HEADER CARRIER PROTEIN 26-AUG-00 1E7A
TITLE CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN COMPLEXED WITH THE GENERAL
TITLE 2 ANESTHETIC PROPOFOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS CARRIER PROTEIN, ALBUMIN, GENERAL ANESTHETIC, PROPOFOL
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.BHATTACHARYA,S.CURRY,N.P.FRANKS
REVDAT 3 13-DEC-23 1E7A 1 REMARK
REVDAT 2 24-FEB-09 1E7A 1 VERSN
REVDAT 1 17-JAN-01 1E7A 0
JRNL AUTH A.A.BHATTACHARYA,S.CURRY,N.P.FRANKS
JRNL TITL BINDING OF THE GENERAL ANESTHETICS PROPOFOL AND HALOTHANE TO
JRNL TITL 2 HUMAN SERUM ALBUMIN. HIGH RESOLUTION CRYSTAL STRUCTURES
JRNL REF J.BIOL.CHEM. V. 275 38731 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10940303
JRNL DOI 10.1074/JBC.M005460200
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 62859
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) : 0.248
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3143
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7223
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 386
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.42
REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.180 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.880 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.120 ; 2.500
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 : PFL.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : PFL.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED REFINEMENT WAS
REMARK 3 PERFORMED WITH MAX ALLOWABLE TEMPERATURE FACTOR OF 150
REMARK 4
REMARK 4 1E7A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1290005320.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-99
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 : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62870
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 29.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29600
REMARK 200 R SYM FOR SHELL (I) : 0.29600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: 1AO6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
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 400
REMARK 400 COMPOUND
REMARK 400 SERUM ALBUMIN, REGULATES THE COLLOIDAL OSMOTIC PRESSURE OF BLOOD
REMARK 400 IT BINDS TO WATER, CA++, NA+, K+, FATTY ACIDS, HORMONES,
REMARK 400 BILIRUBIN AND DRUGS
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 GLN A 33 CD OE1 NE2
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 GLU A 60 CG CD OE1 OE2
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 ARG A 81 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 TYR A 84 CG CD1 CD2 CE1 CE2 CZ OH
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 ARG A 117 CD NE CZ NH1 NH2
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 ARG A 209 CD NE CZ NH1 NH2
REMARK 470 GLU A 227 CG CD OE1 OE2
REMARK 470 GLU A 368 CG CD OE1 OE2
REMARK 470 LYS A 389 CD CE NZ
REMARK 470 GLN A 390 CG CD OE1 NE2
REMARK 470 GLN A 397 CG CD OE1 NE2
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 LYS A 436 CD CE NZ
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 LYS A 475 CE NZ
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 CG CD CE NZ
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 LYS A 560 CG CD CE NZ
REMARK 470 LYS A 574 CG CD CE NZ
REMARK 470 GLU B 60 CG CD OE1 OE2
REMARK 470 TYR B 84 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 86 CG CD OE1 OE2
REMARK 470 ARG B 114 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 117 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 128 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 ARG B 160 CZ NH1 NH2
REMARK 470 GLN B 170 CG CD OE1 NE2
REMARK 470 ARG B 186 CZ NH1 NH2
REMARK 470 LYS B 190 CE NZ
REMARK 470 GLU B 277 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 GLN B 459 CG CD OE1 NE2
REMARK 470 HIS B 510 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 536 CG CD CE NZ
REMARK 470 LYS B 538 CG CD CE NZ
REMARK 470 LYS B 541 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 570 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 CD ARG A 410 O HOH A 2035 1.97
REMARK 500 O GLU A 97 N ASN A 99 2.01
REMARK 500 O PRO A 366 N GLU A 368 2.05
REMARK 500 CG2 VAL B 433 CD2 TYR B 452 2.06
REMARK 500 O HOH B 2018 O HOH B 2048 2.07
REMARK 500 O HOH A 2018 O HOH A 2042 2.10
REMARK 500 O HOH B 2016 O HOH B 2019 2.17
REMARK 500 C GLU A 97 N ASN A 99 2.18
REMARK 500 CB SER B 579 O1 PFL B 4002 2.18
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 PRO A 118 C - N - CA ANGL. DEV. = 10.3 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 -71.14 -49.53
REMARK 500 LEU A 31 70.26 -107.86
REMARK 500 GLU A 57 29.78 -79.95
REMARK 500 SER A 58 0.82 -156.48
REMARK 500 ALA A 59 -92.34 -39.37
REMARK 500 GLU A 60 -75.44 -83.94
REMARK 500 CYS A 62 -17.21 -42.57
REMARK 500 CYS A 75 1.82 -62.77
REMARK 500 THR A 79 -4.63 -57.58
REMARK 500 GLN A 94 -148.89 -108.14
REMARK 500 PRO A 96 -29.21 -39.76
REMARK 500 GLU A 97 20.91 -169.77
REMARK 500 ARG A 98 4.55 -48.17
REMARK 500 ASN A 111 44.28 -79.87
REMARK 500 PRO A 113 152.90 -45.84
REMARK 500 TYR A 150 99.85 -61.16
REMARK 500 GLU A 167 -63.35 -94.61
REMARK 500 ALA A 171 -154.23 -76.66
REMARK 500 LEU A 178 -76.88 -80.53
REMARK 500 LEU A 179 -61.65 -15.70
REMARK 500 PRO A 180 -73.81 -44.66
REMARK 500 PHE A 223 72.18 -117.16
REMARK 500 ASN A 267 45.04 -93.99
REMARK 500 ILE A 271 -70.88 -112.04
REMARK 500 LYS A 276 -63.96 -27.67
REMARK 500 LEU A 283 -72.25 -30.64
REMARK 500 ALA A 300 -90.60 -44.30
REMARK 500 ASP A 365 87.08 -167.30
REMARK 500 PRO A 366 -91.71 -42.80
REMARK 500 HIS A 367 -22.82 -21.95
REMARK 500 GLU A 492 -99.41 -118.12
REMARK 500 HIS A 510 140.86 -13.35
REMARK 500 ASP A 512 -10.84 -40.15
REMARK 500 PRO A 537 -70.40 -48.26
REMARK 500 LYS A 538 -91.85 -55.11
REMARK 500 ALA A 539 106.00 -43.18
REMARK 500 THR A 540 106.72 -177.85
REMARK 500 LYS A 541 -49.91 -148.45
REMARK 500 GLU A 542 14.54 -150.67
REMARK 500 LEU B 31 75.39 -105.33
REMARK 500 PHE B 49 -17.13 -150.89
REMARK 500 THR B 52 2.19 -65.51
REMARK 500 VAL B 54 -93.76 -53.57
REMARK 500 GLU B 57 -102.45 -64.15
REMARK 500 SER B 58 63.44 -55.69
REMARK 500 GLU B 60 -84.84 -33.36
REMARK 500 CYS B 75 -3.61 -54.74
REMARK 500 VAL B 77 -11.49 -155.24
REMARK 500 GLU B 86 -7.90 -50.97
REMARK 500 ALA B 92 -9.64 -58.11
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 PFL A4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFL A4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFL B4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFL B4002
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: 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: 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 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1-24 IN P02768 ENTRY ARE SIGNAL SEQUENCE.
REMARK 999 RESIDUE 1 IN STRUCTURE COORDINATES IS EQUIVALENT
REMARK 999 OF RESIDUE 25 IN P02768.
DBREF 1E7A A 1 585 UNP P02768 ALBU_HUMAN 25 609
DBREF 1E7A 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 PFL A4001 13
HET PFL A4002 13
HET PFL B4001 13
HET PFL B4002 13
HETNAM PFL 2,6-BIS(1-METHYLETHYL)PHENOL
HETSYN PFL 2,6-DIISOPROPYLPHENOL; PROPOFOL
FORMUL 3 PFL 4(C12 H18 O)
FORMUL 7 HOH *120(H2 O)
HELIX 1 1 GLU A 6 GLY A 15 1 10
HELIX 2 2 LEU A 14 LEU A 31 1 18
HELIX 3 3 PRO A 35 ASP A 56 1 22
HELIX 4 4 SER A 65 THR A 79 1 15
HELIX 5 5 LEU A 80 GLY A 85 1 6
HELIX 6 6 GLU A 86 ALA A 92 1 7
HELIX 7 7 ASN A 99 HIS A 105 1 7
HELIX 8 8 GLU A 119 ASN A 130 1 12
HELIX 9 9 ASN A 130 ARG A 144 1 15
HELIX 10 10 TYR A 150 CYS A 169 1 20
HELIX 11 11 ASP A 173 GLY A 207 1 35
HELIX 12 12 GLY A 207 PHE A 223 1 17
HELIX 13 13 GLU A 227 GLY A 248 1 22
HELIX 14 14 ASP A 249 ASN A 267 1 19
HELIX 15 15 ASN A 267 SER A 272 1 6
HELIX 16 16 LEU A 275 GLU A 280 1 6
HELIX 17 17 PRO A 282 ALA A 291 1 10
HELIX 18 18 LEU A 305 VAL A 310 1 6
HELIX 19 19 ASP A 314 ALA A 322 1 9
HELIX 20 20 ALA A 322 ARG A 337 1 16
HELIX 21 21 SER A 342 ALA A 362 1 21
HELIX 22 22 ASP A 365 TYR A 370 1 6
HELIX 23 23 VAL A 373 GLY A 399 1 27
HELIX 24 24 LEU A 398 VAL A 415 1 18
HELIX 25 25 SER A 419 CYS A 438 1 20
HELIX 26 26 PRO A 441 THR A 467 1 27
HELIX 27 27 SER A 470 SER A 480 1 11
HELIX 28 28 ASN A 483 LEU A 491 1 9
HELIX 29 29 ASN A 503 PHE A 507 5 5
HELIX 30 30 HIS A 510 LEU A 516 5 7
HELIX 31 31 SER A 517 LYS A 536 1 20
HELIX 32 32 GLU A 542 ALA A 561 1 20
HELIX 33 33 THR A 566 ALA A 582 1 17
HELIX 34 34 SER B 5 GLY B 15 1 11
HELIX 35 35 GLY B 15 LEU B 31 1 17
HELIX 36 36 PRO B 35 LYS B 51 1 17
HELIX 37 37 SER B 65 THR B 79 1 15
HELIX 38 38 GLU B 86 ALA B 92 1 7
HELIX 39 39 PRO B 96 GLN B 104 1 9
HELIX 40 40 GLU B 119 ASN B 130 1 12
HELIX 41 41 ASN B 130 HIS B 146 1 17
HELIX 42 42 TYR B 150 CYS B 169 1 20
HELIX 43 43 ASP B 173 GLY B 207 1 35
HELIX 44 44 GLY B 207 PHE B 223 1 17
HELIX 45 45 GLU B 227 GLY B 248 1 22
HELIX 46 46 ASP B 249 ASN B 267 1 19
HELIX 47 47 ASN B 267 SER B 272 1 6
HELIX 48 48 LEU B 275 GLU B 280 5 6
HELIX 49 49 PRO B 282 ALA B 291 1 10
HELIX 50 50 LEU B 305 VAL B 310 1 6
HELIX 51 51 ASP B 314 ALA B 322 1 9
HELIX 52 52 ALA B 322 ARG B 337 1 16
HELIX 53 53 SER B 342 ALA B 363 1 22
HELIX 54 54 ASP B 365 TYR B 370 1 6
HELIX 55 55 VAL B 373 GLY B 399 1 27
HELIX 56 56 LEU B 398 VAL B 415 1 18
HELIX 57 57 SER B 419 CYS B 438 1 20
HELIX 58 58 PRO B 441 THR B 467 1 27
HELIX 59 59 SER B 470 SER B 480 1 11
HELIX 60 60 ASN B 483 LEU B 491 1 9
HELIX 61 61 HIS B 510 CYS B 514 5 5
HELIX 62 62 GLU B 518 LYS B 536 1 19
HELIX 63 63 GLU B 542 LYS B 560 1 19
HELIX 64 64 GLU B 565 ALA B 582 1 18
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.02
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.03
SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.05
SSBOND 4 CYS A 124 CYS A 169 1555 1555 2.02
SSBOND 5 CYS A 168 CYS A 177 1555 1555 2.04
SSBOND 6 CYS A 200 CYS A 246 1555 1555 2.05
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 2.04
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 2.06
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 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 1.97
SSBOND 24 CYS B 245 CYS B 253 1555 1555 1.93
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 2.05
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 1.23
SITE 1 AC1 8 ILE A 388 ASN A 391 LEU A 407 ARG A 410
SITE 2 AC1 8 LEU A 430 VAL A 433 GLY A 434 HOH A2036
SITE 1 AC2 3 PHE A 502 LEU A 532 SER A 579
SITE 1 AC3 5 PHE B 403 LEU B 407 ARG B 410 LEU B 430
SITE 2 AC3 5 LEU B 453
SITE 1 AC4 2 LEU B 532 SER B 579
CRYST1 55.400 55.610 120.500 81.11 90.57 65.50 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 0.018050 -0.008226 0.001639 0.00000
SCALE2 0.000000 0.019762 -0.003499 0.00000
SCALE3 0.000000 0.000000 0.008428 0.00000
MTRIX1 1 0.424100 0.905400 0.022400 -47.98370 1
MTRIX2 1 0.905500 -0.424300 0.008800 -34.02910 1
MTRIX3 1 0.017500 0.016500 -0.999700 58.08610 1
(ATOM LINES ARE NOT SHOWN.)
END