HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 01-MAY-18 6DA3
TITLE HUMAN CYP3A4 BOUND TO AN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 3A4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 23-503;
COMPND 5 SYNONYM: 1,8-CINEOLE 2-EXO-MONOOXYGENASE,ALBENDAZOLE MONOOXYGENASE,
COMPND 6 ALBENDAZOLE SULFOXIDASE,CYPIIIA3,CYPIIIA4,CHOLESTEROL 25-HYDROXYLASE,
COMPND 7 CYTOCHROME P450 3A3,CYTOCHROME P450 HLP,CYTOCHROME P450 NF-25,
COMPND 8 CYTOCHROME P450-PCN1,NIFEDIPINE OXIDASE,QUININE 3-MONOOXYGENASE,
COMPND 9 TAUROCHENODEOXYCHOLATE 6-ALPHA-HYDROXYLASE;
COMPND 10 EC: 1.14.14.-,1.14.14.56,1.14.14.55;
COMPND 11 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: CYP3A4, CYP3A3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCWORI
KEYWDS OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR I.F.SEVRIOUKOVA
REVDAT 5 04-OCT-23 6DA3 1 REMARK
REVDAT 4 18-DEC-19 6DA3 1 REMARK
REVDAT 3 12-JUN-19 6DA3 1 JRNL
REVDAT 2 01-MAY-19 6DA3 1 JRNL
REVDAT 1 03-APR-19 6DA3 0
JRNL AUTH E.R.SAMUELS,I.SEVRIOUKOVA
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS OF RATIONALLY DESIGNED
JRNL TITL 2 RITONAVIR ANALOGUES: IMPACT OF SIDE-GROUP STEREOCHEMISTRY,
JRNL TITL 3 HEADGROUP SPACING, AND BACKBONE COMPOSITION ON THE
JRNL TITL 4 INTERACTION WITH CYP3A4.
JRNL REF BIOCHEMISTRY V. 58 2077 2019
JRNL REFN ISSN 0006-2960
JRNL PMID 30912932
JRNL DOI 10.1021/ACS.BIOCHEM.9B00156
REMARK 2
REMARK 2 RESOLUTION. 2.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
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) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 19558
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 948
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 51.0318 - 4.5328 0.91 2666 146 0.1673 0.2177
REMARK 3 2 4.5328 - 3.5981 0.94 2688 117 0.2007 0.2759
REMARK 3 3 3.5981 - 3.1433 0.95 2657 147 0.2299 0.3275
REMARK 3 4 3.1433 - 2.8560 0.97 2701 145 0.2566 0.3319
REMARK 3 5 2.8560 - 2.6513 0.92 2560 113 0.2810 0.3588
REMARK 3 6 2.6513 - 2.4950 0.95 2648 145 0.3035 0.3927
REMARK 3 7 2.4950 - 2.3700 0.98 2690 135 0.3454 0.4095
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.790
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 : 0.009 3825
REMARK 3 ANGLE : 1.106 5194
REMARK 3 CHIRALITY : 0.057 574
REMARK 3 PLANARITY : 0.007 651
REMARK 3 DIHEDRAL : 14.047 2319
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0948 -23.6518 -13.0223
REMARK 3 T TENSOR
REMARK 3 T11: 0.4850 T22: 0.6638
REMARK 3 T33: 0.5830 T12: -0.0331
REMARK 3 T13: 0.0235 T23: -0.0939
REMARK 3 L TENSOR
REMARK 3 L11: 3.0594 L22: 5.4429
REMARK 3 L33: 3.0368 L12: -2.0910
REMARK 3 L13: -1.0314 L23: 1.4100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: 0.3891 S13: -0.2117
REMARK 3 S21: 0.2664 S22: -0.0359 S23: -0.2406
REMARK 3 S31: 0.2664 S32: -0.0022 S33: 0.0302
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 6DA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 103
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19595
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 79.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 1.27800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5VCC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, SODIUM MALONATE, PH 7.0,
REMARK 280 MICROBATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.44450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.02000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.52000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.44450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.02000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.52000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.44450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.02000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.52000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.44450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.02000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.52000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 1
REMARK 465 ALA A 2
REMARK 465 TYR A 23
REMARK 465 LEU A 24
REMARK 465 TYR A 25
REMARK 465 GLY A 26
REMARK 465 ASN A 198
REMARK 465 LEU A 211
REMARK 465 ARG A 212
REMARK 465 PHE A 213
REMARK 465 ASP A 214
REMARK 465 PHE A 215
REMARK 465 LEU A 216
REMARK 465 ASP A 217
REMARK 465 GLU A 262
REMARK 465 ASP A 263
REMARK 465 THR A 264
REMARK 465 GLN A 265
REMARK 465 LYS A 266
REMARK 465 HIS A 267
REMARK 465 ARG A 268
REMARK 465 SER A 281
REMARK 465 LYS A 282
REMARK 465 GLU A 283
REMARK 465 THR A 284
REMARK 465 GLU A 285
REMARK 465 ASP A 497
REMARK 465 GLY A 498
REMARK 465 THR A 499
REMARK 465 VAL A 500
REMARK 465 SER A 501
REMARK 465 GLY A 502
REMARK 465 ALA A 503
REMARK 465 HIS A 504
REMARK 465 HIS A 505
REMARK 465 HIS A 506
REMARK 465 HIS A 507
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 PHE A 46 -59.53 70.03
REMARK 500 VAL A 101 -58.24 -125.73
REMARK 500 PHE A 102 68.40 -101.69
REMARK 500 ASP A 123 -128.69 48.43
REMARK 500 PHE A 137 30.78 -93.70
REMARK 500 GLN A 200 49.51 -75.15
REMARK 500 PRO A 202 -9.84 -48.37
REMARK 500 PRO A 242 108.89 -33.99
REMARK 500 TYR A 307 -66.95 -101.37
REMARK 500 MET A 371 -59.63 68.99
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 442 SG
REMARK 620 2 HEM A 601 NA 98.2
REMARK 620 3 HEM A 601 NB 88.9 87.7
REMARK 620 4 HEM A 601 NC 88.1 173.6 93.9
REMARK 620 5 HEM A 601 ND 95.1 93.2 175.7 84.7
REMARK 620 6 G0D A 602 N26 168.7 88.2 82.0 85.9 93.9
REMARK 620 N 1 2 3 4 5
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 G0D A 602
DBREF 6DA3 A 23 503 UNP P08684 CP3A4_HUMAN 23 503
SEQADV 6DA3 MET A 1 UNP P08684 INITIATING METHIONINE
SEQADV 6DA3 ALA A 2 UNP P08684 EXPRESSION TAG
SEQADV 6DA3 HIS A 504 UNP P08684 EXPRESSION TAG
SEQADV 6DA3 HIS A 505 UNP P08684 EXPRESSION TAG
SEQADV 6DA3 HIS A 506 UNP P08684 EXPRESSION TAG
SEQADV 6DA3 HIS A 507 UNP P08684 EXPRESSION TAG
SEQRES 1 A 487 MET ALA TYR LEU TYR GLY THR HIS SER HIS GLY LEU PHE
SEQRES 2 A 487 LYS LYS LEU GLY ILE PRO GLY PRO THR PRO LEU PRO PHE
SEQRES 3 A 487 LEU GLY ASN ILE LEU SER TYR HIS LYS GLY PHE CYS MET
SEQRES 4 A 487 PHE ASP MET GLU CYS HIS LYS LYS TYR GLY LYS VAL TRP
SEQRES 5 A 487 GLY PHE TYR ASP GLY GLN GLN PRO VAL LEU ALA ILE THR
SEQRES 6 A 487 ASP PRO ASP MET ILE LYS THR VAL LEU VAL LYS GLU CYS
SEQRES 7 A 487 TYR SER VAL PHE THR ASN ARG ARG PRO PHE GLY PRO VAL
SEQRES 8 A 487 GLY PHE MET LYS SER ALA ILE SER ILE ALA GLU ASP GLU
SEQRES 9 A 487 GLU TRP LYS ARG LEU ARG SER LEU LEU SER PRO THR PHE
SEQRES 10 A 487 THR SER GLY LYS LEU LYS GLU MET VAL PRO ILE ILE ALA
SEQRES 11 A 487 GLN TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU
SEQRES 12 A 487 ALA GLU THR GLY LYS PRO VAL THR LEU LYS ASP VAL PHE
SEQRES 13 A 487 GLY ALA TYR SER MET ASP VAL ILE THR SER THR SER PHE
SEQRES 14 A 487 GLY VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO
SEQRES 15 A 487 PHE VAL GLU ASN THR LYS LYS LEU LEU ARG PHE ASP PHE
SEQRES 16 A 487 LEU ASP PRO PHE PHE LEU SER ILE THR VAL PHE PRO PHE
SEQRES 17 A 487 LEU ILE PRO ILE LEU GLU VAL LEU ASN ILE CYS VAL PHE
SEQRES 18 A 487 PRO ARG GLU VAL THR ASN PHE LEU ARG LYS SER VAL LYS
SEQRES 19 A 487 ARG MET LYS GLU SER ARG LEU GLU ASP THR GLN LYS HIS
SEQRES 20 A 487 ARG VAL ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN
SEQRES 21 A 487 SER LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU
SEQRES 22 A 487 GLU LEU VAL ALA GLN SER ILE ILE PHE ILE PHE ALA GLY
SEQRES 23 A 487 TYR GLU THR THR SER SER VAL LEU SER PHE ILE MET TYR
SEQRES 24 A 487 GLU LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN
SEQRES 25 A 487 GLU GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO
SEQRES 26 A 487 THR TYR ASP THR VAL LEU GLN MET GLU TYR LEU ASP MET
SEQRES 27 A 487 VAL VAL ASN GLU THR LEU ARG LEU PHE PRO ILE ALA MET
SEQRES 28 A 487 ARG LEU GLU ARG VAL CYS LYS LYS ASP VAL GLU ILE ASN
SEQRES 29 A 487 GLY MET PHE ILE PRO LYS GLY VAL VAL VAL MET ILE PRO
SEQRES 30 A 487 SER TYR ALA LEU HIS ARG ASP PRO LYS TYR TRP THR GLU
SEQRES 31 A 487 PRO GLU LYS PHE LEU PRO GLU ARG PHE SER LYS LYS ASN
SEQRES 32 A 487 LYS ASP ASN ILE ASP PRO TYR ILE TYR THR PRO PHE GLY
SEQRES 33 A 487 SER GLY PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU
SEQRES 34 A 487 MET ASN MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN
SEQRES 35 A 487 PHE SER PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU
SEQRES 36 A 487 LYS LEU SER LEU GLY GLY LEU LEU GLN PRO GLU LYS PRO
SEQRES 37 A 487 VAL VAL LEU LYS VAL GLU SER ARG ASP GLY THR VAL SER
SEQRES 38 A 487 GLY ALA HIS HIS HIS HIS
HET HEM A 601 43
HET G0D A 602 36
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM G0D TERT-BUTYL [(2R)-1-{[(2R)-1-OXO-3-PHENYL-1-{[(PYRIDIN-
HETNAM 2 G0D 3-YL)METHYL]AMINO}PROPAN-2-YL]SULFANYL}-3-
HETNAM 3 G0D PHENYLPROPAN-2-YL]CARBAMATE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 G0D C29 H35 N3 O3 S
FORMUL 4 HOH *8(H2 O)
HELIX 1 AA1 HIS A 28 HIS A 30 5 3
HELIX 2 AA2 GLY A 31 LEU A 36 1 6
HELIX 3 AA3 ASN A 49 HIS A 54 5 6
HELIX 4 AA4 LYS A 55 GLY A 69 1 15
HELIX 5 AA5 ASP A 86 VAL A 95 1 10
HELIX 6 AA6 VAL A 111 ALA A 117 5 7
HELIX 7 AA7 GLU A 122 SER A 134 1 13
HELIX 8 AA8 PRO A 135 PHE A 137 5 3
HELIX 9 AA9 THR A 138 GLU A 165 1 28
HELIX 10 AB1 LEU A 172 GLY A 190 1 19
HELIX 11 AB2 PHE A 219 PHE A 226 1 8
HELIX 12 AB3 LEU A 229 VAL A 235 1 7
HELIX 13 AB4 PRO A 242 LEU A 261 1 20
HELIX 14 AB5 ASP A 270 ASP A 277 1 8
HELIX 15 AB6 SER A 291 GLY A 306 1 16
HELIX 16 AB7 TYR A 307 THR A 323 1 17
HELIX 17 AB8 HIS A 324 LEU A 339 1 16
HELIX 18 AB9 THR A 346 GLN A 352 1 7
HELIX 19 AC1 MET A 353 PHE A 367 1 15
HELIX 20 AC2 PRO A 397 ARG A 403 1 7
HELIX 21 AC3 LEU A 415 SER A 420 5 6
HELIX 22 AC4 GLY A 444 ASN A 462 1 19
SHEET 1 AA1 4 VAL A 71 ASP A 76 0
SHEET 2 AA1 4 GLN A 79 ILE A 84 -1 O VAL A 81 N PHE A 74
SHEET 3 AA1 4 VAL A 393 ILE A 396 1 O VAL A 393 N LEU A 82
SHEET 4 AA1 4 LEU A 373 VAL A 376 -1 N LEU A 373 O ILE A 396
SHEET 1 AA2 3 VAL A 170 THR A 171 0
SHEET 2 AA2 3 VAL A 490 SER A 495 -1 O LEU A 491 N VAL A 170
SHEET 3 AA2 3 PHE A 463 PRO A 467 -1 N LYS A 466 O LYS A 492
SHEET 1 AA3 2 VAL A 381 GLU A 382 0
SHEET 2 AA3 2 PHE A 387 ILE A 388 -1 O ILE A 388 N VAL A 381
LINK SG CYS A 442 FE HEM A 601 1555 1555 2.31
LINK FE HEM A 601 N26 G0D A 602 1555 1555 2.26
CISPEP 1 THR A 27 HIS A 28 0 -0.36
CISPEP 2 GLY A 109 PRO A 110 0 -2.08
CISPEP 3 ILE A 473 PRO A 474 0 -0.94
SITE 1 AC1 22 ARG A 105 ILE A 118 TRP A 126 ARG A 130
SITE 2 AC1 22 PHE A 137 PHE A 302 ALA A 305 GLY A 306
SITE 3 AC1 22 VAL A 313 ALA A 370 LEU A 373 ARG A 375
SITE 4 AC1 22 PRO A 434 PHE A 435 GLY A 436 SER A 437
SITE 5 AC1 22 ARG A 440 ASN A 441 CYS A 442 ILE A 443
SITE 6 AC1 22 ALA A 448 G0D A 602
SITE 1 AC2 8 PHE A 108 SER A 119 PHE A 241 ILE A 301
SITE 2 AC2 8 PHE A 304 ALA A 305 THR A 309 HEM A 601
CRYST1 76.889 102.040 127.040 90.00 90.00 90.00 I 2 2 2 8
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 0.013006 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009800 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007872 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
