HEADER OXIDOREDUCTASE 16-FEB-00 1DZ4
TITLE FERRIC P450CAM FROM PSEUDOMONAS PUTIDA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450-CAM;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: HEME ATTACHED VIA CYS357
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, MONO-OXYGENASE, HEME, FERRIC
EXPDTA X-RAY DIFFRACTION
AUTHOR I.SCHLICHTING,J.BERENDZEN,K.CHU,A.M.STOCK,S.A.MAVES,D.E.BENSON,
AUTHOR 2 R.M.SWEET,D.RINGE,G.A.PETSKO,S.G.SLIGAR
REVDAT 5 24-JUL-19 1DZ4 1 REMARK
REVDAT 4 03-APR-19 1DZ4 1 REMARK
REVDAT 3 12-JUL-17 1DZ4 1
REVDAT 2 24-FEB-09 1DZ4 1 VERSN
REVDAT 1 20-JUL-00 1DZ4 0
JRNL AUTH I.SCHLICHTING,J.BERENDZEN,K.CHU,A.M.STOCK,S.A.MAVES,
JRNL AUTH 2 D.E.BENSON,R.M.SWEET,D.RINGE,G.A.PETSKO,S.G.SLIGAR
JRNL TITL THE CATALYTIC PATHWAY OF CYTOCHROME P450CAM AT ATOMIC
JRNL TITL 2 RESOLUTION
JRNL REF SCIENCE V. 287 1615 2000
JRNL REFN ISSN 0036-8075
JRNL PMID 10698731
JRNL DOI 10.1126/SCIENCE.287.5458.1615
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.VIDAKOVIC,S.G.SLIGAR,H.LI,T.L.POULOS
REMARK 1 TITL UNDERSTANDING THE ROLE OF THE ESSENTIAL ASP251 ICYTOCHROME
REMARK 1 TITL 2 P450CAM USING SITE-DIRECTED MCRYSTALLOGRAPHY, AND KINETIC
REMARK 1 TITL 3 SOLVENT ISOTOPE EFFECTUTAGENESIS, N
REMARK 1 REF BIOCHEMISTRY V. 37 9211 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9649301
REMARK 1 DOI 10.1021/BI980189F
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.L.POULOS,B.C.FINZEL,A.J.HOWARD
REMARK 1 TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450CAM
REMARK 1 REF J.MOL.BIOL. V. 195 687 1987
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 3656428
REMARK 1 DOI 10.1016/0022-2836(87)90190-2
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 132096
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6063
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6408
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 119
REMARK 3 SOLVENT ATOMS : 673
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.50
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.267
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.029 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.034 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1290004625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8443
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : 101046
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 39.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 2.390
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.23
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.22700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: 20% GLYCEROL WAS USED AS CRYOPROTECTANT, THE CRYSTALS WERE
REMARK 200 FREEZE QUENCHED IN LIQUID NITROGEN.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN USING THE SITTING
REMARK 280 DROP GEOMETRY AT 2 DEG. C. 5 UL OF 30 MG/ML P450 IN 50 MM TRIS
REMARK 280 HCL, 250 MM KCL, 0.5 MM CAMPHOR WERE MIXED WITH AN EQUAL VOLUME
REMARK 280 OF THE RESERVOIR SOLUTION (27-30% PEG 4000, 100 MM DTE, SAME
REMARK 280 BUFFER AS PROTEIN)., PH 7.40, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 275K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 31.35000
REMARK 290 SMTRY3 2 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 300 REMARK: BIOLOGICAL_UNIT: MONOMER
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: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 ILE A 5
REMARK 465 GLN A 6
REMARK 465 SER A 7
REMARK 465 ASN A 8
REMARK 465 ALA A 9
REMARK 465 ASN A 10
REMARK 465 THR B 1
REMARK 465 THR B 2
REMARK 465 GLU B 3
REMARK 465 THR B 4
REMARK 465 ILE B 5
REMARK 465 GLN B 6
REMARK 465 SER B 7
REMARK 465 ASN B 8
REMARK 465 ALA B 9
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 186 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 299 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 342 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 364 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 377 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP B 25 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TYR B 29 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 109 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 109 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG B 112 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG B 186 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 202 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 231 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 GLU B 237 OE1 - CD - OE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 290 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 291 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 299 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 30 67.11 -166.40
REMARK 500 TYR A 154 -51.47 -145.14
REMARK 500 THR A 252 -78.89 -122.07
REMARK 500 ASP A 297 -156.24 -122.36
REMARK 500 ASN B 30 63.11 -162.90
REMARK 500 TYR B 154 -48.37 -151.56
REMARK 500 THR B 252 -76.31 -120.19
REMARK 500 ASP B 297 -163.08 -116.27
REMARK 500 VAL B 345 98.20 -40.87
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 K A 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 84 O
REMARK 620 2 GLY A 93 O 84.5
REMARK 620 3 GLU A 94 O 155.8 77.0
REMARK 620 4 TYR A 96 O 98.4 83.1 94.8
REMARK 620 5 HOH A 872 O 86.2 92.0 79.0 172.9
REMARK 620 6 HOH A 881 O 103.2 167.7 97.9 86.2 98.0
REMARK 620 N 1 2 3 4 5
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 357 SG
REMARK 620 2 HEM A 501 NA 103.3
REMARK 620 3 HEM A 501 NB 91.6 88.0
REMARK 620 4 HEM A 501 NC 95.0 161.4 88.2
REMARK 620 5 HEM A 501 ND 106.0 88.5 162.4 89.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 15 O
REMARK 620 2 PRO B 16 O 71.5
REMARK 620 3 VAL B 18 O 83.3 101.4
REMARK 620 4 GLU B 20 OE2 147.7 137.8 99.2
REMARK 620 5 HOH B 764 O 69.8 108.4 129.9 84.9
REMARK 620 6 THR A 217 OG1 69.6 138.0 59.0 84.0 72.1
REMARK 620 7 HOH A 748 O 124.7 82.8 150.8 62.3 73.6 133.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 503 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 84 O
REMARK 620 2 GLY B 93 O 84.4
REMARK 620 3 GLU B 94 O 157.6 77.0
REMARK 620 4 TYR B 96 O 98.4 85.9 92.8
REMARK 620 5 HOH B 913 O 104.6 166.3 96.0 82.6
REMARK 620 6 HOH B 918 O 87.0 93.4 81.7 174.4 97.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 357 SG
REMARK 620 2 HEM B 501 NA 100.3
REMARK 620 3 HEM B 501 NB 89.2 89.9
REMARK 620 4 HEM B 501 NC 96.9 162.6 87.9
REMARK 620 5 HEM B 501 ND 106.8 89.0 163.9 88.3
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 K A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K K 715
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAM A 420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAM B 420
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CPP RELATED DB: PDB
REMARK 900 RELATED ID: 3CPP RELATED DB: PDB
REMARK 900 RELATED ID: 4CPP RELATED DB: PDB
REMARK 900 RELATED ID: 5CPP RELATED DB: PDB
REMARK 900 RELATED ID: 6CPP RELATED DB: PDB
REMARK 900 RELATED ID: 7CPP RELATED DB: PDB
REMARK 900 RELATED ID: 8CPP RELATED DB: PDB
REMARK 900 RELATED ID: 1CP4 RELATED DB: PDB
REMARK 900 RELATED ID: 2CP4 RELATED DB: PDB
REMARK 900 RELATED ID: 3CP4 RELATED DB: PDB
REMARK 900 RELATED ID: 4CP4 RELATED DB: PDB
REMARK 900 RELATED ID: 5CP4 RELATED DB: PDB
REMARK 900 RELATED ID: 6CP4 RELATED DB: PDB
REMARK 900 RELATED ID: 1NOO RELATED DB: PDB
REMARK 900 RELATED ID: 1PHA RELATED DB: PDB
REMARK 900 RELATED ID: 1PHB RELATED DB: PDB
REMARK 900 RELATED ID: 1PHC RELATED DB: PDB
REMARK 900 RELATED ID: 1PHD RELATED DB: PDB
REMARK 900 RELATED ID: 1PHE RELATED DB: PDB
REMARK 900 RELATED ID: 1PHF RELATED DB: PDB
REMARK 900 RELATED ID: 1PHG RELATED DB: PDB
REMARK 900 RELATED ID: 1AKD RELATED DB: PDB
REMARK 900 RELATED ID: 1DZ6 RELATED DB: PDB
REMARK 900 RELATED ID: 1DZ8 RELATED DB: PDB
REMARK 900 RELATED ID: 1DZ9 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINUS IS DISORDERED
DBREF 1DZ4 A 1 414 UNP P00183 CPXA_PSEPU 1 414
DBREF 1DZ4 B 1 414 UNP P00183 CPXA_PSEPU 1 414
SEQRES 1 A 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO
SEQRES 2 A 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE
SEQRES 3 A 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN
SEQRES 4 A 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP
SEQRES 5 A 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA
SEQRES 6 A 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR
SEQRES 7 A 414 ARG HIS PHE SER SER GLU CYS PRO PHE ILE PRO ARG GLU
SEQRES 8 A 414 ALA GLY GLU ALA TYR ASP PHE ILE PRO THR SER MET ASP
SEQRES 9 A 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN
SEQRES 10 A 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG
SEQRES 11 A 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG
SEQRES 12 A 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU
SEQRES 13 A 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU
SEQRES 14 A 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP
SEQRES 15 A 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU
SEQRES 16 A 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE
SEQRES 17 A 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER
SEQRES 18 A 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR
SEQRES 19 A 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU VAL
SEQRES 20 A 414 GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE SER
SEQRES 21 A 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU
SEQRES 22 A 414 LEU ILE GLN ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU
SEQRES 23 A 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG
SEQRES 24 A 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU
SEQRES 25 A 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER
SEQRES 26 A 414 GLY LEU ASP GLU ARG GLU ASN ALA CYS PRO MET HIS VAL
SEQRES 27 A 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY
SEQRES 28 A 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG
SEQRES 29 A 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG
SEQRES 30 A 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN
SEQRES 31 A 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO
SEQRES 32 A 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
SEQRES 1 B 414 THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA PRO
SEQRES 2 B 414 LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP PHE
SEQRES 3 B 414 ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL GLN
SEQRES 4 B 414 GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO ASP
SEQRES 5 B 414 LEU VAL TRP THR ARG CYS ASN GLY GLY HIS TRP ILE ALA
SEQRES 6 B 414 THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP TYR
SEQRES 7 B 414 ARG HIS PHE SER SER GLU CYS PRO PHE ILE PRO ARG GLU
SEQRES 8 B 414 ALA GLY GLU ALA TYR ASP PHE ILE PRO THR SER MET ASP
SEQRES 9 B 414 PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN GLN
SEQRES 10 B 414 VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN ARG
SEQRES 11 B 414 ILE GLN GLU LEU ALA CYS SER LEU ILE GLU SER LEU ARG
SEQRES 12 B 414 PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA GLU
SEQRES 13 B 414 PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY LEU
SEQRES 14 B 414 PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR ASP
SEQRES 15 B 414 GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA GLU
SEQRES 16 B 414 ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE ILE
SEQRES 17 B 414 GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE SER
SEQRES 18 B 414 ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE THR
SEQRES 19 B 414 SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU VAL
SEQRES 20 B 414 GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE SER
SEQRES 21 B 414 MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN GLU
SEQRES 22 B 414 LEU ILE GLN ARG PRO GLU ARG ILE PRO ALA ALA CYS GLU
SEQRES 23 B 414 GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY ARG
SEQRES 24 B 414 ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN LEU
SEQRES 25 B 414 LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU SER
SEQRES 26 B 414 GLY LEU ASP GLU ARG GLU ASN ALA CYS PRO MET HIS VAL
SEQRES 27 B 414 ASP PHE SER ARG GLN LYS VAL SER HIS THR THR PHE GLY
SEQRES 28 B 414 HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA ARG
SEQRES 29 B 414 ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR ARG
SEQRES 30 B 414 ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE GLN
SEQRES 31 B 414 HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU PRO
SEQRES 32 B 414 LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
HET HEM A 501 43
HET CAM A 502 11
HET TRS A 503 8
HET K A 504 1
HET HEM B 501 43
HET CAM B 502 11
HET K B 503 1
HET K B 504 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CAM CAMPHOR
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM K POTASSIUM ION
HETSYN HEM HEME
HETSYN TRS TRIS BUFFER
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 CAM 2(C10 H16 O)
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 6 K 3(K 1+)
FORMUL 11 HOH *673(H2 O)
HELIX 1 1 PRO A 19 LEU A 22 5 4
HELIX 2 2 ASN A 33 ALA A 36 5 4
HELIX 3 3 GLY A 37 VAL A 44 1 8
HELIX 4 4 LEU A 45 GLU A 47 5 3
HELIX 5 5 ARG A 57 GLY A 61 5 5
HELIX 6 6 ARG A 67 ASP A 77 1 11
HELIX 7 7 PRO A 89 TYR A 96 1 8
HELIX 8 8 GLN A 108 GLY A 120 1 13
HELIX 9 9 GLY A 120 ARG A 143 1 24
HELIX 10 10 PHE A 150 TYR A 154 1 5
HELIX 11 11 GLU A 156 GLY A 168 1 13
HELIX 12 12 PRO A 170 GLU A 172 5 3
HELIX 13 13 ASP A 173 ARG A 186 1 14
HELIX 14 14 THR A 192 LYS A 214 1 23
HELIX 15 15 ASP A 218 ASN A 225 1 8
HELIX 16 16 THR A 234 ASP A 251 1 18
HELIX 17 17 THR A 252 LYS A 266 1 15
HELIX 18 18 SER A 267 ARG A 277 1 11
HELIX 19 19 ARG A 280 PHE A 292 1 13
HELIX 20 20 LEU A 324 ASP A 328 5 5
HELIX 21 21 HIS A 352 LEU A 356 5 5
HELIX 22 22 GLY A 359 ILE A 378 1 20
HELIX 23 23 ASP A 407 THR A 411 5 5
HELIX 24 24 PRO B 19 LEU B 22 5 4
HELIX 25 25 ASN B 33 ALA B 36 5 4
HELIX 26 26 GLY B 37 ALA B 43 1 7
HELIX 27 27 VAL B 44 GLU B 47 5 4
HELIX 28 28 ARG B 57 GLY B 61 5 5
HELIX 29 29 ARG B 67 ASP B 77 1 11
HELIX 30 30 PRO B 89 TYR B 96 1 8
HELIX 31 31 GLN B 108 GLY B 120 1 13
HELIX 32 32 GLY B 120 ARG B 143 1 24
HELIX 33 33 PHE B 150 TYR B 154 1 5
HELIX 34 34 GLU B 156 GLY B 168 1 13
HELIX 35 35 PRO B 170 GLU B 172 5 3
HELIX 36 36 ASP B 173 ARG B 186 1 14
HELIX 37 37 THR B 192 LYS B 214 1 23
HELIX 38 38 ASP B 218 ASN B 225 1 8
HELIX 39 39 THR B 234 ASP B 251 1 18
HELIX 40 40 THR B 252 SER B 267 1 16
HELIX 41 41 SER B 267 ARG B 277 1 11
HELIX 42 42 ARG B 280 PHE B 292 1 13
HELIX 43 43 PRO B 321 SER B 325 5 5
HELIX 44 44 HIS B 352 LEU B 356 5 5
HELIX 45 45 GLY B 359 ILE B 378 1 20
HELIX 46 46 ASP B 407 THR B 411 5 5
SHEET 1 A 4 LEU A 53 THR A 56 0
SHEET 2 A 4 HIS A 62 ALA A 65 -1 N ILE A 64 O VAL A 54
SHEET 3 A 4 GLN A 317 LEU A 320 1 N LEU A 319 O TRP A 63
SHEET 4 A 4 ASP A 297 ILE A 300 -1 N ARG A 299 O ILE A 318
SHEET 1 B 2 GLN A 147 ASN A 149 0
SHEET 2 B 2 PRO A 403 VAL A 405 -1 N LEU A 404 O CYS A 148
SHEET 1 C 2 TYR A 305 PHE A 307 0
SHEET 2 C 2 VAL A 310 LEU A 312 -1 N LEU A 312 O TYR A 305
SHEET 1 D 4 LEU B 53 THR B 56 0
SHEET 2 D 4 HIS B 62 ALA B 65 -1 N ILE B 64 O VAL B 54
SHEET 3 D 4 GLN B 317 LEU B 320 1 N LEU B 319 O TRP B 63
SHEET 4 D 4 ASP B 297 ILE B 300 -1 N ARG B 299 O ILE B 318
SHEET 1 E 2 GLN B 147 ASN B 149 0
SHEET 2 E 2 PRO B 403 VAL B 405 -1 N LEU B 404 O CYS B 148
SHEET 1 F 2 TYR B 305 PHE B 307 0
SHEET 2 F 2 VAL B 310 LEU B 312 -1 N LEU B 312 O TYR B 305
LINK O GLU A 84 K K A 504 1555 1555 2.70
LINK O GLY A 93 K K A 504 1555 1555 2.88
LINK O GLU A 94 K K A 504 1555 1555 2.96
LINK O TYR A 96 K K A 504 1555 1555 2.74
LINK SG CYS A 357 FE HEM A 501 1555 1555 2.37
LINK O PRO B 15 K K B 504 1555 1555 2.98
LINK O PRO B 16 K K B 504 1555 1555 2.88
LINK O VAL B 18 K K B 504 1555 1555 2.70
LINK OE2 GLU B 20 K K B 504 1555 1555 2.93
LINK O GLU B 84 K K B 503 1555 1555 2.67
LINK O GLY B 93 K K B 503 1555 1555 2.81
LINK O GLU B 94 K K B 503 1555 1555 2.86
LINK O TYR B 96 K K B 503 1555 1555 2.74
LINK SG CYS B 357 FE HEM B 501 1555 1555 2.36
LINK K K A 504 O HOH A 872 1555 1555 2.84
LINK K K A 504 O HOH A 881 1555 1555 3.09
LINK K K B 503 O HOH B 913 1555 1555 2.84
LINK K K B 503 O HOH B 918 1555 1555 2.91
LINK K K B 504 O HOH B 764 1555 1555 2.88
LINK OG1 THR A 217 K K B 504 1555 2645 2.94
LINK K K B 504 O HOH A 748 1555 2655 2.77
CISPEP 1 ILE A 88 PRO A 89 0 6.99
CISPEP 2 ILE A 99 PRO A 100 0 8.41
CISPEP 3 PRO A 105 PRO A 106 0 2.02
CISPEP 4 ILE B 88 PRO B 89 0 1.82
CISPEP 5 ILE B 99 PRO B 100 0 10.53
CISPEP 6 PRO B 105 PRO B 106 0 4.87
SITE 1 AC1 6 GLU A 84 GLY A 93 GLU A 94 TYR A 96
SITE 2 AC1 6 HOH A 872 HOH A 881
SITE 1 AC2 6 GLU B 84 GLY B 93 GLU B 94 TYR B 96
SITE 2 AC2 6 HOH B 918 HOH B 913
SITE 1 AC3 6 LEU B 14 PRO B 15 PRO B 16 VAL B 18
SITE 2 AC3 6 GLU B 20 HOH B 764
SITE 1 AC4 18 PRO A 100 THR A 101 GLN A 108 ARG A 112
SITE 2 AC4 18 LEU A 244 LEU A 245 GLY A 248 THR A 252
SITE 3 AC4 18 ASP A 297 ARG A 299 GLN A 322 THR A 349
SITE 4 AC4 18 PHE A 350 GLY A 351 HIS A 355 CYS A 357
SITE 5 AC4 18 CAM A 502 HOH A 732
SITE 1 AC5 3 PHE A 87 TYR A 96 HEM A 501
SITE 1 AC6 10 PRO A 268 ARG A 271 GLN A 272 ILE A 275
SITE 2 AC6 10 PRO A 379 ASP A 380 HOH A 740 HOH A 708
SITE 3 AC6 10 HOH A 778 GLU B 172
SITE 1 AC7 20 PRO B 100 THR B 101 GLN B 108 ARG B 112
SITE 2 AC7 20 LEU B 244 LEU B 245 GLY B 248 THR B 252
SITE 3 AC7 20 ASP B 297 ARG B 299 GLN B 322 THR B 349
SITE 4 AC7 20 PHE B 350 GLY B 351 HIS B 355 CYS B 357
SITE 5 AC7 20 GLY B 359 CAM B 502 HOH B 657 HOH B 730
SITE 1 AC8 3 PHE B 87 TYR B 96 HEM B 501
CRYST1 67.400 62.700 95.500 90.00 90.65 90.00 P 1 21 1 4
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 0.014837 0.000000 0.000168 0.00000
SCALE2 0.000000 0.015949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010472 0.00000
MTRIX1 1 -0.973500 0.016000 0.228000 32.81110 1
MTRIX2 1 0.021000 0.999600 0.019300 -29.72220 1
MTRIX3 1 -0.227600 0.023600 -0.973500 47.19460 1
(ATOM LINES ARE NOT SHOWN.)
END
