REMARK 900 BY MOLECULAR REPLACEMENT METHOD, USING LOW RESOLUTION STRUCTURE
REMARK 900 MODEL OF TETRAGONAL FORM OF HUMAN SERUM ALBUMIN
REMARK 900 RELATED ID: 1YSX RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DOMAIN 3 FROM HUMAN SERUM ALBUMINCOMPLEXED TO
REMARK 900 AN ANTI-APOPTOTIC LIGAND DIRECTED AGAINST BCL-XL AND BCL-2
REMARK 900 RELATED ID: 2BX8 RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH AZAPROPAZONE
REMARK 900 RELATED ID: 2BXA RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH 3-CARBOXY-4-METHYL-5-PROPYL-2-
REMARK 900 FURANPROPANOIC ACID (CMPF)
REMARK 900 RELATED ID: 2BXB RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH OXYPHENBUTAZONE
REMARK 900 RELATED ID: 2BXD RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH WARFARIN
REMARK 900 RELATED ID: 2BXE RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH DIFLUNISAL
REMARK 900 RELATED ID: 2BXF RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH DIAZEPAM
REMARK 900 RELATED ID: 2BXG RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH IBUPROFEN
REMARK 900 RELATED ID: 2BXH RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH INDOXYL SULFATE
REMARK 900 RELATED ID: 2BXI RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND AZAPROPAZONE
REMARK 900 RELATED ID: 2BXK RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, AZAPROPAZONE AND
REMARK 900 INDOMETHACIN
REMARK 900 RELATED ID: 2BXL RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND 3,5-
REMARK 900 DIIODOSALICYLIC ACID
REMARK 900 RELATED ID: 2BXM RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND INDOMETHACIN
REMARK 900 RELATED ID: 2BXN RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND IODIPAMIDE
REMARK 900 RELATED ID: 2BXO RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND OXYPHENBUTAZONE
REMARK 900 RELATED ID: 2BXP RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE AND PHENYLBUTAZONE
REMARK 900 RELATED ID: 2BXQ RELATED DB: PDB
REMARK 900 HUMAN SERUM ALBUMIN COMPLEXED WITH MYRISTATE, PHENYLBUTAZONE AND
REMARK 900 INDOMETHACIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE IS FOR PRE-CURSOR. MATURE POLYPEPTIDE WAS
REMARK 999 CRYSTALLISED (WHICH LACKS SIGNAL AND PROPEPTIDES -
REMARK 999 RESIDUES 1-24)
DBREF 2BXC A 1 585 UNP P02768 ALBU_HUMAN 25 609
DBREF 2BXC B 1 585 UNP P02768 ALBU_HUMAN 25 609
SEQRES 1 A 585 ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP
SEQRES 2 A 585 LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA
SEQRES 3 A 585 PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS
SEQRES 4 A 585 VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR
SEQRES 5 A 585 CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER
SEQRES 6 A 585 LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA
SEQRES 7 A 585 THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS
SEQRES 8 A 585 ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN
SEQRES 9 A 585 HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG
SEQRES 10 A 585 PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN
SEQRES 11 A 585 GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA
SEQRES 12 A 585 ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE
SEQRES 13 A 585 PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS
SEQRES 14 A 585 GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU
SEQRES 15 A 585 ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS
SEQRES 16 A 585 GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU
SEQRES 17 A 585 ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN
SEQRES 18 A 585 ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU
SEQRES 19 A 585 VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS
SEQRES 20 A 585 GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU
SEQRES 21 A 585 ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER
SEQRES 22 A 585 LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS
SEQRES 23 A 585 SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO
SEQRES 24 A 585 ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER
SEQRES 25 A 585 LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL
SEQRES 26 A 585 PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS
SEQRES 27 A 585 PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS
SEQRES 28 A 585 THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA
SEQRES 29 A 585 ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE
SEQRES 30 A 585 LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN
SEQRES 31 A 585 ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE
SEQRES 32 A 585 GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO
SEQRES 33 A 585 GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN
SEQRES 34 A 585 LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU
SEQRES 35 A 585 ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL
SEQRES 36 A 585 VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO
SEQRES 37 A 585 VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU
SEQRES 38 A 585 VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP
SEQRES 39 A 585 GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE
SEQRES 40 A 585 THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU
SEQRES 41 A 585 ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL
SEQRES 42 A 585 LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA
SEQRES 43 A 585 VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS
SEQRES 44 A 585 LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY
SEQRES 45 A 585 LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU
SEQRES 1 B 585 ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP
SEQRES 2 B 585 LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA
SEQRES 3 B 585 PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS
SEQRES 4 B 585 VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR
SEQRES 5 B 585 CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER
SEQRES 6 B 585 LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA
SEQRES 7 B 585 THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS
SEQRES 8 B 585 ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN
SEQRES 9 B 585 HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG
SEQRES 10 B 585 PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN
SEQRES 11 B 585 GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA
SEQRES 12 B 585 ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE
SEQRES 13 B 585 PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS
SEQRES 14 B 585 GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU
SEQRES 15 B 585 ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS
SEQRES 16 B 585 GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU
SEQRES 17 B 585 ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN
SEQRES 18 B 585 ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU
SEQRES 19 B 585 VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS
SEQRES 20 B 585 GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU
SEQRES 21 B 585 ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER
SEQRES 22 B 585 LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS
SEQRES 23 B 585 SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO
SEQRES 24 B 585 ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER
SEQRES 25 B 585 LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL
SEQRES 26 B 585 PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS
SEQRES 27 B 585 PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS
SEQRES 28 B 585 THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA
SEQRES 29 B 585 ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE
SEQRES 30 B 585 LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN
SEQRES 31 B 585 ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE
SEQRES 32 B 585 GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO
SEQRES 33 B 585 GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN
SEQRES 34 B 585 LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU
SEQRES 35 B 585 ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL
SEQRES 36 B 585 VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO
SEQRES 37 B 585 VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU
SEQRES 38 B 585 VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP
SEQRES 39 B 585 GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE
SEQRES 40 B 585 THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU
SEQRES 41 B 585 ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL
SEQRES 42 B 585 LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA
SEQRES 43 B 585 VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS
SEQRES 44 B 585 LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY
SEQRES 45 B 585 LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU
HET P1Z A2001 23
HET P1Z B2001 23
HETNAM P1Z 4-BUTYL-1,2-DIPHENYL-PYRAZOLIDINE-3,5-DIONE
FORMUL 3 P1Z 2(C19 H20 N2 O2)
HELIX 1 1 GLU A 6 LEU A 31 1 26
HELIX 2 2 PRO A 35 ASP A 56 1 22
HELIX 3 3 SER A 65 CYS A 75 1 11
HELIX 4 4 LEU A 80 GLY A 85 1 6
HELIX 5 5 GLU A 86 ALA A 92 1 7
HELIX 6 6 GLU A 97 HIS A 105 1 9
HELIX 7 7 GLU A 119 ASN A 130 1 12
HELIX 8 8 ASN A 130 ARG A 144 1 15
HELIX 9 9 TYR A 150 CYS A 169 1 20
HELIX 10 10 ASP A 173 PHE A 223 1 51
HELIX 11 11 GLU A 227 GLY A 248 1 22
HELIX 12 12 ASP A 249 ASN A 267 1 19
HELIX 13 13 ASN A 267 SER A 272 1 6
HELIX 14 14 LEU A 275 GLU A 280 1 6
HELIX 15 15 PRO A 282 ALA A 291 1 10
HELIX 16 16 LEU A 305 VAL A 310 1 6
HELIX 17 17 ASP A 314 ALA A 322 1 9
HELIX 18 18 ALA A 322 ARG A 337 1 16
HELIX 19 19 SER A 342 ALA A 362 1 21
HELIX 20 20 ASP A 365 TYR A 370 1 6
HELIX 21 21 VAL A 373 VAL A 415 1 43
HELIX 22 22 SER A 419 CYS A 438 1 20
HELIX 23 23 PRO A 441 THR A 467 1 27
HELIX 24 24 SER A 470 GLU A 479 1 10
HELIX 25 25 ASN A 483 LEU A 491 1 9
HELIX 26 26 ASN A 503 PHE A 507 5 5
HELIX 27 27 HIS A 510 THR A 515 5 6
HELIX 28 28 SER A 517 LYS A 536 1 20
HELIX 29 29 GLU A 542 ALA A 561 1 20
HELIX 30 30 THR A 566 ALA A 582 1 17
HELIX 31 31 SER B 5 GLY B 15 1 11
HELIX 32 32 GLY B 15 LEU B 31 1 17
HELIX 33 33 PRO B 35 LYS B 51 1 17
HELIX 34 34 SER B 65 THR B 79 1 15
HELIX 35 35 GLU B 86 LYS B 93 1 8
HELIX 36 36 PRO B 96 GLN B 104 1 9
HELIX 37 37 GLU B 119 ASN B 130 1 12
HELIX 38 38 ASN B 130 ARG B 144 1 15
HELIX 39 39 TYR B 150 CYS B 169 1 20
HELIX 40 40 ASP B 173 GLY B 207 1 35
HELIX 41 41 GLY B 207 PHE B 223 1 17
HELIX 42 42 GLU B 227 GLY B 248 1 22
HELIX 43 43 ASP B 249 ASN B 267 1 19
HELIX 44 44 ASN B 267 SER B 272 1 6
HELIX 45 45 LEU B 275 GLU B 280 5 6
HELIX 46 46 PRO B 282 ALA B 291 1 10
HELIX 47 47 LEU B 305 VAL B 310 1 6
HELIX 48 48 ASP B 314 ALA B 322 1 9
HELIX 49 49 ALA B 322 ARG B 337 1 16
HELIX 50 50 SER B 342 ALA B 363 1 22
HELIX 51 51 ASP B 365 TYR B 370 1 6
HELIX 52 52 VAL B 373 ASP B 375 5 3
HELIX 53 53 GLU B 376 VAL B 415 1 40
HELIX 54 54 SER B 419 CYS B 438 1 20
HELIX 55 55 PRO B 441 THR B 467 1 27
HELIX 56 56 SER B 470 GLU B 479 1 10
HELIX 57 57 ASN B 483 LEU B 491 1 9
HELIX 58 58 ASN B 503 PHE B 507 5 5
HELIX 59 59 HIS B 510 CYS B 514 5 5
HELIX 60 60 SER B 517 LYS B 534 1 18
HELIX 61 61 GLU B 542 LYS B 560 1 19
HELIX 62 62 LYS B 574 ALA B 582 1 9
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.03
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.03
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 2.03
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 2.03
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 2.01
SSBOND 18 CYS B 53 CYS B 62 1555 1555 2.03
SSBOND 19 CYS B 75 CYS B 91 1555 1555 2.03
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 2.04
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
CISPEP 1 GLU B 95 PRO B 96 0 -0.28
SITE 1 AC1 13 TYR A 150 GLU A 153 GLN A 196 LYS A 199
SITE 2 AC1 13 LEU A 219 ARG A 222 LEU A 238 HIS A 242
SITE 3 AC1 13 ARG A 257 ALA A 261 SER A 287 ILE A 290
SITE 4 AC1 13 ALA A 291
SITE 1 AC2 8 TYR B 150 LEU B 219 ARG B 222 LEU B 238
SITE 2 AC2 8 HIS B 242 ARG B 257 ALA B 261 ALA B 291
CRYST1 54.650 55.330 120.000 81.52 91.61 64.92 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 0.018298 -0.008564 0.002054 0.00000
SCALE2 0.000000 0.019955 -0.003568 0.00000
SCALE3 0.000000 0.000000 0.008469 0.00000
MTRIX1 1 0.431900 0.901200 0.036500 -47.90770 1
MTRIX2 1 0.901100 -0.432900 0.025100 -33.61930 1
MTRIX3 1 0.038400 0.022100 -0.999000 57.06670 1
(ATOM LINES ARE NOT SHOWN.)
END