HEADER OXIDOREDUCTASE 16-OCT-07 2VE4
TITLE SUBSTRATE FREE CYANOBACTERIAL CYP120A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE CYTOCHROME P450 120;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CYTOCHROME P450 ENZYME;
COMPND 5 EC: 1.14.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)
KEYWDS OXIDOREDUCTASE, MONOOXYGENASE, METAL-BINDING, HEME, IRON
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KUHNEL,N.KE,S.G.SLIGAR,M.A.SCHULER,I.SCHLICHTING
REVDAT 3 16-MAR-11 2VE4 1 VERSN
REVDAT 2 24-FEB-09 2VE4 1 VERSN
REVDAT 1 29-APR-08 2VE4 0
JRNL AUTH K.KUHNEL,N.KE,M.J.CRYLE,S.G.SLIGAR,M.A.SCHULER,
JRNL AUTH 2 I.SCHLICHTING
JRNL TITL CRYSTAL STRUCTURES OF SUBSTRATE-FREE AND RETINOIC
JRNL TITL 2 ACID-BOUND CYANOBACTERIAL CYTOCHROME P450 CYP120A1.
JRNL REF BIOCHEMISTRY V. 47 6552 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18512957
JRNL DOI 10.1021/BI800328S
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 39760
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 + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2092
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2575
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 135
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6897
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -0.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.449
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.315
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.260
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.165
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7187 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9792 ; 1.441 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 861 ; 6.651 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 335 ;38.464 ;23.910
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1181 ;19.223 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;19.659 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1045 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5561 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3294 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4796 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 285 ; 0.178 ; 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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): 37 ; 0.170 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.126 ; 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): 4437 ; 0.659 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6975 ; 1.113 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3102 ; 1.395 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2813 ; 2.207 ; 4.500
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
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2VE4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-OCT-07.
REMARK 100 THE PDBE ID CODE IS EBI-34162.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40633
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : 5.2
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.4
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% ETHYLENE GLYCOL, 7% PEG
REMARK 280 3350, 0.1 M TRIS PH7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 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 76.82000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 76.82000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 61.08500
REMARK 290 SMTRY3 4 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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B2038 LIES ON A SPECIAL POSITION.
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 ILE A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 PRO A 5
REMARK 465 THR A 6
REMARK 465 ASN A 7
REMARK 465 LEU A 8
REMARK 465 ASN A 9
REMARK 465 SER A 10
REMARK 465 SER A 442
REMARK 465 LEU A 443
REMARK 465 MET A 444
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 PRO B 5
REMARK 465 THR B 6
REMARK 465 ASN B 7
REMARK 465 LEU B 8
REMARK 465 ASN B 9
REMARK 465 SER B 10
REMARK 465 LEU B 443
REMARK 465 MET B 444
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 GLU A 162 CG CD OE1 OE2
REMARK 470 LYS A 163 CG CD CE NZ
REMARK 470 GLN A 288 CG CD OE1 NE2
REMARK 470 GLN A 291 CG CD OE1 NE2
REMARK 470 LYS A 361 CG CD CE NZ
REMARK 470 ASP A 434 CG OD1 OD2
REMARK 470 ARG A 437 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 LYS B 71 CG CD CE NZ
REMARK 470 LYS B 106 CG CD CE NZ
REMARK 470 GLU B 162 CG CD OE1 OE2
REMARK 470 LYS B 163 CG CD CE NZ
REMARK 470 GLU B 278 CG CD OE1 OE2
REMARK 470 GLN B 288 CG CD OE1 NE2
REMARK 470 GLN B 291 CG CD OE1 NE2
REMARK 470 LYS B 361 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG B 66 OG1 THR B 70 2.18
REMARK 500 O TRP A 80 NH1 ARG A 85 2.19
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 TRP A 22 -66.09 67.11
REMARK 500 THR A 75 -61.27 -91.07
REMARK 500 PRO A 187 57.61 -92.79
REMARK 500 ASN A 190 55.36 -97.04
REMARK 500 HIS A 256 -80.02 -64.96
REMARK 500 LEU A 289 72.70 -69.35
REMARK 500 ILE A 315 79.35 -117.27
REMARK 500 LYS A 338 141.55 -33.17
REMARK 500 PRO A 359 7.40 -66.36
REMARK 500 PRO A 369 -29.12 -22.06
REMARK 500 HIS A 375 40.72 -99.30
REMARK 500 ASN A 435 43.15 38.34
REMARK 500 LEU A 436 93.96 60.27
REMARK 500 TRP B 22 -68.28 61.37
REMARK 500 GLN B 41 42.82 -69.68
REMARK 500 GLN B 42 -56.01 -161.18
REMARK 500 PRO B 187 56.51 -93.02
REMARK 500 HIS B 256 -78.11 -72.00
REMARK 500 HIS B 273 76.27 -119.75
REMARK 500 GLN B 288 57.84 -98.09
REMARK 500 SER B 290 -156.18 -99.05
REMARK 500 GLN B 291 32.01 -89.64
REMARK 500 PRO B 369 -38.61 -19.31
REMARK 500 PHE B 379 40.48 76.58
REMARK 500 CYS B 391 120.09 -38.54
REMARK 500 VAL B 426 71.05 -119.10
REMARK 500 LEU B 436 81.07 57.46
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 ARG A 437 VAL A 438 -149.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASN A 435 24.3 L L OUTSIDE RANGE
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 A1442 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEM A1442 ND
REMARK 620 2 CYS A 391 SG 96.6
REMARK 620 3 HEM A1442 NA 89.0 103.1
REMARK 620 4 HEM A1442 NB 170.4 92.1 85.1
REMARK 620 5 HEM A1442 NC 98.3 83.0 170.0 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B1443 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEM B1443 NC
REMARK 620 2 CYS B 391 SG 89.7
REMARK 620 3 HEM B1443 NB 86.4 89.8
REMARK 620 4 HEM B1443 ND 94.4 102.0 168.2
REMARK 620 5 HEM B1443 NA 166.0 101.6 85.4 91.3
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 A1442
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B1443
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VE3 RELATED DB: PDB
REMARK 900 RETINOIC ACID BOUND CYANOBACTERIAL CYP120A1
DBREF 2VE4 A 1 444 UNP Q59990 CP120_SYNY3 1 444
DBREF 2VE4 B 1 444 UNP Q59990 CP120_SYNY3 1 444
SEQRES 1 A 444 MET ILE THR SER PRO THR ASN LEU ASN SER LEU PRO ILE
SEQRES 2 A 444 PRO PRO GLY ASP PHE GLY LEU PRO TRP LEU GLY GLU THR
SEQRES 3 A 444 LEU ASN PHE LEU ASN ASP GLY ASP PHE GLY LYS LYS ARG
SEQRES 4 A 444 GLN GLN GLN PHE GLY PRO ILE PHE LYS THR ARG LEU PHE
SEQRES 5 A 444 GLY LYS ASN VAL ILE PHE ILE SER GLY ALA LEU ALA ASN
SEQRES 6 A 444 ARG PHE LEU PHE THR LYS GLU GLN GLU THR PHE GLN ALA
SEQRES 7 A 444 THR TRP PRO LEU SER THR ARG ILE LEU LEU GLY PRO ASN
SEQRES 8 A 444 ALA LEU ALA THR GLN MET GLY GLU ILE HIS ARG SER ARG
SEQRES 9 A 444 ARG LYS ILE LEU TYR GLN ALA PHE LEU PRO ARG THR LEU
SEQRES 10 A 444 ASP SER TYR LEU PRO LYS MET ASP GLY ILE VAL GLN GLY
SEQRES 11 A 444 TYR LEU GLU GLN TRP GLY LYS ALA ASN GLU VAL ILE TRP
SEQRES 12 A 444 TYR PRO GLN LEU ARG ARG MET THR PHE ASP VAL ALA ALA
SEQRES 13 A 444 THR LEU PHE MET GLY GLU LYS VAL SER GLN ASN PRO GLN
SEQRES 14 A 444 LEU PHE PRO TRP PHE GLU THR TYR ILE GLN GLY LEU PHE
SEQRES 15 A 444 SER LEU PRO ILE PRO LEU PRO ASN THR LEU PHE GLY LYS
SEQRES 16 A 444 SER GLN ARG ALA ARG ALA LEU LEU LEU ALA GLU LEU GLU
SEQRES 17 A 444 LYS ILE ILE LYS ALA ARG GLN GLN GLN PRO PRO SER GLU
SEQRES 18 A 444 GLU ASP ALA LEU GLY ILE LEU LEU ALA ALA ARG ASP ASP
SEQRES 19 A 444 ASN ASN GLN PRO LEU SER LEU PRO GLU LEU LYS ASP GLN
SEQRES 20 A 444 ILE LEU LEU LEU LEU PHE ALA GLY HIS GLU THR LEU THR
SEQRES 21 A 444 SER ALA LEU SER SER PHE CYS LEU LEU LEU GLY GLN HIS
SEQRES 22 A 444 SER ASP ILE ARG GLU ARG VAL ARG GLN GLU GLN ASN LYS
SEQRES 23 A 444 LEU GLN LEU SER GLN GLU LEU THR ALA GLU THR LEU LYS
SEQRES 24 A 444 LYS MET PRO TYR LEU ASP GLN VAL LEU GLN GLU VAL LEU
SEQRES 25 A 444 ARG LEU ILE PRO PRO VAL GLY GLY GLY PHE ARG GLU LEU
SEQRES 26 A 444 ILE GLN ASP CYS GLN PHE GLN GLY PHE HIS PHE PRO LYS
SEQRES 27 A 444 GLY TRP LEU VAL SER TYR GLN ILE SER GLN THR HIS ALA
SEQRES 28 A 444 ASP PRO ASP LEU TYR PRO ASP PRO GLU LYS PHE ASP PRO
SEQRES 29 A 444 GLU ARG PHE THR PRO ASP GLY SER ALA THR HIS ASN PRO
SEQRES 30 A 444 PRO PHE ALA HIS VAL PRO PHE GLY GLY GLY LEU ARG GLU
SEQRES 31 A 444 CYS LEU GLY LYS GLU PHE ALA ARG LEU GLU MET LYS LEU
SEQRES 32 A 444 PHE ALA THR ARG LEU ILE GLN GLN PHE ASP TRP THR LEU
SEQRES 33 A 444 LEU PRO GLY GLN ASN LEU GLU LEU VAL VAL THR PRO SER
SEQRES 34 A 444 PRO ARG PRO LYS ASP ASN LEU ARG VAL LYS LEU HIS SER
SEQRES 35 A 444 LEU MET
SEQRES 1 B 444 MET ILE THR SER PRO THR ASN LEU ASN SER LEU PRO ILE
SEQRES 2 B 444 PRO PRO GLY ASP PHE GLY LEU PRO TRP LEU GLY GLU THR
SEQRES 3 B 444 LEU ASN PHE LEU ASN ASP GLY ASP PHE GLY LYS LYS ARG
SEQRES 4 B 444 GLN GLN GLN PHE GLY PRO ILE PHE LYS THR ARG LEU PHE
SEQRES 5 B 444 GLY LYS ASN VAL ILE PHE ILE SER GLY ALA LEU ALA ASN
SEQRES 6 B 444 ARG PHE LEU PHE THR LYS GLU GLN GLU THR PHE GLN ALA
SEQRES 7 B 444 THR TRP PRO LEU SER THR ARG ILE LEU LEU GLY PRO ASN
SEQRES 8 B 444 ALA LEU ALA THR GLN MET GLY GLU ILE HIS ARG SER ARG
SEQRES 9 B 444 ARG LYS ILE LEU TYR GLN ALA PHE LEU PRO ARG THR LEU
SEQRES 10 B 444 ASP SER TYR LEU PRO LYS MET ASP GLY ILE VAL GLN GLY
SEQRES 11 B 444 TYR LEU GLU GLN TRP GLY LYS ALA ASN GLU VAL ILE TRP
SEQRES 12 B 444 TYR PRO GLN LEU ARG ARG MET THR PHE ASP VAL ALA ALA
SEQRES 13 B 444 THR LEU PHE MET GLY GLU LYS VAL SER GLN ASN PRO GLN
SEQRES 14 B 444 LEU PHE PRO TRP PHE GLU THR TYR ILE GLN GLY LEU PHE
SEQRES 15 B 444 SER LEU PRO ILE PRO LEU PRO ASN THR LEU PHE GLY LYS
SEQRES 16 B 444 SER GLN ARG ALA ARG ALA LEU LEU LEU ALA GLU LEU GLU
SEQRES 17 B 444 LYS ILE ILE LYS ALA ARG GLN GLN GLN PRO PRO SER GLU
SEQRES 18 B 444 GLU ASP ALA LEU GLY ILE LEU LEU ALA ALA ARG ASP ASP
SEQRES 19 B 444 ASN ASN GLN PRO LEU SER LEU PRO GLU LEU LYS ASP GLN
SEQRES 20 B 444 ILE LEU LEU LEU LEU PHE ALA GLY HIS GLU THR LEU THR
SEQRES 21 B 444 SER ALA LEU SER SER PHE CYS LEU LEU LEU GLY GLN HIS
SEQRES 22 B 444 SER ASP ILE ARG GLU ARG VAL ARG GLN GLU GLN ASN LYS
SEQRES 23 B 444 LEU GLN LEU SER GLN GLU LEU THR ALA GLU THR LEU LYS
SEQRES 24 B 444 LYS MET PRO TYR LEU ASP GLN VAL LEU GLN GLU VAL LEU
SEQRES 25 B 444 ARG LEU ILE PRO PRO VAL GLY GLY GLY PHE ARG GLU LEU
SEQRES 26 B 444 ILE GLN ASP CYS GLN PHE GLN GLY PHE HIS PHE PRO LYS
SEQRES 27 B 444 GLY TRP LEU VAL SER TYR GLN ILE SER GLN THR HIS ALA
SEQRES 28 B 444 ASP PRO ASP LEU TYR PRO ASP PRO GLU LYS PHE ASP PRO
SEQRES 29 B 444 GLU ARG PHE THR PRO ASP GLY SER ALA THR HIS ASN PRO
SEQRES 30 B 444 PRO PHE ALA HIS VAL PRO PHE GLY GLY GLY LEU ARG GLU
SEQRES 31 B 444 CYS LEU GLY LYS GLU PHE ALA ARG LEU GLU MET LYS LEU
SEQRES 32 B 444 PHE ALA THR ARG LEU ILE GLN GLN PHE ASP TRP THR LEU
SEQRES 33 B 444 LEU PRO GLY GLN ASN LEU GLU LEU VAL VAL THR PRO SER
SEQRES 34 B 444 PRO ARG PRO LYS ASP ASN LEU ARG VAL LYS LEU HIS SER
SEQRES 35 B 444 LEU MET
HET HEM A1442 43
HET HEM B1443 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 HOH *161(H2 O)
HELIX 1 1 GLU A 25 ASP A 32 1 8
HELIX 2 2 ASP A 34 GLY A 44 1 11
HELIX 3 3 GLY A 61 PHE A 69 1 9
HELIX 4 4 LYS A 71 THR A 75 1 5
HELIX 5 5 PRO A 81 GLY A 89 1 9
HELIX 6 6 ALA A 92 GLN A 96 5 5
HELIX 7 7 MET A 97 TYR A 109 1 13
HELIX 8 8 GLN A 110 PHE A 112 5 3
HELIX 9 9 LEU A 113 SER A 119 1 7
HELIX 10 10 TYR A 120 ALA A 138 1 19
HELIX 11 11 TRP A 143 GLY A 161 1 19
HELIX 12 12 GLY A 161 GLN A 166 1 6
HELIX 13 13 GLN A 169 GLY A 180 1 12
HELIX 14 14 THR A 191 GLN A 216 1 26
HELIX 15 15 ASP A 223 ALA A 231 1 9
HELIX 16 16 SER A 240 LEU A 270 1 31
HELIX 17 17 HIS A 273 LYS A 286 1 14
HELIX 18 18 THR A 294 LYS A 299 1 6
HELIX 19 19 MET A 301 ILE A 315 1 15
HELIX 20 20 GLN A 345 HIS A 350 1 6
HELIX 21 21 ASP A 363 THR A 368 5 6
HELIX 22 22 GLY A 386 GLU A 390 5 5
HELIX 23 23 GLY A 393 PHE A 412 1 20
HELIX 24 24 GLU B 25 ASP B 32 1 8
HELIX 25 25 ARG B 39 GLY B 44 1 6
HELIX 26 26 GLY B 61 PHE B 69 1 9
HELIX 27 27 LYS B 71 THR B 75 1 5
HELIX 28 28 PRO B 81 GLY B 89 1 9
HELIX 29 29 MET B 97 TYR B 109 1 13
HELIX 30 30 GLN B 110 PHE B 112 5 3
HELIX 31 31 LEU B 113 LYS B 137 1 25
HELIX 32 32 TRP B 143 GLY B 161 1 19
HELIX 33 33 LYS B 163 ASN B 167 5 5
HELIX 34 34 GLN B 169 GLY B 180 1 12
HELIX 35 35 THR B 191 GLN B 215 1 25
HELIX 36 36 ASP B 223 ALA B 230 1 8
HELIX 37 37 SER B 240 HIS B 273 1 34
HELIX 38 38 HIS B 273 LEU B 287 1 15
HELIX 39 39 THR B 294 LYS B 299 1 6
HELIX 40 40 MET B 301 ILE B 315 1 15
HELIX 41 41 ILE B 346 HIS B 350 1 5
HELIX 42 42 ASP B 363 THR B 368 5 6
HELIX 43 43 GLY B 386 GLU B 390 5 5
HELIX 44 44 GLY B 393 PHE B 412 1 20
SHEET 1 AA 5 PHE A 47 LEU A 51 0
SHEET 2 AA 5 LYS A 54 PHE A 58 -1 O LYS A 54 N LEU A 51
SHEET 3 AA 5 LEU A 341 TYR A 344 1 O LEU A 341 N ILE A 57
SHEET 4 AA 5 GLY A 321 LEU A 325 -1 O GLY A 321 N TYR A 344
SHEET 5 AA 5 PHE A 76 GLN A 77 -1 O GLN A 77 N GLU A 324
SHEET 1 AB 3 VAL A 141 ILE A 142 0
SHEET 2 AB 3 ARG A 437 LEU A 440 -1 O VAL A 438 N VAL A 141
SHEET 3 AB 3 TRP A 414 LEU A 416 -1 O THR A 415 N LYS A 439
SHEET 1 AC 2 CYS A 329 PHE A 331 0
SHEET 2 AC 2 PHE A 334 PHE A 336 -1 O PHE A 334 N PHE A 331
SHEET 1 AD 2 LEU A 424 VAL A 425 0
SHEET 2 AD 2 ARG A 431 PRO A 432 -1 O ARG A 431 N VAL A 425
SHEET 1 BA 5 PHE B 47 LEU B 51 0
SHEET 2 BA 5 LYS B 54 SER B 60 -1 O LYS B 54 N LEU B 51
SHEET 3 BA 5 LEU B 341 GLN B 345 1 O LEU B 341 N ILE B 57
SHEET 4 BA 5 GLY B 320 LEU B 325 -1 O GLY B 321 N TYR B 344
SHEET 5 BA 5 PHE B 76 ALA B 78 -1 O GLN B 77 N GLU B 324
SHEET 1 BB 3 VAL B 141 ILE B 142 0
SHEET 2 BB 3 ARG B 437 HIS B 441 -1 O VAL B 438 N VAL B 141
SHEET 3 BB 3 ASP B 413 LEU B 416 -1 O ASP B 413 N HIS B 441
SHEET 1 BC 2 CYS B 329 PHE B 331 0
SHEET 2 BC 2 PHE B 334 PHE B 336 -1 O PHE B 334 N PHE B 331
SHEET 1 BD 2 LEU B 424 VAL B 426 0
SHEET 2 BD 2 PRO B 430 PRO B 432 -1 O ARG B 431 N VAL B 425
LINK FE HEM A1442 SG CYS A 391 1555 1555 2.36
LINK FE HEM B1443 SG CYS B 391 1555 1555 2.36
CISPEP 1 THR A 427 PRO A 428 0 -0.83
CISPEP 2 THR B 427 PRO B 428 0 -6.92
SITE 1 AC1 20 LEU A 93 HIS A 101 ARG A 105 ALA A 254
SITE 2 AC1 20 GLY A 255 THR A 258 LEU A 259 VAL A 318
SITE 3 AC1 20 ARG A 323 TYR A 344 ILE A 346 PRO A 383
SITE 4 AC1 20 PHE A 384 GLY A 385 ARG A 389 CYS A 391
SITE 5 AC1 20 GLY A 393 PHE A 396 ALA A 397 HOH A2075
SITE 1 AC2 20 LEU B 93 HIS B 101 ARG B 105 PHE B 159
SITE 2 AC2 20 LEU B 251 ALA B 254 GLY B 255 THR B 258
SITE 3 AC2 20 PRO B 317 VAL B 318 ARG B 323 TYR B 344
SITE 4 AC2 20 PRO B 383 PHE B 384 GLY B 385 ARG B 389
SITE 5 AC2 20 CYS B 391 GLY B 393 PHE B 396 HOH B2084
CRYST1 153.640 122.170 64.920 90.00 115.00 90.00 C 1 2 1 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 0.006509 0.000000 0.003035 0.00000
SCALE2 0.000000 0.008185 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016996 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
