HEADER OXIDOREDUCTASE 23-MAR-01 1H9Y
TITLE CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED FORM COMPLEXED TO CN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME CD1 NITRITE REDUCTASE;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS PANTOTROPHUS;
SOURCE 3 ORGANISM_TAXID: 82367;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM;
SOURCE 5 OTHER_DETAILS: ORGANISM FORMERLY KNOWN AS THIOSPHAERA PANTOTROPHA
KEYWDS ENZYME, NITRITE REDUCTASE, OXIDOREDUCTASE, CN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SJOGREN,J.HAJDU
REVDAT 6 13-DEC-23 1H9Y 1 REMARK LINK
REVDAT 5 08-MAY-19 1H9Y 1 REMARK LINK
REVDAT 4 17-JAN-18 1H9Y 1 REMARK
REVDAT 3 24-FEB-09 1H9Y 1 VERSN
REVDAT 2 12-JUN-06 1H9Y 1 SHEET LINK
REVDAT 1 09-AUG-01 1H9Y 0
JRNL AUTH T.SJOGREN,J.HAJDU
JRNL TITL THE STRUCTURE OF AN ALTERNATIVE FORM OF PARACOCCUS
JRNL TITL 2 PANTOTROPHUS CYTOCHROME CD1 NITRITE REDUCTASE
JRNL REF J.BIOL.CHEM. V. 276 29450 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11373294
JRNL DOI 10.1074/JBC.M103657200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.A.WILLIAMS,V.FULOP,E.F.GARMAN,N.F.W.SAUNDERS,S.J.FERGUSON,
REMARK 1 AUTH 2 J.HAJDU
REMARK 1 TITL HAEM LIGAND-SWITCHING DURING CATALYSIS IN CRYSTALS OF A
REMARK 1 TITL 2 NITROGEN CYCLE ENZYME
REMARK 1 REF NATURE V. 389 406 1997
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 9311786
REMARK 1 DOI 10.1038/38775
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.FULOP,J.W.B.MOIR,N.F.W.SAUNDERS,S.J.FERGUSON,J.HAJDU
REMARK 1 TITL THE ANATOMY OF A BIFUNCTIONAL ENZYME: STRUCTURAL BASIS FOR
REMARK 1 TITL 2 REDUCTION OF OXYGEN TO WATER AND SYNTHESIS OF NITRIC OXIDE
REMARK 1 TITL 3 BY CYTOCHROME CD1
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 81 369 1995
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 7736589
REMARK 1 DOI 10.1016/0092-8674(95)90390-9
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 83427
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) : 0.238
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8107
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 202
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.20
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): 0.259
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.610
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.080 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.026 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.024 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.005 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.980 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.184 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.243 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.160 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 15.000; NULL
REMARK 3 PLANAR (DEGREES) : 3.000 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 14.900; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 31.600; 20.000
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: IN SUBUNIT A RESIDUES A 1 - A 47 ARE
REMARK 3 DISORDERED STRUCTURE AND WERE NOT MODELLED. IN SUBUNIT B
REMARK 3 RESIDUES B 1 - B 48 ARE DISORDERED STRUCTURE AND WERE NOT
REMARK 3 MODELLED.
REMARK 4
REMARK 4 1H9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1290005958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0232
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83427
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28700
REMARK 200 R SYM FOR SHELL (I) : 0.28700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1H9X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP USING 2.1 M AMMONIUM
REMARK 280 SULPHATE AND 100 MM CHES PH 7.0 1 MM ASCORMBATE AND 2.5 UM PMS
REMARK 280 FROM REDUCTION OF PROTEIN WAS ALSO PRESENT IN CRYSTALLISATION.,
REMARK 280 PH 9.00, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 131.60050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 63.78650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.78650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 197.40075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.78650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.78650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.80025
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.78650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.78650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 197.40075
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.78650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.78650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.80025
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 131.60050
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 1
REMARK 465 GLU A 2
REMARK 465 GLN A 3
REMARK 465 VAL A 4
REMARK 465 ALA A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 LYS A 8
REMARK 465 ASP A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 GLU A 15
REMARK 465 ASP A 16
REMARK 465 HIS A 17
REMARK 465 LYS A 18
REMARK 465 THR A 19
REMARK 465 ARG A 20
REMARK 465 THR A 21
REMARK 465 ASP A 22
REMARK 465 ASN A 23
REMARK 465 ARG A 24
REMARK 465 TYR A 25
REMARK 465 GLU A 26
REMARK 465 PRO A 27
REMARK 465 SER A 28
REMARK 465 LEU A 29
REMARK 465 ASP A 30
REMARK 465 ASN A 31
REMARK 465 LEU A 32
REMARK 465 ALA A 33
REMARK 465 GLN A 34
REMARK 465 GLN A 35
REMARK 465 ASP A 36
REMARK 465 VAL A 37
REMARK 465 ALA A 38
REMARK 465 ALA A 39
REMARK 465 PRO A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 PRO A 43
REMARK 465 GLU A 44
REMARK 465 GLY A 45
REMARK 465 VAL A 46
REMARK 465 SER A 47
REMARK 465 GLN B 1
REMARK 465 GLU B 2
REMARK 465 GLN B 3
REMARK 465 VAL B 4
REMARK 465 ALA B 5
REMARK 465 PRO B 6
REMARK 465 PRO B 7
REMARK 465 LYS B 8
REMARK 465 ASP B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 14
REMARK 465 GLU B 15
REMARK 465 ASP B 16
REMARK 465 HIS B 17
REMARK 465 LYS B 18
REMARK 465 THR B 19
REMARK 465 ARG B 20
REMARK 465 THR B 21
REMARK 465 ASP B 22
REMARK 465 ASN B 23
REMARK 465 ARG B 24
REMARK 465 TYR B 25
REMARK 465 GLU B 26
REMARK 465 PRO B 27
REMARK 465 SER B 28
REMARK 465 LEU B 29
REMARK 465 ASP B 30
REMARK 465 ASN B 31
REMARK 465 LEU B 32
REMARK 465 ALA B 33
REMARK 465 GLN B 34
REMARK 465 GLN B 35
REMARK 465 ASP B 36
REMARK 465 VAL B 37
REMARK 465 ALA B 38
REMARK 465 ALA B 39
REMARK 465 PRO B 40
REMARK 465 GLY B 41
REMARK 465 ALA B 42
REMARK 465 PRO B 43
REMARK 465 GLU B 44
REMARK 465 GLY B 45
REMARK 465 VAL B 46
REMARK 465 SER B 47
REMARK 465 ALA B 48
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 64 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 255 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 309 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 363 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 363 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 174 CD - NE - CZ ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG B 174 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 174 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 VAL B 199 CB - CA - C ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG B 363 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 GLY B 390 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 ASP B 484 CA - CB - CG ANGL. DEV. = 14.1 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 ALA A 76 -100.51 -144.30
REMARK 500 ASP A 164 78.80 -106.76
REMARK 500 GLU A 297 55.59 -143.38
REMARK 500 ALA A 301 -129.30 -96.79
REMARK 500 ASN A 332 67.02 -109.92
REMARK 500 ALA A 340 -106.68 -125.26
REMARK 500 HIS A 345 -93.77 -139.45
REMARK 500 THR A 386 74.79 62.83
REMARK 500 ALA A 437 -143.18 -113.96
REMARK 500 ALA A 458 41.18 -157.56
REMARK 500 THR A 499 -36.34 -133.27
REMARK 500 GLN A 507 111.77 49.53
REMARK 500 ASP A 547 148.06 -173.87
REMARK 500 THR A 552 65.53 32.09
REMARK 500 THR A 554 -102.38 -122.79
REMARK 500 ALA B 76 -99.61 -142.76
REMARK 500 LEU B 173 78.04 -100.34
REMARK 500 ARG B 174 -72.28 -31.54
REMARK 500 THR B 195 -50.90 -120.21
REMARK 500 ARG B 243 -23.01 -143.35
REMARK 500 GLU B 297 64.17 -150.64
REMARK 500 ALA B 301 -130.55 -95.93
REMARK 500 ASN B 332 69.28 -104.42
REMARK 500 ALA B 340 -103.33 -129.87
REMARK 500 PHE B 343 20.15 81.43
REMARK 500 HIS B 345 -98.38 -131.54
REMARK 500 THR B 386 74.31 56.61
REMARK 500 ALA B 437 -135.36 -116.54
REMARK 500 ALA B 458 36.84 -153.69
REMARK 500 GLN B 507 108.53 51.10
REMARK 500 THR B 552 63.74 37.31
REMARK 500 THR B 554 -93.68 -125.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 SO4 B 621
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 HEC A 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 NE2
REMARK 620 2 HEC A 601 NA 87.2
REMARK 620 3 HEC A 601 NB 90.1 89.7
REMARK 620 4 HEC A 601 NC 91.6 178.2 89.0
REMARK 620 5 HEC A 601 ND 87.5 90.9 177.5 90.3
REMARK 620 6 MET A 106 SD 178.5 91.9 88.7 89.2 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 DHE A 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 200 NE2
REMARK 620 2 DHE A 602 NA 83.8
REMARK 620 3 DHE A 602 NB 98.2 89.6
REMARK 620 4 DHE A 602 NC 97.1 179.1 90.1
REMARK 620 5 DHE A 602 ND 82.4 90.6 179.4 89.7
REMARK 620 6 CYN A 603 N 163.2 81.7 90.1 97.4 89.3
REMARK 620 7 CYN A 603 C 175.4 92.2 83.8 87.0 95.6 12.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 69 NE2
REMARK 620 2 HEC B 601 NA 89.3
REMARK 620 3 HEC B 601 NB 89.0 90.3
REMARK 620 4 HEC B 601 NC 91.3 179.1 89.0
REMARK 620 5 HEC B 601 ND 90.5 91.0 178.6 89.7
REMARK 620 6 MET B 106 SD 172.4 94.4 84.3 85.0 96.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 DHE B 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 200 NE2
REMARK 620 2 DHE B 602 NA 92.1
REMARK 620 3 DHE B 602 NB 100.5 90.5
REMARK 620 4 DHE B 602 NC 94.1 173.5 90.2
REMARK 620 5 DHE B 602 ND 86.0 90.5 173.4 88.1
REMARK 620 6 CYN B 603 C 172.2 86.2 87.2 87.3 86.4
REMARK 620 7 CYN B 603 N 167.6 75.9 76.9 98.0 97.1 14.8
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHE A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHE B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H9X RELATED DB: PDB
REMARK 900 CYTOCHROME CD1 NITRITE REDUCTASE, REDUCED FORM
REMARK 900 RELATED ID: 1HCM RELATED DB: PDB
REMARK 900 CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FROM FROM TETRAGONAL
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1HJ3 RELATED DB: PDB
REMARK 900 CYTOCHROME CD1 NITRITE REDUCTASE, DIOXYGEN COMPLEX
REMARK 900 RELATED ID: 1HJ4 RELATED DB: PDB
REMARK 900 CYTOCHROME CD1 NITRITE REDUCTASE, X-RAY REDUCED DIOXYGEN COMPLEX
REMARK 900 RELATED ID: 1HJ5 RELATED DB: PDB
REMARK 900 CYTOCHROME CD1 NITRITE REDUCTASE, REOXIDISED ENZYME
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 1-47 OF CHAIN A ARE DISORDERED AND
REMARK 999 COULD NOT BE MODELLED
REMARK 999 RESIDUES 1-48 OF CHAIN B ARE DISORDERED.
DBREF 1H9Y A 1 567 UNP Q9FCQ0 Q9FCQ0 30 596
DBREF 1H9Y B 1 567 UNP Q9FCQ0 Q9FCQ0 30 596
SEQRES 1 A 567 GLN GLU GLN VAL ALA PRO PRO LYS ASP PRO ALA ALA ALA
SEQRES 2 A 567 LEU GLU ASP HIS LYS THR ARG THR ASP ASN ARG TYR GLU
SEQRES 3 A 567 PRO SER LEU ASP ASN LEU ALA GLN GLN ASP VAL ALA ALA
SEQRES 4 A 567 PRO GLY ALA PRO GLU GLY VAL SER ALA LEU SER ASP ALA
SEQRES 5 A 567 GLN TYR ASN GLU ALA ASN LYS ILE TYR PHE GLU ARG CYS
SEQRES 6 A 567 ALA GLY CYS HIS GLY VAL LEU ARG LYS GLY ALA THR GLY
SEQRES 7 A 567 LYS ALA LEU THR PRO ASP LEU THR ARG ASP LEU GLY PHE
SEQRES 8 A 567 ASP TYR LEU GLN SER PHE ILE THR TYR GLY SER PRO ALA
SEQRES 9 A 567 GLY MET PRO ASN TRP GLY THR SER GLY GLU LEU SER ALA
SEQRES 10 A 567 GLU GLN VAL ASP LEU MET ALA ASN TYR LEU LEU LEU ASP
SEQRES 11 A 567 PRO ALA ALA PRO PRO GLU PHE GLY MET LYS GLU MET ARG
SEQRES 12 A 567 GLU SER TRP LYS VAL HIS VAL ALA PRO GLU ASP ARG PRO
SEQRES 13 A 567 THR GLN GLN GLU ASN ASP TRP ASP LEU GLU ASN LEU PHE
SEQRES 14 A 567 SER VAL THR LEU ARG ASP ALA GLY GLN ILE ALA LEU ILE
SEQRES 15 A 567 ASP GLY ALA THR TYR GLU ILE LYS SER VAL LEU ASP THR
SEQRES 16 A 567 GLY TYR ALA VAL HIS ILE SER ARG LEU SER ALA SER GLY
SEQRES 17 A 567 ARG TYR LEU PHE VAL ILE GLY ARG ASP GLY LYS VAL ASN
SEQRES 18 A 567 MET ILE ASP LEU TRP MET LYS GLU PRO THR THR VAL ALA
SEQRES 19 A 567 GLU ILE LYS ILE GLY SER GLU ALA ARG SER ILE GLU THR
SEQRES 20 A 567 SER LYS MET GLU GLY TRP GLU ASP LYS TYR ALA ILE ALA
SEQRES 21 A 567 GLY ALA TYR TRP PRO PRO GLN TYR VAL ILE MET ASP GLY
SEQRES 22 A 567 GLU THR LEU GLU PRO LYS LYS ILE GLN SER THR ARG GLY
SEQRES 23 A 567 MET THR TYR ASP GLU GLN GLU TYR HIS PRO GLU PRO ARG
SEQRES 24 A 567 VAL ALA ALA ILE LEU ALA SER HIS TYR ARG PRO GLU PHE
SEQRES 25 A 567 ILE VAL ASN VAL LYS GLU THR GLY LYS ILE LEU LEU VAL
SEQRES 26 A 567 ASP TYR THR ASP LEU ASP ASN LEU LYS THR THR GLU ILE
SEQRES 27 A 567 SER ALA GLU ARG PHE LEU HIS ASP GLY GLY LEU ASP GLY
SEQRES 28 A 567 SER HIS ARG TYR PHE ILE THR ALA ALA ASN ALA ARG ASN
SEQRES 29 A 567 LYS LEU VAL VAL ILE ASP THR LYS GLU GLY LYS LEU VAL
SEQRES 30 A 567 ALA ILE GLU ASP THR GLY GLY GLN THR PRO HIS PRO GLY
SEQRES 31 A 567 ARG GLY ALA ASN PHE VAL HIS PRO THR PHE GLY PRO VAL
SEQRES 32 A 567 TRP ALA THR SER HIS MET GLY ASP ASP SER VAL ALA LEU
SEQRES 33 A 567 ILE GLY THR ASP PRO GLU GLY HIS PRO ASP ASN ALA TRP
SEQRES 34 A 567 LYS ILE LEU ASP SER PHE PRO ALA LEU GLY GLY GLY SER
SEQRES 35 A 567 LEU PHE ILE LYS THR HIS PRO ASN SER GLN TYR LEU TYR
SEQRES 36 A 567 VAL ASP ALA THR LEU ASN PRO GLU ALA GLU ILE SER GLY
SEQRES 37 A 567 SER VAL ALA VAL PHE ASP ILE LYS ALA MET THR GLY ASP
SEQRES 38 A 567 GLY SER ASP PRO GLU PHE LYS THR LEU PRO ILE ALA GLU
SEQRES 39 A 567 TRP ALA GLY ILE THR GLU GLY GLN PRO ARG VAL VAL GLN
SEQRES 40 A 567 GLY GLU PHE ASN LYS ASP GLY THR GLU VAL TRP PHE SER
SEQRES 41 A 567 VAL TRP ASN GLY LYS ASP GLN GLU SER ALA LEU VAL VAL
SEQRES 42 A 567 VAL ASP ASP LYS THR LEU GLU LEU LYS HIS VAL ILE LYS
SEQRES 43 A 567 ASP GLU ARG LEU VAL THR PRO THR GLY LYS PHE ASN VAL
SEQRES 44 A 567 TYR ASN THR MET THR ASP THR TYR
SEQRES 1 B 567 GLN GLU GLN VAL ALA PRO PRO LYS ASP PRO ALA ALA ALA
SEQRES 2 B 567 LEU GLU ASP HIS LYS THR ARG THR ASP ASN ARG TYR GLU
SEQRES 3 B 567 PRO SER LEU ASP ASN LEU ALA GLN GLN ASP VAL ALA ALA
SEQRES 4 B 567 PRO GLY ALA PRO GLU GLY VAL SER ALA LEU SER ASP ALA
SEQRES 5 B 567 GLN TYR ASN GLU ALA ASN LYS ILE TYR PHE GLU ARG CYS
SEQRES 6 B 567 ALA GLY CYS HIS GLY VAL LEU ARG LYS GLY ALA THR GLY
SEQRES 7 B 567 LYS ALA LEU THR PRO ASP LEU THR ARG ASP LEU GLY PHE
SEQRES 8 B 567 ASP TYR LEU GLN SER PHE ILE THR TYR GLY SER PRO ALA
SEQRES 9 B 567 GLY MET PRO ASN TRP GLY THR SER GLY GLU LEU SER ALA
SEQRES 10 B 567 GLU GLN VAL ASP LEU MET ALA ASN TYR LEU LEU LEU ASP
SEQRES 11 B 567 PRO ALA ALA PRO PRO GLU PHE GLY MET LYS GLU MET ARG
SEQRES 12 B 567 GLU SER TRP LYS VAL HIS VAL ALA PRO GLU ASP ARG PRO
SEQRES 13 B 567 THR GLN GLN GLU ASN ASP TRP ASP LEU GLU ASN LEU PHE
SEQRES 14 B 567 SER VAL THR LEU ARG ASP ALA GLY GLN ILE ALA LEU ILE
SEQRES 15 B 567 ASP GLY ALA THR TYR GLU ILE LYS SER VAL LEU ASP THR
SEQRES 16 B 567 GLY TYR ALA VAL HIS ILE SER ARG LEU SER ALA SER GLY
SEQRES 17 B 567 ARG TYR LEU PHE VAL ILE GLY ARG ASP GLY LYS VAL ASN
SEQRES 18 B 567 MET ILE ASP LEU TRP MET LYS GLU PRO THR THR VAL ALA
SEQRES 19 B 567 GLU ILE LYS ILE GLY SER GLU ALA ARG SER ILE GLU THR
SEQRES 20 B 567 SER LYS MET GLU GLY TRP GLU ASP LYS TYR ALA ILE ALA
SEQRES 21 B 567 GLY ALA TYR TRP PRO PRO GLN TYR VAL ILE MET ASP GLY
SEQRES 22 B 567 GLU THR LEU GLU PRO LYS LYS ILE GLN SER THR ARG GLY
SEQRES 23 B 567 MET THR TYR ASP GLU GLN GLU TYR HIS PRO GLU PRO ARG
SEQRES 24 B 567 VAL ALA ALA ILE LEU ALA SER HIS TYR ARG PRO GLU PHE
SEQRES 25 B 567 ILE VAL ASN VAL LYS GLU THR GLY LYS ILE LEU LEU VAL
SEQRES 26 B 567 ASP TYR THR ASP LEU ASP ASN LEU LYS THR THR GLU ILE
SEQRES 27 B 567 SER ALA GLU ARG PHE LEU HIS ASP GLY GLY LEU ASP GLY
SEQRES 28 B 567 SER HIS ARG TYR PHE ILE THR ALA ALA ASN ALA ARG ASN
SEQRES 29 B 567 LYS LEU VAL VAL ILE ASP THR LYS GLU GLY LYS LEU VAL
SEQRES 30 B 567 ALA ILE GLU ASP THR GLY GLY GLN THR PRO HIS PRO GLY
SEQRES 31 B 567 ARG GLY ALA ASN PHE VAL HIS PRO THR PHE GLY PRO VAL
SEQRES 32 B 567 TRP ALA THR SER HIS MET GLY ASP ASP SER VAL ALA LEU
SEQRES 33 B 567 ILE GLY THR ASP PRO GLU GLY HIS PRO ASP ASN ALA TRP
SEQRES 34 B 567 LYS ILE LEU ASP SER PHE PRO ALA LEU GLY GLY GLY SER
SEQRES 35 B 567 LEU PHE ILE LYS THR HIS PRO ASN SER GLN TYR LEU TYR
SEQRES 36 B 567 VAL ASP ALA THR LEU ASN PRO GLU ALA GLU ILE SER GLY
SEQRES 37 B 567 SER VAL ALA VAL PHE ASP ILE LYS ALA MET THR GLY ASP
SEQRES 38 B 567 GLY SER ASP PRO GLU PHE LYS THR LEU PRO ILE ALA GLU
SEQRES 39 B 567 TRP ALA GLY ILE THR GLU GLY GLN PRO ARG VAL VAL GLN
SEQRES 40 B 567 GLY GLU PHE ASN LYS ASP GLY THR GLU VAL TRP PHE SER
SEQRES 41 B 567 VAL TRP ASN GLY LYS ASP GLN GLU SER ALA LEU VAL VAL
SEQRES 42 B 567 VAL ASP ASP LYS THR LEU GLU LEU LYS HIS VAL ILE LYS
SEQRES 43 B 567 ASP GLU ARG LEU VAL THR PRO THR GLY LYS PHE ASN VAL
SEQRES 44 B 567 TYR ASN THR MET THR ASP THR TYR
HET HEC A 601 43
HET DHE A 602 49
HET CYN A 603 2
HET SO4 A 621 5
HET HEC B 601 43
HET DHE B 602 49
HET CYN B 603 2
HET SO4 B 621 4
HET SO4 B 622 5
HETNAM HEC HEME C
HETNAM DHE HEME D
HETNAM CYN CYANIDE ION
HETNAM SO4 SULFATE ION
FORMUL 3 HEC 2(C34 H34 FE N4 O4)
FORMUL 4 DHE 2(C34 H32 FE N4 O10)
FORMUL 5 CYN 2(C N 1-)
FORMUL 6 SO4 3(O4 S 2-)
FORMUL 12 HOH *242(H2 O)
HELIX 1 1 SER A 50 CYS A 65 1 16
HELIX 2 2 CYS A 65 GLY A 70 1 6
HELIX 3 3 THR A 82 GLY A 90 1 9
HELIX 4 4 GLY A 90 GLY A 101 1 12
HELIX 5 5 SER A 116 LEU A 127 1 12
HELIX 6 6 GLY A 138 TRP A 146 1 9
HELIX 7 7 ALA A 151 ARG A 155 5 5
HELIX 8 8 ASP A 164 ASN A 167 5 4
HELIX 9 9 GLU A 463 GLY A 468 1 6
HELIX 10 10 LYS A 476 MET A 478 5 3
HELIX 11 11 PRO A 491 GLY A 497 1 7
HELIX 12 12 VAL A 559 THR A 564 1 6
HELIX 13 13 SER B 50 CYS B 65 1 16
HELIX 14 14 CYS B 65 GLY B 70 1 6
HELIX 15 15 THR B 82 GLY B 90 1 9
HELIX 16 16 LEU B 89 GLY B 101 1 13
HELIX 17 17 ASN B 108 GLY B 113 1 6
HELIX 18 18 SER B 116 LEU B 129 1 14
HELIX 19 19 GLY B 138 TRP B 146 1 9
HELIX 20 20 ALA B 151 ARG B 155 5 5
HELIX 21 21 ASP B 164 GLU B 166 5 3
HELIX 22 22 GLU B 463 GLY B 468 1 6
HELIX 23 23 LYS B 476 MET B 478 5 3
HELIX 24 24 PRO B 491 GLY B 497 1 7
HELIX 25 25 VAL B 559 THR B 564 1 6
SHEET 1 AA 5 LYS A 147 VAL A 148 0
SHEET 2 AA 5 THR A 232 LYS A 237 -1 O GLU A 235 N LYS A 147
SHEET 3 AA 5 LYS A 219 ASP A 224 -1 O VAL A 220 N ILE A 236
SHEET 4 AA 5 TYR A 210 GLY A 215 -1 O LEU A 211 N ILE A 223
SHEET 5 AA 5 VAL A 199 LEU A 204 -1 N HIS A 200 O ILE A 214
SHEET 1 AB 4 ILE A 189 ASP A 194 0
SHEET 2 AB 4 GLN A 178 ILE A 182 -1 O ILE A 179 N LEU A 193
SHEET 3 AB 4 PHE A 169 LEU A 173 -1 O PHE A 169 N ILE A 182
SHEET 4 AB 4 PRO A 553 ASN A 558 -1 N THR A 554 O THR A 172
SHEET 1 AC 4 GLU A 241 THR A 247 0
SHEET 2 AC 4 TYR A 257 TRP A 264 -1 O ILE A 259 N GLU A 246
SHEET 3 AC 4 GLN A 267 ASP A 272 -1 O GLN A 267 N ALA A 262
SHEET 4 AC 4 PRO A 278 SER A 283 -1 N LYS A 279 O ILE A 270
SHEET 1 AD 2 GLY A 286 MET A 287 0
SHEET 2 AD 2 TYR A 294 HIS A 295 -1 O HIS A 295 N GLY A 286
SHEET 1 AE 8 VAL A 300 ALA A 305 0
SHEET 2 AE 8 GLU A 311 VAL A 316 -1 O ILE A 313 N LEU A 304
SHEET 3 AE 8 LYS A 321 ASP A 326 -1 O LYS A 321 N VAL A 316
SHEET 4 AE 8 ASN A 332 SER A 339 -1 O LYS A 334 N ASP A 326
SHEET 5 AE 8 ASN B 332 SER B 339 -1 O LEU B 333 N GLU A 337
SHEET 6 AE 8 LYS B 321 ASP B 326 -1 O ILE B 322 N ILE B 338
SHEET 7 AE 8 GLU B 311 VAL B 316 -1 O PHE B 312 N VAL B 325
SHEET 8 AE 8 VAL B 300 ALA B 305 -1 N ALA B 301 O ASN B 315
SHEET 1 AF 4 LEU A 344 LEU A 349 0
SHEET 2 AF 4 TYR A 355 ALA A 360 -1 O ILE A 357 N GLY A 348
SHEET 3 AF 4 LYS A 365 ASP A 370 -1 O LYS A 365 N ALA A 360
SHEET 4 AF 4 LYS A 375 ASP A 381 -1 O LYS A 375 N ASP A 370
SHEET 1 AG 4 ALA A 393 HIS A 397 0
SHEET 2 AG 4 GLY A 401 THR A 406 -1 O GLY A 401 N HIS A 397
SHEET 3 AG 4 SER A 413 GLY A 418 -1 O ALA A 415 N THR A 406
SHEET 4 AG 4 ILE A 431 PRO A 436 -1 N LEU A 432 O LEU A 416
SHEET 1 AH 4 ILE A 445 LYS A 446 0
SHEET 2 AH 4 TYR A 453 VAL A 456 -1 O TYR A 455 N LYS A 446
SHEET 3 AH 4 VAL A 470 ASP A 474 -1 O ALA A 471 N VAL A 456
SHEET 4 AH 4 PHE A 487 LEU A 490 -1 O LYS A 488 N VAL A 472
SHEET 1 AI 4 ARG A 504 PHE A 510 0
SHEET 2 AI 4 GLU A 516 TRP A 522 -1 O TRP A 518 N GLU A 509
SHEET 3 AI 4 ALA A 530 ASP A 535 -1 O ALA A 530 N VAL A 521
SHEET 4 AI 4 GLU A 540 ILE A 545 -1 O GLU A 540 N ASP A 535
SHEET 1 BA 5 LYS B 147 VAL B 148 0
SHEET 2 BA 5 THR B 232 LYS B 237 -1 O GLU B 235 N LYS B 147
SHEET 3 BA 5 LYS B 219 ASP B 224 -1 O VAL B 220 N ILE B 236
SHEET 4 BA 5 TYR B 210 GLY B 215 -1 O LEU B 211 N ILE B 223
SHEET 5 BA 5 VAL B 199 LEU B 204 -1 N HIS B 200 O ILE B 214
SHEET 1 BB 4 ILE B 189 ASP B 194 0
SHEET 2 BB 4 GLN B 178 ASP B 183 -1 O ILE B 179 N LEU B 193
SHEET 3 BB 4 LEU B 168 LEU B 173 -1 O PHE B 169 N ILE B 182
SHEET 4 BB 4 PRO B 553 ASN B 558 -1 N THR B 554 O THR B 172
SHEET 1 BC 4 GLU B 241 THR B 247 0
SHEET 2 BC 4 TYR B 257 TRP B 264 -1 O ILE B 259 N GLU B 246
SHEET 3 BC 4 GLN B 267 ASP B 272 -1 O GLN B 267 N ALA B 262
SHEET 4 BC 4 PRO B 278 SER B 283 -1 N LYS B 279 O ILE B 270
SHEET 1 BD 2 GLY B 286 MET B 287 0
SHEET 2 BD 2 TYR B 294 HIS B 295 -1 O HIS B 295 N GLY B 286
SHEET 1 BE 4 LEU B 344 LEU B 349 0
SHEET 2 BE 4 TYR B 355 ALA B 360 -1 O ILE B 357 N GLY B 348
SHEET 3 BE 4 LYS B 365 ASP B 370 -1 O LYS B 365 N ALA B 360
SHEET 4 BE 4 LYS B 375 ASP B 381 -1 O LYS B 375 N ASP B 370
SHEET 1 BF 4 ALA B 393 HIS B 397 0
SHEET 2 BF 4 GLY B 401 THR B 406 -1 O GLY B 401 N HIS B 397
SHEET 3 BF 4 SER B 413 GLY B 418 -1 O ALA B 415 N THR B 406
SHEET 4 BF 4 ILE B 431 PRO B 436 -1 N LEU B 432 O LEU B 416
SHEET 1 BG 4 ILE B 445 LYS B 446 0
SHEET 2 BG 4 TYR B 453 VAL B 456 -1 O TYR B 455 N LYS B 446
SHEET 3 BG 4 VAL B 470 ASP B 474 -1 O ALA B 471 N VAL B 456
SHEET 4 BG 4 LYS B 488 LEU B 490 -1 O LYS B 488 N VAL B 472
SHEET 1 BH 4 ARG B 504 PHE B 510 0
SHEET 2 BH 4 GLU B 516 TRP B 522 -1 O TRP B 518 N GLU B 509
SHEET 3 BH 4 ALA B 530 ASP B 535 -1 O ALA B 530 N VAL B 521
SHEET 4 BH 4 GLU B 540 ILE B 545 -1 O GLU B 540 N ASP B 535
LINK SG CYS A 65 CAB HEC A 601 1555 1555 1.88
LINK SG CYS A 68 CAC HEC A 601 1555 1555 1.92
LINK SG CYS B 65 CAB HEC B 601 1555 1555 1.87
LINK SG CYS B 68 CAC HEC B 601 1555 1555 1.90
LINK NE2 HIS A 69 FE HEC A 601 1555 1555 2.02
LINK SD MET A 106 FE HEC A 601 1555 1555 2.12
LINK NE2 HIS A 200 FE DHE A 602 1555 1555 2.05
LINK FE DHE A 602 N CYN A 603 1555 1555 3.06
LINK FE DHE A 602 C CYN A 603 1555 1555 2.04
LINK NE2 HIS B 69 FE HEC B 601 1555 1555 1.98
LINK SD MET B 106 FE HEC B 601 1555 1555 2.06
LINK NE2 HIS B 200 FE DHE B 602 1555 1555 2.04
LINK FE DHE B 602 C CYN B 603 1555 1555 2.04
LINK FE DHE B 602 N CYN B 603 1555 1555 2.99
CISPEP 1 TRP A 264 PRO A 265 0 -3.20
CISPEP 2 TRP B 264 PRO B 265 0 -3.69
SITE 1 AC1 5 GLY A 70 VAL A 71 LEU A 72 ARG A 73
SITE 2 AC1 5 LYS A 74
SITE 1 AC2 5 ARG A 354 LYS A 372 GLU A 373 LYS B 79
SITE 2 AC2 5 HOH B2124
SITE 1 AC3 2 HIS A 307 HIS A 353
SITE 1 AC4 3 HIS A 345 HIS A 388 DHE A 602
SITE 1 AC5 3 HIS B 345 HIS B 388 DHE B 602
SITE 1 AC6 17 ARG A 64 CYS A 65 CYS A 68 HIS A 69
SITE 2 AC6 17 THR A 77 GLY A 78 LYS A 79 TYR A 93
SITE 3 AC6 17 LEU A 94 PHE A 97 SER A 102 ALA A 104
SITE 4 AC6 17 GLY A 105 MET A 106 PRO A 107 TRP A 109
SITE 5 AC6 17 LEU A 127
SITE 1 AC7 25 ARG A 174 HIS A 200 ILE A 201 ARG A 203
SITE 2 AC7 25 ARG A 216 ARG A 243 SER A 244 ILE A 245
SITE 3 AC7 25 TYR A 263 ALA A 301 ALA A 302 ILE A 303
SITE 4 AC7 25 HIS A 345 ARG A 391 PHE A 444 GLN A 507
SITE 5 AC7 25 THR A 554 GLY A 555 PHE A 557 CYN A 603
SITE 6 AC7 25 HOH A2036 HOH A2115 HOH A2116 HOH A2117
SITE 7 AC7 25 HOH A2118
SITE 1 AC8 21 LYS A 372 ARG B 64 CYS B 65 CYS B 68
SITE 2 AC8 21 HIS B 69 THR B 77 GLY B 78 LYS B 79
SITE 3 AC8 21 LEU B 81 LEU B 89 TYR B 93 PHE B 97
SITE 4 AC8 21 ILE B 98 SER B 102 ALA B 104 GLY B 105
SITE 5 AC8 21 MET B 106 PRO B 107 TRP B 109 HOH B2006
SITE 6 AC8 21 HOH B2120
SITE 1 AC9 25 ARG B 174 HIS B 200 ILE B 201 ARG B 203
SITE 2 AC9 25 ARG B 216 ARG B 243 SER B 244 ILE B 245
SITE 3 AC9 25 TYR B 263 ALA B 301 ALA B 302 ILE B 303
SITE 4 AC9 25 HIS B 345 ARG B 391 PHE B 444 GLN B 507
SITE 5 AC9 25 THR B 554 GLY B 555 PHE B 557 CYN B 603
SITE 6 AC9 25 HOH B2031 HOH B2039 HOH B2121 HOH B2122
SITE 7 AC9 25 HOH B2123
CRYST1 127.573 127.573 263.201 90.00 90.00 90.00 P 43 21 2 16
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 0.007839 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007839 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003799 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
