HEADER OXIDOREDUCTASE 21-APR-15 4ZF6
TITLE CYTOCHROME P450 PENTAMUTANT FROM BM3 WITH BOUND PEG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL P-450/NADPH-P450 REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-461;
COMPND 5 SYNONYM: CYTOCHROME P450(BM-3),CYTOCHROME P450BM-3;
COMPND 6 EC: 1.14.14.1,1.6.2.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 GENE: CYP102A1, CYP102;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS CYTOCHROME P450, HEME OXIDASE DOMAIN, OXIDOREDUCTASE, BACILLUS
KEYWDS 2 MEGATERIUM
EXPDTA X-RAY DIFFRACTION
AUTHOR W.E.ROGERS,T.OTHMAN,D.K.HEIDARY,T.HUXFORD
REVDAT 2 27-SEP-23 4ZF6 1 JRNL REMARK LINK
REVDAT 1 13-JUL-16 4ZF6 0
JRNL AUTH I.GERONIMO,C.A.DENNING,W.E.ROGERS,T.OTHMAN,T.HUXFORD,
JRNL AUTH 2 D.K.HEIDARY,E.C.GLAZER,C.M.PAYNE
JRNL TITL EFFECT OF MUTATION AND SUBSTRATE BINDING ON THE STABILITY OF
JRNL TITL 2 CYTOCHROME P450BM3 VARIANTS.
JRNL REF BIOCHEMISTRY V. 55 3594 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27267136
JRNL DOI 10.1021/ACS.BIOCHEM.6B00183
REMARK 2
REMARK 2 RESOLUTION. 2.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 17994
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 : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 918
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 59.2826 - 5.3043 1.00 2842 146 0.1931 0.2217
REMARK 3 2 5.3043 - 4.2105 1.00 2565 115 0.1736 0.2006
REMARK 3 3 4.2105 - 3.6784 1.00 2505 140 0.1878 0.2324
REMARK 3 4 3.6784 - 3.3421 1.00 2461 129 0.2076 0.3052
REMARK 3 5 3.3421 - 3.1026 1.00 2401 151 0.2202 0.3053
REMARK 3 6 3.1026 - 2.9196 1.00 2435 117 0.2555 0.3272
REMARK 3 7 2.9196 - 2.7734 0.79 1867 120 0.2923 0.4153
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.130
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 : 0.004 3840
REMARK 3 ANGLE : 0.947 5201
REMARK 3 CHIRALITY : 0.037 557
REMARK 3 PLANARITY : 0.004 674
REMARK 3 DIHEDRAL : 13.674 1456
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4ZF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209148.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18183
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.770
REMARK 200 RESOLUTION RANGE LOW (A) : 177.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3NPL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17.5MM NICL2, 50MM PEG MME 2000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 474.15267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 237.07633
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 355.61450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 118.53817
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 592.69083
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 474.15267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 237.07633
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 118.53817
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 355.61450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 592.69083
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 0
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 CE1 HIS A 236 NI NI A 507 0.93
REMARK 500 O THR A 91 O HOH A 601 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG1 THR A 1 OE1 GLU A 348 10555 1.85
REMARK 500 OG1 THR A 1 OD2 ASP A 338 10555 2.11
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 LYS A 15 -120.14 57.01
REMARK 500 ASP A 84 45.08 -96.51
REMARK 500 GLU A 93 93.79 -66.46
REMARK 500 LYS A 94 70.22 -112.52
REMARK 500 ASP A 168 -75.48 -64.67
REMARK 500 SER A 226 162.11 67.47
REMARK 500 GLU A 228 -135.84 35.83
REMARK 500 HIS A 266 -27.14 -149.36
REMARK 500 GLU A 344 -32.78 -137.68
REMARK 500 ILE A 366 -37.06 -142.81
REMARK 500 ASP A 370 49.88 -82.72
REMARK 500 LEU A 437 -57.54 71.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 94 ASN A 95 136.88
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 NI A 506 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 1 N
REMARK 620 2 THR A 1 OG1 88.9
REMARK 620 3 ASP A 338 OD2 84.9 40.8
REMARK 620 4 GLU A 348 OE1 76.0 43.4 8.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 504 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 138 NE2
REMARK 620 2 HIS A 426 NE2 91.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 505 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 214 OD1
REMARK 620 2 ASP A 214 OD2 66.6
REMARK 620 3 HIS A 285 NE2 61.3 44.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 507 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 231 OD1
REMARK 620 2 ASP A 231 OD2 66.4
REMARK 620 3 HIS A 236 ND1 111.8 121.4
REMARK 620 4 HIS A 236 NE2 141.5 150.3 65.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 400 SG
REMARK 620 2 HEM A 501 NA 100.5
REMARK 620 3 HEM A 501 NB 91.0 86.4
REMARK 620 4 HEM A 501 NC 86.4 172.3 90.0
REMARK 620 5 HEM A 501 ND 94.3 92.8 174.7 90.1
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZF8 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZF9 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZFA RELATED DB: PDB
REMARK 900 RELATED ID: 4ZFB RELATED DB: PDB
REMARK 900 RELATED ID: 4ZFD RELATED DB: PDB
REMARK 900 RELATED ID: 4ZFE RELATED DB: PDB
DBREF 4ZF6 A 0 460 UNP P14779 CPXB_BACME 1 461
SEQADV 4ZF6 LEU A 47 UNP P14779 ARG 48 ENGINEERED MUTATION
SEQADV 4ZF6 ILE A 81 UNP P14779 PHE 82 ENGINEERED MUTATION
SEQADV 4ZF6 VAL A 87 UNP P14779 PHE 88 ENGINEERED MUTATION
SEQADV 4ZF6 GLN A 188 UNP P14779 LEU 189 ENGINEERED MUTATION
SEQADV 4ZF6 VAL A 267 UNP P14779 GLU 268 ENGINEERED MUTATION
SEQRES 1 A 461 MET THR ILE LYS GLU MET PRO GLN PRO LYS THR PHE GLY
SEQRES 2 A 461 GLU LEU LYS ASN LEU PRO LEU LEU ASN THR ASP LYS PRO
SEQRES 3 A 461 VAL GLN ALA LEU MET LYS ILE ALA ASP GLU LEU GLY GLU
SEQRES 4 A 461 ILE PHE LYS PHE GLU ALA PRO GLY LEU VAL THR ARG TYR
SEQRES 5 A 461 LEU SER SER GLN ARG LEU ILE LYS GLU ALA CYS ASP GLU
SEQRES 6 A 461 SER ARG PHE ASP LYS ASN LEU SER GLN ALA LEU LYS PHE
SEQRES 7 A 461 VAL ARG ASP ILE ALA GLY ASP GLY LEU VAL THR SER TRP
SEQRES 8 A 461 THR HIS GLU LYS ASN TRP LYS LYS ALA HIS ASN ILE LEU
SEQRES 9 A 461 LEU PRO SER PHE SER GLN GLN ALA MET LYS GLY TYR HIS
SEQRES 10 A 461 ALA MET MET VAL ASP ILE ALA VAL GLN LEU VAL GLN LYS
SEQRES 11 A 461 TRP GLU ARG LEU ASN ALA ASP GLU HIS ILE GLU VAL PRO
SEQRES 12 A 461 GLU ASP MET THR ARG LEU THR LEU ASP THR ILE GLY LEU
SEQRES 13 A 461 CYS GLY PHE ASN TYR ARG PHE ASN SER PHE TYR ARG ASP
SEQRES 14 A 461 GLN PRO HIS PRO PHE ILE THR SER MET VAL ARG ALA LEU
SEQRES 15 A 461 ASP GLU ALA MET ASN LYS GLN GLN ARG ALA ASN PRO ASP
SEQRES 16 A 461 ASP PRO ALA TYR ASP GLU ASN LYS ARG GLN PHE GLN GLU
SEQRES 17 A 461 ASP ILE LYS VAL MET ASN ASP LEU VAL ASP LYS ILE ILE
SEQRES 18 A 461 ALA ASP ARG LYS ALA SER GLY GLU GLN SER ASP ASP LEU
SEQRES 19 A 461 LEU THR HIS MET LEU ASN GLY LYS ASP PRO GLU THR GLY
SEQRES 20 A 461 GLU PRO LEU ASP ASP GLU ASN ILE ARG TYR GLN ILE ILE
SEQRES 21 A 461 THR PHE LEU ILE ALA GLY HIS VAL THR THR SER GLY LEU
SEQRES 22 A 461 LEU SER PHE ALA LEU TYR PHE LEU VAL LYS ASN PRO HIS
SEQRES 23 A 461 VAL LEU GLN LYS ALA ALA GLU GLU ALA ALA ARG VAL LEU
SEQRES 24 A 461 VAL ASP PRO VAL PRO SER TYR LYS GLN VAL LYS GLN LEU
SEQRES 25 A 461 LYS TYR VAL GLY MET VAL LEU ASN GLU ALA LEU ARG LEU
SEQRES 26 A 461 TRP PRO THR ALA PRO ALA PHE SER LEU TYR ALA LYS GLU
SEQRES 27 A 461 ASP THR VAL LEU GLY GLY GLU TYR PRO LEU GLU LYS GLY
SEQRES 28 A 461 ASP GLU LEU MET VAL LEU ILE PRO GLN LEU HIS ARG ASP
SEQRES 29 A 461 LYS THR ILE TRP GLY ASP ASP VAL GLU GLU PHE ARG PRO
SEQRES 30 A 461 GLU ARG PHE GLU ASN PRO SER ALA ILE PRO GLN HIS ALA
SEQRES 31 A 461 PHE LYS PRO PHE GLY ASN GLY GLN ARG ALA CYS ILE GLY
SEQRES 32 A 461 GLN GLN PHE ALA LEU HIS GLU ALA THR LEU VAL LEU GLY
SEQRES 33 A 461 MET MET LEU LYS HIS PHE ASP PHE GLU ASP HIS THR ASN
SEQRES 34 A 461 TYR GLU LEU ASP ILE LYS GLU THR LEU THR LEU LYS PRO
SEQRES 35 A 461 GLU GLY PHE VAL VAL LYS ALA LYS SER LYS LYS ILE PRO
SEQRES 36 A 461 LEU GLY GLY ILE PRO SER
HET HEM A 501 43
HET 1PE A 502 16
HET EDO A 503 4
HET NI A 504 1
HET NI A 505 1
HET NI A 506 1
HET NI A 507 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NI NICKEL (II) ION
HETSYN HEM HEME
HETSYN 1PE PEG400
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 1PE C10 H22 O6
FORMUL 4 EDO C2 H6 O2
FORMUL 5 NI 4(NI 2+)
FORMUL 9 HOH *59(H2 O)
HELIX 1 AA1 PHE A 11 LYS A 15 5 5
HELIX 2 AA2 ASN A 16 ASN A 21 5 6
HELIX 3 AA3 LYS A 24 GLY A 37 1 14
HELIX 4 AA4 SER A 54 CYS A 62 1 9
HELIX 5 AA5 SER A 72 GLY A 83 1 12
HELIX 6 AA6 ASN A 95 LEU A 104 1 10
HELIX 7 AA7 PRO A 105 PHE A 107 5 3
HELIX 8 AA8 SER A 108 GLU A 131 1 24
HELIX 9 AA9 VAL A 141 ASN A 159 1 19
HELIX 10 AB1 ASN A 163 ARG A 167 5 5
HELIX 11 AB2 HIS A 171 LYS A 187 1 17
HELIX 12 AB3 GLN A 188 ARG A 190 5 3
HELIX 13 AB4 ASP A 195 ALA A 197 5 3
HELIX 14 AB5 TYR A 198 LYS A 224 1 27
HELIX 15 AB6 ASP A 232 GLY A 240 1 9
HELIX 16 AB7 ASP A 250 GLY A 265 1 16
HELIX 17 AB8 HIS A 266 ASN A 283 1 18
HELIX 18 AB9 ASN A 283 LEU A 298 1 16
HELIX 19 AC1 SER A 304 GLN A 310 1 7
HELIX 20 AC2 LEU A 311 TRP A 325 1 15
HELIX 21 AC3 ILE A 357 HIS A 361 1 5
HELIX 22 AC4 ASP A 363 GLY A 368 1 6
HELIX 23 AC5 ARG A 375 ASN A 381 5 7
HELIX 24 AC6 ASN A 395 ALA A 399 5 5
HELIX 25 AC7 GLY A 402 HIS A 420 1 19
SHEET 1 AA1 5 ILE A 39 ALA A 44 0
SHEET 2 AA1 5 LEU A 47 LEU A 52 -1 O THR A 49 N PHE A 42
SHEET 3 AA1 5 GLU A 352 LEU A 356 1 O MET A 354 N ARG A 50
SHEET 4 AA1 5 ALA A 330 ALA A 335 -1 N LEU A 333 O LEU A 353
SHEET 5 AA1 5 PHE A 67 ASN A 70 -1 N ASP A 68 O TYR A 334
SHEET 1 AA2 3 ILE A 139 GLU A 140 0
SHEET 2 AA2 3 VAL A 445 SER A 450 -1 O VAL A 446 N ILE A 139
SHEET 3 AA2 3 PHE A 421 GLU A 424 -1 N GLU A 424 O LYS A 447
SHEET 1 AA3 2 THR A 339 LEU A 341 0
SHEET 2 AA3 2 TYR A 345 LEU A 347 -1 O LEU A 347 N THR A 339
SHEET 1 AA4 2 ILE A 433 GLU A 435 0
SHEET 2 AA4 2 LEU A 439 PRO A 441 -1 O LYS A 440 N LYS A 434
LINK N THR A 1 NI NI A 506 1555 1555 1.98
LINK OG1 THR A 1 NI NI A 506 1555 1555 1.98
LINK NE2 HIS A 138 NI NI A 504 1555 1555 1.98
LINK OD1 ASP A 214 NI NI A 505 1555 1445 1.98
LINK OD2 ASP A 214 NI NI A 505 1555 1445 1.99
LINK OD1 ASP A 231 NI NI A 507 1555 1555 1.98
LINK OD2 ASP A 231 NI NI A 507 1555 1555 1.98
LINK ND1 HIS A 236 NI NI A 507 1555 1555 1.98
LINK NE2 HIS A 236 NI NI A 507 1555 1555 1.98
LINK NE2 HIS A 285 NI NI A 505 1555 1555 1.98
LINK OD2 ASP A 338 NI NI A 506 1555 10555 1.98
LINK OE1 GLU A 348 NI NI A 506 1555 10555 1.99
LINK SG CYS A 400 FE HEM A 501 1555 1555 2.30
LINK NE2 HIS A 426 NI NI A 504 1555 1555 1.98
SITE 1 AC1 26 LYS A 69 LEU A 86 VAL A 87 TRP A 96
SITE 2 AC1 26 PHE A 261 ALA A 264 GLY A 265 THR A 268
SITE 3 AC1 26 LEU A 272 THR A 327 ALA A 328 PHE A 331
SITE 4 AC1 26 PRO A 392 PHE A 393 GLY A 394 ARG A 398
SITE 5 AC1 26 CYS A 400 ILE A 401 GLY A 402 ALA A 406
SITE 6 AC1 26 EDO A 503 HOH A 604 HOH A 613 HOH A 616
SITE 7 AC1 26 HOH A 619 HOH A 636
SITE 1 AC2 7 VAL A 26 VAL A 78 PRO A 329 ALA A 330
SITE 2 AC2 7 LEU A 437 EDO A 503 HOH A 625
SITE 1 AC3 4 ALA A 264 THR A 268 HEM A 501 1PE A 502
SITE 1 AC4 2 HIS A 138 HIS A 426
SITE 1 AC5 2 ASP A 214 HIS A 285
SITE 1 AC6 3 THR A 1 ASP A 338 GLU A 348
SITE 1 AC7 2 ASP A 231 HIS A 236
CRYST1 56.047 56.047 711.229 90.00 90.00 120.00 P 65 2 2 12
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 0.017842 0.010301 0.000000 0.00000
SCALE2 0.000000 0.020603 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001406 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
