HEADER OXIDOREDUCTASE 30-MAY-08 3DAX
TITLE CRYSTAL STRUCTURE OF HUMAN CYP7A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 7A1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CHOLESTEROL 7-ALPHA-MONOOXYGENASE, CYPVII, CHOLESTEROL 7-
COMPND 5 ALPHA-HYDROXYLASE;
COMPND 6 EC: 1.14.13.17;
COMPND 7 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: CYP7A1, CYP7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS CYTOCHROME P450, CHOLESTEROL, CHOLESTEROL 7-ALPHA HYDROXYLASE,
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 3 CHOLESTEROL METABOLISM, ENDOPLASMIC RETICULUM, HEME, IRON, LIPID
KEYWDS 4 METABOLISM, MEMBRANE, METAL-BINDING, MICROSOME, MONOOXYGENASE, NADP,
KEYWDS 5 OXIDOREDUCTASE, POLYMORPHISM, STEROID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR N.V.STRUSHKEVICH,W.TEMPEL,L.DOMBROVSKI,A.DONG,P.LOPPNAU,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,M.WILKSTROM,A.BOCHKAREV,H.PARK,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 30-AUG-23 3DAX 1 REMARK
REVDAT 4 21-OCT-20 3DAX 1 REMARK
REVDAT 3 25-OCT-17 3DAX 1 REMARK
REVDAT 2 24-FEB-09 3DAX 1 VERSN
REVDAT 1 05-AUG-08 3DAX 0
JRNL AUTH N.V.STRUSHKEVICH,W.TEMPEL,L.DOMBROVSKI,A.DONG,P.LOPPNAU,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,M.WILKSTROM,
JRNL AUTH 3 A.BOCHKAREV,H.PARK
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CYP7A1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 63038
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.201
REMARK 3 FREE R VALUE TEST SET COUNT : 2018
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3645
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7455
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06100
REMARK 3 B22 (A**2) : 0.08100
REMARK 3 B33 (A**2) : -0.08100
REMARK 3 B12 (A**2) : -0.16200
REMARK 3 B13 (A**2) : -0.00700
REMARK 3 B23 (A**2) : 0.19000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.213
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.221
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7817 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5284 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10633 ; 1.288 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12872 ; 0.877 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 964 ; 5.969 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;35.131 ;23.704
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1314 ;14.595 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.185 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1156 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8671 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1619 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1571 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5138 ; 0.188 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3776 ; 0.178 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3968 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 215 ; 0.122 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 11 ; 0.098 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 34 ; 0.205 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.217 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4951 ; 2.526 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1901 ; 0.615 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7628 ; 3.606 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3364 ; 2.432 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2988 ; 3.393 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000047810.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-07; NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; NULL
REMARK 200 RADIATION SOURCE : NSLS; NULL
REMARK 200 BEAMLINE : X25; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96860; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65596
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR, MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2IAG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG400, 0.1M POTASSIUM CHLORIDE,
REMARK 280 0.1M TRISODIUM CITRATE, PH 5.5, VAPOR DIFFUSION, TEMPERATURE 291K
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
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL ASSEMBLY IS NOT KNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 MET A 18
REMARK 465 ALA A 19
REMARK 465 LYS A 20
REMARK 465 LYS A 21
REMARK 465 THR A 22
REMARK 465 SER A 23
REMARK 465 PRO A 155
REMARK 465 PRO A 156
REMARK 465 VAL A 157
REMARK 465 SER A 158
REMARK 465 SER A 159
REMARK 465 ASN A 160
REMARK 465 SER A 161
REMARK 465 LYS A 162
REMARK 465 THR A 163
REMARK 465 ALA A 164
REMARK 465 HIS A 506
REMARK 465 HIS A 507
REMARK 465 HIS A 508
REMARK 465 MET B 18
REMARK 465 ALA B 19
REMARK 465 LYS B 20
REMARK 465 LYS B 21
REMARK 465 THR B 22
REMARK 465 SER B 23
REMARK 465 PRO B 155
REMARK 465 PRO B 156
REMARK 465 VAL B 157
REMARK 465 SER B 158
REMARK 465 SER B 159
REMARK 465 ASN B 160
REMARK 465 SER B 161
REMARK 465 LYS B 162
REMARK 465 THR B 163
REMARK 465 HIS B 503
REMARK 465 HIS B 504
REMARK 465 HIS B 505
REMARK 465 HIS B 506
REMARK 465 HIS B 507
REMARK 465 HIS B 508
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 SER A 24 OG
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 36 CG OD1 ND2
REMARK 470 LYS A 62 CE NZ
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 LYS A 87 CD CE NZ
REMARK 470 HIS A 91 CG ND1 CD2 CE1 NE2
REMARK 470 ASN A 126 CG OD1 ND2
REMARK 470 LYS A 131 CD CE NZ
REMARK 470 GLU A 143 CD OE1 OE2
REMARK 470 GLU A 147 CD OE1 OE2
REMARK 470 ARG A 190 NE CZ NH1 NH2
REMARK 470 ARG A 194 NE CZ NH1 NH2
REMARK 470 GLN A 198 CG CD OE1 NE2
REMARK 470 LYS A 199 CD CE NZ
REMARK 470 ARG A 229 NE CZ NH1 NH2
REMARK 470 GLU A 245 CG CD OE1 OE2
REMARK 470 LYS A 249 CE NZ
REMARK 470 GLU A 255 CD OE1 OE2
REMARK 470 GLU A 306 CG CD OE1 OE2
REMARK 470 LYS A 309 CE NZ
REMARK 470 ARG A 317 NE CZ NH1 NH2
REMARK 470 LYS A 325 CG CD CE NZ
REMARK 470 GLU A 368 CG CD OE1 OE2
REMARK 470 GLU A 375 CD OE1 OE2
REMARK 470 GLU A 399 OE1 OE2
REMARK 470 GLU A 415 CG CD OE1 OE2
REMARK 470 LYS A 418 CG CD CE NZ
REMARK 470 THR A 442 OG1 CG2
REMARK 470 ASN B 36 CG OD1 ND2
REMARK 470 LYS B 62 CE NZ
REMARK 470 LYS B 87 CE NZ
REMARK 470 HIS B 91 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 98 CE NZ
REMARK 470 ASN B 126 CG OD1 ND2
REMARK 470 LYS B 131 CG CD CE NZ
REMARK 470 ARG B 190 NE CZ NH1 NH2
REMARK 470 ARG B 194 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 199 CG CD CE NZ
REMARK 470 LYS B 214 CE NZ
REMARK 470 ARG B 229 NE CZ NH1 NH2
REMARK 470 GLU B 245 CG CD OE1 OE2
REMARK 470 GLU B 306 CD OE1 OE2
REMARK 470 LYS B 309 CE NZ
REMARK 470 GLU B 313 CG CD OE1 OE2
REMARK 470 ARG B 317 NE CZ NH1 NH2
REMARK 470 VAL B 326 CG1 CG2
REMARK 470 GLU B 375 CG CD OE1 OE2
REMARK 470 GLU B 399 CG CD OE1 OE2
REMARK 470 GLU B 415 CG CD OE1 OE2
REMARK 470 LYS B 418 CD CE NZ
REMARK 470 THR B 442 OG1 CG2
REMARK 470 LYS B 498 CG CD CE NZ
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 ALA A 359 56.50 -142.03
REMARK 500 LYS A 475 150.04 -49.99
REMARK 500 HIS B 91 85.00 -65.30
REMARK 500 ALA B 359 55.99 -142.90
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 HEM A 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 444 SG
REMARK 620 2 HEM A 601 NA 98.0
REMARK 620 3 HEM A 601 NB 93.3 90.6
REMARK 620 4 HEM A 601 NC 91.7 170.0 86.5
REMARK 620 5 HEM A 601 ND 95.1 89.1 171.6 92.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 444 SG
REMARK 620 2 HEM B 601 NA 98.0
REMARK 620 3 HEM B 601 NB 94.0 92.6
REMARK 620 4 HEM B 601 NC 91.6 170.2 88.9
REMARK 620 5 HEM B 601 ND 95.3 86.6 170.7 90.3
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 HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 2
DBREF 3DAX A 25 503 UNP P22680 CP7A1_HUMAN 25 503
DBREF 3DAX B 25 503 UNP P22680 CP7A1_HUMAN 25 503
SEQADV 3DAX MET A 18 UNP P22680 EXPRESSION TAG
SEQADV 3DAX ALA A 19 UNP P22680 EXPRESSION TAG
SEQADV 3DAX LYS A 20 UNP P22680 EXPRESSION TAG
SEQADV 3DAX LYS A 21 UNP P22680 EXPRESSION TAG
SEQADV 3DAX THR A 22 UNP P22680 EXPRESSION TAG
SEQADV 3DAX SER A 23 UNP P22680 EXPRESSION TAG
SEQADV 3DAX SER A 24 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS A 504 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS A 505 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS A 506 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS A 507 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS A 508 UNP P22680 EXPRESSION TAG
SEQADV 3DAX MET B 18 UNP P22680 EXPRESSION TAG
SEQADV 3DAX ALA B 19 UNP P22680 EXPRESSION TAG
SEQADV 3DAX LYS B 20 UNP P22680 EXPRESSION TAG
SEQADV 3DAX LYS B 21 UNP P22680 EXPRESSION TAG
SEQADV 3DAX THR B 22 UNP P22680 EXPRESSION TAG
SEQADV 3DAX SER B 23 UNP P22680 EXPRESSION TAG
SEQADV 3DAX SER B 24 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS B 504 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS B 505 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS B 506 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS B 507 UNP P22680 EXPRESSION TAG
SEQADV 3DAX HIS B 508 UNP P22680 EXPRESSION TAG
SEQRES 1 A 491 MET ALA LYS LYS THR SER SER ARG ARG ARG GLN THR GLY
SEQRES 2 A 491 GLU PRO PRO LEU GLU ASN GLY LEU ILE PRO TYR LEU GLY
SEQRES 3 A 491 CYS ALA LEU GLN PHE GLY ALA ASN PRO LEU GLU PHE LEU
SEQRES 4 A 491 ARG ALA ASN GLN ARG LYS HIS GLY HIS VAL PHE THR CYS
SEQRES 5 A 491 LYS LEU MET GLY LYS TYR VAL HIS PHE ILE THR ASN PRO
SEQRES 6 A 491 LEU SER TYR HIS LYS VAL LEU CYS HIS GLY LYS TYR PHE
SEQRES 7 A 491 ASP TRP LYS LYS PHE HIS PHE ALA THR SER ALA LYS ALA
SEQRES 8 A 491 PHE GLY HIS ARG SER ILE ASP PRO MET ASP GLY ASN THR
SEQRES 9 A 491 THR GLU ASN ILE ASN ASP THR PHE ILE LYS THR LEU GLN
SEQRES 10 A 491 GLY HIS ALA LEU ASN SER LEU THR GLU SER MET MET GLU
SEQRES 11 A 491 ASN LEU GLN ARG ILE MET ARG PRO PRO VAL SER SER ASN
SEQRES 12 A 491 SER LYS THR ALA ALA TRP VAL THR GLU GLY MET TYR SER
SEQRES 13 A 491 PHE CYS TYR ARG VAL MET PHE GLU ALA GLY TYR LEU THR
SEQRES 14 A 491 ILE PHE GLY ARG ASP LEU THR ARG ARG ASP THR GLN LYS
SEQRES 15 A 491 ALA HIS ILE LEU ASN ASN LEU ASP ASN PHE LYS GLN PHE
SEQRES 16 A 491 ASP LYS VAL PHE PRO ALA LEU VAL ALA GLY LEU PRO ILE
SEQRES 17 A 491 HIS MET PHE ARG THR ALA HIS ASN ALA ARG GLU LYS LEU
SEQRES 18 A 491 ALA GLU SER LEU ARG HIS GLU ASN LEU GLN LYS ARG GLU
SEQRES 19 A 491 SER ILE SER GLU LEU ILE SER LEU ARG MET PHE LEU ASN
SEQRES 20 A 491 ASP THR LEU SER THR PHE ASP ASP LEU GLU LYS ALA LYS
SEQRES 21 A 491 THR HIS LEU VAL VAL LEU TRP ALA SER GLN ALA ASN THR
SEQRES 22 A 491 ILE PRO ALA THR PHE TRP SER LEU PHE GLN MET ILE ARG
SEQRES 23 A 491 ASN PRO GLU ALA MET LYS ALA ALA THR GLU GLU VAL LYS
SEQRES 24 A 491 ARG THR LEU GLU ASN ALA GLY GLN LYS VAL SER LEU GLU
SEQRES 25 A 491 GLY ASN PRO ILE CYS LEU SER GLN ALA GLU LEU ASN ASP
SEQRES 26 A 491 LEU PRO VAL LEU ASP SER ILE ILE LYS GLU SER LEU ARG
SEQRES 27 A 491 LEU SER SER ALA SER LEU ASN ILE ARG THR ALA LYS GLU
SEQRES 28 A 491 ASP PHE THR LEU HIS LEU GLU ASP GLY SER TYR ASN ILE
SEQRES 29 A 491 ARG LYS ASP ASP ILE ILE ALA LEU TYR PRO GLN LEU MET
SEQRES 30 A 491 HIS LEU ASP PRO GLU ILE TYR PRO ASP PRO LEU THR PHE
SEQRES 31 A 491 LYS TYR ASP ARG TYR LEU ASP GLU ASN GLY LYS THR LYS
SEQRES 32 A 491 THR THR PHE TYR CYS ASN GLY LEU LYS LEU LYS TYR TYR
SEQRES 33 A 491 TYR MET PRO PHE GLY SER GLY ALA THR ILE CYS PRO GLY
SEQRES 34 A 491 ARG LEU PHE ALA ILE HIS GLU ILE LYS GLN PHE LEU ILE
SEQRES 35 A 491 LEU MET LEU SER TYR PHE GLU LEU GLU LEU ILE GLU GLY
SEQRES 36 A 491 GLN ALA LYS CYS PRO PRO LEU ASP GLN SER ARG ALA GLY
SEQRES 37 A 491 LEU GLY ILE LEU PRO PRO LEU ASN ASP ILE GLU PHE LYS
SEQRES 38 A 491 TYR LYS PHE LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 491 MET ALA LYS LYS THR SER SER ARG ARG ARG GLN THR GLY
SEQRES 2 B 491 GLU PRO PRO LEU GLU ASN GLY LEU ILE PRO TYR LEU GLY
SEQRES 3 B 491 CYS ALA LEU GLN PHE GLY ALA ASN PRO LEU GLU PHE LEU
SEQRES 4 B 491 ARG ALA ASN GLN ARG LYS HIS GLY HIS VAL PHE THR CYS
SEQRES 5 B 491 LYS LEU MET GLY LYS TYR VAL HIS PHE ILE THR ASN PRO
SEQRES 6 B 491 LEU SER TYR HIS LYS VAL LEU CYS HIS GLY LYS TYR PHE
SEQRES 7 B 491 ASP TRP LYS LYS PHE HIS PHE ALA THR SER ALA LYS ALA
SEQRES 8 B 491 PHE GLY HIS ARG SER ILE ASP PRO MET ASP GLY ASN THR
SEQRES 9 B 491 THR GLU ASN ILE ASN ASP THR PHE ILE LYS THR LEU GLN
SEQRES 10 B 491 GLY HIS ALA LEU ASN SER LEU THR GLU SER MET MET GLU
SEQRES 11 B 491 ASN LEU GLN ARG ILE MET ARG PRO PRO VAL SER SER ASN
SEQRES 12 B 491 SER LYS THR ALA ALA TRP VAL THR GLU GLY MET TYR SER
SEQRES 13 B 491 PHE CYS TYR ARG VAL MET PHE GLU ALA GLY TYR LEU THR
SEQRES 14 B 491 ILE PHE GLY ARG ASP LEU THR ARG ARG ASP THR GLN LYS
SEQRES 15 B 491 ALA HIS ILE LEU ASN ASN LEU ASP ASN PHE LYS GLN PHE
SEQRES 16 B 491 ASP LYS VAL PHE PRO ALA LEU VAL ALA GLY LEU PRO ILE
SEQRES 17 B 491 HIS MET PHE ARG THR ALA HIS ASN ALA ARG GLU LYS LEU
SEQRES 18 B 491 ALA GLU SER LEU ARG HIS GLU ASN LEU GLN LYS ARG GLU
SEQRES 19 B 491 SER ILE SER GLU LEU ILE SER LEU ARG MET PHE LEU ASN
SEQRES 20 B 491 ASP THR LEU SER THR PHE ASP ASP LEU GLU LYS ALA LYS
SEQRES 21 B 491 THR HIS LEU VAL VAL LEU TRP ALA SER GLN ALA ASN THR
SEQRES 22 B 491 ILE PRO ALA THR PHE TRP SER LEU PHE GLN MET ILE ARG
SEQRES 23 B 491 ASN PRO GLU ALA MET LYS ALA ALA THR GLU GLU VAL LYS
SEQRES 24 B 491 ARG THR LEU GLU ASN ALA GLY GLN LYS VAL SER LEU GLU
SEQRES 25 B 491 GLY ASN PRO ILE CYS LEU SER GLN ALA GLU LEU ASN ASP
SEQRES 26 B 491 LEU PRO VAL LEU ASP SER ILE ILE LYS GLU SER LEU ARG
SEQRES 27 B 491 LEU SER SER ALA SER LEU ASN ILE ARG THR ALA LYS GLU
SEQRES 28 B 491 ASP PHE THR LEU HIS LEU GLU ASP GLY SER TYR ASN ILE
SEQRES 29 B 491 ARG LYS ASP ASP ILE ILE ALA LEU TYR PRO GLN LEU MET
SEQRES 30 B 491 HIS LEU ASP PRO GLU ILE TYR PRO ASP PRO LEU THR PHE
SEQRES 31 B 491 LYS TYR ASP ARG TYR LEU ASP GLU ASN GLY LYS THR LYS
SEQRES 32 B 491 THR THR PHE TYR CYS ASN GLY LEU LYS LEU LYS TYR TYR
SEQRES 33 B 491 TYR MET PRO PHE GLY SER GLY ALA THR ILE CYS PRO GLY
SEQRES 34 B 491 ARG LEU PHE ALA ILE HIS GLU ILE LYS GLN PHE LEU ILE
SEQRES 35 B 491 LEU MET LEU SER TYR PHE GLU LEU GLU LEU ILE GLU GLY
SEQRES 36 B 491 GLN ALA LYS CYS PRO PRO LEU ASP GLN SER ARG ALA GLY
SEQRES 37 B 491 LEU GLY ILE LEU PRO PRO LEU ASN ASP ILE GLU PHE LYS
SEQRES 38 B 491 TYR LYS PHE LYS HIS HIS HIS HIS HIS HIS
HET HEM A 601 43
HET UNX A 1 1
HET HEM B 601 43
HET UNX B 2 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 UNX 2(X)
FORMUL 7 HOH *130(H2 O)
HELIX 1 1 ALA A 45 GLY A 49 5 5
HELIX 2 2 ASN A 51 GLY A 64 1 14
HELIX 3 3 ASN A 81 SER A 84 5 4
HELIX 4 4 TYR A 85 CYS A 90 1 6
HELIX 5 5 LYS A 98 GLY A 110 1 13
HELIX 6 6 ASP A 115 GLY A 119 5 5
HELIX 7 7 ASN A 124 GLN A 134 1 11
HELIX 8 8 GLN A 134 ARG A 154 1 21
HELIX 9 9 MET A 171 GLY A 189 1 19
HELIX 10 10 ARG A 194 ASP A 196 5 3
HELIX 11 11 THR A 197 ALA A 221 1 25
HELIX 12 12 PRO A 224 MET A 227 5 4
HELIX 13 13 PHE A 228 LEU A 242 1 15
HELIX 14 14 ARG A 243 GLN A 248 1 6
HELIX 15 15 SER A 254 SER A 268 1 15
HELIX 16 16 ASP A 271 ALA A 288 1 18
HELIX 17 17 ASN A 289 ASN A 304 1 16
HELIX 18 18 ASN A 304 ASN A 321 1 18
HELIX 19 19 SER A 336 ASP A 342 1 7
HELIX 20 20 LEU A 343 SER A 357 1 15
HELIX 21 21 PRO A 391 LEU A 396 1 6
HELIX 22 22 GLY A 446 TYR A 464 1 19
HELIX 23 23 ASP A 480 ALA A 484 5 5
HELIX 24 24 ALA B 45 GLY B 49 5 5
HELIX 25 25 ASN B 51 GLY B 64 1 14
HELIX 26 26 ASN B 81 LEU B 83 5 3
HELIX 27 27 SER B 84 CYS B 90 1 7
HELIX 28 28 LYS B 98 GLY B 110 1 13
HELIX 29 29 ASP B 115 GLY B 119 5 5
HELIX 30 30 ASN B 124 GLN B 134 1 11
HELIX 31 31 GLY B 135 ARG B 154 1 20
HELIX 32 32 MET B 171 GLY B 189 1 19
HELIX 33 33 ARG B 194 ASP B 196 5 3
HELIX 34 34 THR B 197 VAL B 215 1 19
HELIX 35 35 VAL B 215 ALA B 221 1 7
HELIX 36 36 PRO B 224 MET B 227 5 4
HELIX 37 37 PHE B 228 LEU B 242 1 15
HELIX 38 38 ARG B 243 GLN B 248 1 6
HELIX 39 39 SER B 254 SER B 268 1 15
HELIX 40 40 ASP B 271 ALA B 288 1 18
HELIX 41 41 ASN B 289 ASN B 304 1 16
HELIX 42 42 ASN B 304 ALA B 322 1 19
HELIX 43 43 SER B 336 ASP B 342 1 7
HELIX 44 44 LEU B 343 SER B 357 1 15
HELIX 45 45 PRO B 391 LEU B 396 1 6
HELIX 46 46 GLY B 446 TYR B 464 1 19
HELIX 47 47 ASP B 480 ALA B 484 5 5
SHEET 1 A 6 LEU A 34 ILE A 39 0
SHEET 2 A 6 VAL A 66 LEU A 71 1 O THR A 68 N GLU A 35
SHEET 3 A 6 LYS A 74 ILE A 79 -1 O VAL A 76 N CYS A 69
SHEET 4 A 6 ILE A 386 LEU A 389 1 O ILE A 386 N HIS A 77
SHEET 5 A 6 ASN A 362 ALA A 366 -1 N ARG A 364 O ILE A 387
SHEET 6 A 6 PHE A 95 ASP A 96 -1 N ASP A 96 O THR A 365
SHEET 1 B 3 VAL A 167 GLY A 170 0
SHEET 2 B 3 GLU A 496 PHE A 501 -1 O TYR A 499 N VAL A 167
SHEET 3 B 3 PHE A 465 LEU A 469 -1 N GLU A 468 O LYS A 498
SHEET 1 C 2 SER A 358 SER A 360 0
SHEET 2 C 2 LEU A 486 ILE A 488 -1 O GLY A 487 N ALA A 359
SHEET 1 D 2 PHE A 370 LEU A 374 0
SHEET 2 D 2 GLY A 377 ILE A 381 -1 O ILE A 381 N PHE A 370
SHEET 1 E 2 TYR A 424 CYS A 425 0
SHEET 2 E 2 LEU A 428 LYS A 429 -1 O LEU A 428 N CYS A 425
SHEET 1 F 2 GLY A 438 SER A 439 0
SHEET 2 F 2 THR A 442 ILE A 443 -1 O THR A 442 N SER A 439
SHEET 1 G 6 LEU B 34 ILE B 39 0
SHEET 2 G 6 VAL B 66 LEU B 71 1 O THR B 68 N GLU B 35
SHEET 3 G 6 LYS B 74 ILE B 79 -1 O PHE B 78 N PHE B 67
SHEET 4 G 6 ILE B 386 LEU B 389 1 O ALA B 388 N HIS B 77
SHEET 5 G 6 ASN B 362 ALA B 366 -1 N ARG B 364 O ILE B 387
SHEET 6 G 6 PHE B 95 ASP B 96 -1 N ASP B 96 O THR B 365
SHEET 1 H 3 VAL B 167 GLY B 170 0
SHEET 2 H 3 GLU B 496 PHE B 501 -1 O TYR B 499 N VAL B 167
SHEET 3 H 3 PHE B 465 LEU B 469 -1 N GLU B 466 O LYS B 500
SHEET 1 I 2 SER B 358 SER B 360 0
SHEET 2 I 2 LEU B 486 ILE B 488 -1 O GLY B 487 N ALA B 359
SHEET 1 J 2 PHE B 370 LEU B 374 0
SHEET 2 J 2 GLY B 377 ILE B 381 -1 O GLY B 377 N LEU B 374
SHEET 1 K 2 TYR B 424 CYS B 425 0
SHEET 2 K 2 LEU B 428 LYS B 429 -1 O LEU B 428 N CYS B 425
SHEET 1 L 2 GLY B 438 SER B 439 0
SHEET 2 L 2 THR B 442 ILE B 443 -1 O THR B 442 N SER B 439
LINK SG CYS A 444 FE HEM A 601 1555 1555 2.35
LINK SG CYS B 444 FE HEM B 601 1555 1555 2.36
SITE 1 AC1 16 HIS A 101 PHE A 129 ALA A 285 SER A 286
SITE 2 AC1 16 ASN A 289 THR A 290 ALA A 293 SER A 360
SITE 3 AC1 16 PRO A 436 PHE A 437 THR A 442 CYS A 444
SITE 4 AC1 16 PRO A 445 ALA A 450 GLU A 453 HOH A 659
SITE 1 AC2 14 HIS B 101 PHE B 129 ALA B 285 ASN B 289
SITE 2 AC2 14 THR B 290 ALA B 293 SER B 360 PRO B 436
SITE 3 AC2 14 PHE B 437 THR B 442 CYS B 444 PRO B 445
SITE 4 AC2 14 ALA B 450 GLU B 453
SITE 1 AC3 2 ALA A 285 ASN A 289
SITE 1 AC4 2 ALA B 285 ASN B 289
CRYST1 55.339 80.159 84.937 64.36 75.23 72.17 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 0.018070 -0.005812 -0.002739 0.00000
SCALE2 0.000000 0.013105 -0.005470 0.00000
SCALE3 0.000000 0.000000 0.013194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
