HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 25-MAY-10 3N5W
TITLE STRUCTURE OF NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX
TITLE 2 WITH 6,6'-(2,2'-(PYRIDINE-3,5-DIYL)BIS(ETHANE-2,1-DIYL))BIS(4-
TITLE 3 METHYLPYRIDIN-2-AMINE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ENDOTHELIAL NOS, ENOS, EC-NOS, NOS TYPE III, NOSIII,
COMPND 5 CONSTITUTIVE NOS, CNOS;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NOS3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS HEME ENZYME, NITRIC OXIDE SYNTHASE, SUBSTRATE INHIBITOR, ZN BINDING',
KEYWDS 2 OXIDOREDUCTASE, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,S.L.DELKER,T.L.POULOS
REVDAT 4 06-SEP-23 3N5W 1 REMARK LINK
REVDAT 3 17-JUL-19 3N5W 1 REMARK
REVDAT 2 08-NOV-17 3N5W 1 REMARK
REVDAT 1 09-FEB-11 3N5W 0
JRNL AUTH S.L.DELKER,F.XUE,H.LI,J.JAMAL,R.B.SILVERMAN,T.L.POULOS
JRNL TITL ROLE OF ZINC IN ISOFORM-SELECTIVE INHIBITOR BINDING TO
JRNL TITL 2 NEURONAL NITRIC OXIDE SYNTHASE .
JRNL REF BIOCHEMISTRY V. 49 10803 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 21138269
JRNL DOI 10.1021/BI1013479
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.11
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 95347
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5018
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) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6930
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3170
REMARK 3 BIN FREE R VALUE SET COUNT : 376
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6658
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 203
REMARK 3 SOLVENT ATOMS : 594
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.11000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.270
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7089 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9649 ; 1.241 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 820 ; 5.461 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 333 ;34.235 ;23.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1169 ;13.549 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;16.645 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 985 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5475 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4090 ; 0.648 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6634 ; 1.220 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2999 ; 1.945 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3012 ; 3.146 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 299 A 860
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4100 4.8770 22.5780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0741 T22: 0.0979
REMARK 3 T33: 0.0460 T12: -0.0216
REMARK 3 T13: 0.0072 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.4030 L22: 0.6295
REMARK 3 L33: 3.3716 L12: -0.0109
REMARK 3 L13: -0.2031 L23: -0.2379
REMARK 3 S TENSOR
REMARK 3 S11: -0.0601 S12: 0.1055 S13: 0.0024
REMARK 3 S21: -0.0438 S22: -0.0131 S23: 0.0265
REMARK 3 S31: -0.0236 S32: -0.2374 S33: 0.0732
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 299 B 860
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2900 4.8330 59.9820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0321 T22: 0.0399
REMARK 3 T33: 0.0410 T12: 0.0084
REMARK 3 T13: 0.0154 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.6143 L22: 0.5672
REMARK 3 L33: 1.9964 L12: -0.1198
REMARK 3 L13: -0.1220 L23: 0.2206
REMARK 3 S TENSOR
REMARK 3 S11: -0.0461 S12: -0.0488 S13: 0.0413
REMARK 3 S21: -0.0338 S22: -0.0258 S23: 0.0022
REMARK 3 S31: 0.0064 S32: 0.0348 S33: 0.0719
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3N5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101279
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.59000
REMARK 200 R SYM FOR SHELL (I) : 0.59000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350 100MM MES 100-140MM
REMARK 280 AMMONIUM ACETATE 5MM GSH, 35UM SDS, PH 5.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.17000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.41000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.60500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.41000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.17000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.60500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -196.0 KCAL/MOL
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 CYS A 297
REMARK 465 PRO A 298
REMARK 465 SER A 339
REMARK 465 GLN A 340
REMARK 465 HIS A 341
REMARK 465 THR A 342
REMARK 465 ARG A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
REMARK 465 GLU A 346
REMARK 465 ASP A 347
REMARK 465 VAL A 348
REMARK 465 ARG A 349
REMARK 465 LYS A 717
REMARK 465 GLY A 718
REMARK 465 CYS B 297
REMARK 465 PRO B 298
REMARK 465 SER B 339
REMARK 465 GLN B 340
REMARK 465 HIS B 341
REMARK 465 THR B 342
REMARK 465 ARG B 343
REMARK 465 LYS B 344
REMARK 465 PRO B 345
REMARK 465 GLU B 346
REMARK 465 ASP B 347
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 ASP A 309 -2.67 65.99
REMARK 500 THR A 321 -58.41 -124.00
REMARK 500 LYS A 423 78.03 -106.75
REMARK 500 THR A 466 -91.08 -110.37
REMARK 500 CYS A 582 55.52 -151.74
REMARK 500 ARG A 603 -136.63 -116.10
REMARK 500 THR B 321 -63.77 -122.64
REMARK 500 THR B 466 -84.18 -112.57
REMARK 500 CYS B 582 61.23 -150.38
REMARK 500 ARG B 603 -134.74 -120.29
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 ZN A 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS A 331 SG 114.7
REMARK 620 3 CYS B 326 SG 120.9 103.0
REMARK 620 4 CYS B 331 SG 102.1 101.0 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 415 SG
REMARK 620 2 HEM A 750 NA 97.1
REMARK 620 3 HEM A 750 NB 91.6 89.3
REMARK 620 4 HEM A 750 NC 91.7 171.2 89.7
REMARK 620 5 HEM A 750 ND 97.0 90.3 171.4 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 600 OD1
REMARK 620 2 XFJ A 805 N11 101.5
REMARK 620 3 HIS B 692 NE2 105.9 104.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 719 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 692 NE2
REMARK 620 2 ASP B 600 OD1 105.4
REMARK 620 3 XFJ B 805 N11 103.9 101.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 415 SG
REMARK 620 2 HEM B 750 NA 96.5
REMARK 620 3 HEM B 750 NB 92.8 87.9
REMARK 620 4 HEM B 750 NC 93.6 169.9 91.0
REMARK 620 5 HEM B 750 ND 96.4 90.8 170.8 88.6
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 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 719
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XFJ B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 910
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N5P RELATED DB: PDB
REMARK 900 RELATED ID: 3N5Q RELATED DB: PDB
REMARK 900 RELATED ID: 3N5R RELATED DB: PDB
REMARK 900 RELATED ID: 3N5S RELATED DB: PDB
REMARK 900 RELATED ID: 3N5T RELATED DB: PDB
REMARK 900 RELATED ID: 3N5V RELATED DB: PDB
REMARK 900 RELATED ID: 3N5X RELATED DB: PDB
REMARK 900 RELATED ID: 3N5Y RELATED DB: PDB
REMARK 900 RELATED ID: 3N5Z RELATED DB: PDB
REMARK 900 RELATED ID: 3N60 RELATED DB: PDB
REMARK 900 RELATED ID: 3N61 RELATED DB: PDB
REMARK 900 RELATED ID: 3N62 RELATED DB: PDB
REMARK 900 RELATED ID: 3N63 RELATED DB: PDB
REMARK 900 RELATED ID: 3N64 RELATED DB: PDB
REMARK 900 RELATED ID: 3N65 RELATED DB: PDB
REMARK 900 RELATED ID: 3N66 RELATED DB: PDB
REMARK 900 RELATED ID: 3N67 RELATED DB: PDB
REMARK 900 RELATED ID: 3N68 RELATED DB: PDB
REMARK 900 RELATED ID: 3N69 RELATED DB: PDB
REMARK 900 RELATED ID: 3N6A RELATED DB: PDB
REMARK 900 RELATED ID: 3N6B RELATED DB: PDB
REMARK 900 RELATED ID: 3N6C RELATED DB: PDB
REMARK 900 RELATED ID: 3N6D RELATED DB: PDB
REMARK 900 RELATED ID: 3N6E RELATED DB: PDB
REMARK 900 RELATED ID: 3N6F RELATED DB: PDB
REMARK 900 RELATED ID: 3N6G RELATED DB: PDB
DBREF 3N5W A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 3N5W B 297 718 UNP P29476 NOS1_RAT 297 718
SEQRES 1 A 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 A 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 A 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 A 422 ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 A 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 A 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 A 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 422 THR HIS VAL TRP LYS GLY
SEQRES 1 B 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 B 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 B 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 B 422 ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 B 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 B 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 B 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 422 THR HIS VAL TRP LYS GLY
HET HEM A 750 43
HET XFJ A 800 26
HET XFJ A 805 26
HET ACT A 860 4
HET CL A 910 1
HET ZN A 900 1
HET ZN A 901 1
HET ZN A 719 1
HET HEM B 750 43
HET XFJ B 800 26
HET XFJ B 805 26
HET ACT B 860 4
HET CL B 910 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM XFJ 6,6'-(PYRIDINE-3,5-DIYLDIETHANE-2,1-DIYL)BIS(4-
HETNAM 2 XFJ METHYLPYRIDIN-2-AMINE)
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETNAM ZN ZINC ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 XFJ 4(C21 H25 N5)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 7 CL 2(CL 1-)
FORMUL 8 ZN 3(ZN 2+)
FORMUL 16 HOH *594(H2 O)
HELIX 1 1 THR A 315 SER A 320 5 6
HELIX 2 2 THR A 350 ILE A 369 1 20
HELIX 3 3 SER A 374 SER A 392 1 19
HELIX 4 4 LYS A 397 ASN A 411 1 15
HELIX 5 5 GLY A 417 TRP A 421 5 5
HELIX 6 6 THR A 434 ASN A 451 1 18
HELIX 7 7 LYS A 452 ASN A 454 5 3
HELIX 8 8 ASN A 498 GLN A 508 1 11
HELIX 9 9 PRO A 537 VAL A 541 5 5
HELIX 10 10 PHE A 551 GLY A 558 5 8
HELIX 11 11 GLY A 590 VAL A 595 1 6
HELIX 12 12 VAL A 595 ASP A 600 1 6
HELIX 13 13 ILE A 606 MET A 614 1 9
HELIX 14 14 LYS A 620 SER A 623 5 4
HELIX 15 15 LEU A 624 ASP A 644 1 21
HELIX 16 16 ASP A 650 GLY A 670 1 21
HELIX 17 17 ASP A 675 VAL A 680 1 6
HELIX 18 18 SER A 684 THR A 688 5 5
HELIX 19 19 ASP A 709 THR A 713 5 5
HELIX 20 20 THR B 315 SER B 320 5 6
HELIX 21 21 THR B 350 ILE B 369 1 20
HELIX 22 22 SER B 374 SER B 392 1 19
HELIX 23 23 LYS B 397 ASN B 411 1 15
HELIX 24 24 GLY B 417 TRP B 421 5 5
HELIX 25 25 THR B 434 ASN B 451 1 18
HELIX 26 26 LYS B 452 ASN B 454 5 3
HELIX 27 27 ASN B 498 GLN B 508 1 11
HELIX 28 28 PRO B 537 VAL B 541 5 5
HELIX 29 29 PHE B 551 GLY B 558 5 8
HELIX 30 30 GLY B 590 VAL B 595 1 6
HELIX 31 31 VAL B 595 ASP B 600 1 6
HELIX 32 32 ILE B 606 MET B 614 1 9
HELIX 33 33 LYS B 620 SER B 623 5 4
HELIX 34 34 LEU B 624 ASP B 644 1 21
HELIX 35 35 ASP B 650 GLY B 670 1 21
HELIX 36 36 ASP B 675 VAL B 680 1 6
HELIX 37 37 SER B 684 THR B 688 5 5
HELIX 38 38 ASP B 709 HIS B 714 1 6
SHEET 1 A 2 LEU A 301 LYS A 304 0
SHEET 2 A 2 VAL A 311 ASP A 314 -1 O ASP A 314 N LEU A 301
SHEET 1 B 4 GLN A 425 ASP A 428 0
SHEET 2 B 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 B 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 B 4 ALA A 566 VAL A 567 -1 N VAL A 567 O PHE A 584
SHEET 1 C 3 ARG A 473 VAL A 474 0
SHEET 2 C 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 C 3 GLU A 532 PHE A 534 -1 O PHE A 534 N LEU A 522
SHEET 1 D 2 GLY A 484 LYS A 486 0
SHEET 2 D 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 E 2 GLU A 543 PRO A 545 0
SHEET 2 E 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 F 3 LEU A 577 PHE A 579 0
SHEET 2 F 3 MET A 570 ILE A 574 -1 N LEU A 572 O PHE A 579
SHEET 3 F 3 SER A 703 TYR A 706 -1 O SER A 703 N GLU A 573
SHEET 1 G 2 TYR A 588 MET A 589 0
SHEET 2 G 2 ILE A 648 VAL A 649 1 O VAL A 649 N TYR A 588
SHEET 1 H 2 LEU B 301 LYS B 304 0
SHEET 2 H 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 I 4 GLN B 425 ASP B 428 0
SHEET 2 I 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 I 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 I 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 J 3 ARG B 473 VAL B 474 0
SHEET 2 J 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 J 3 GLU B 532 PHE B 534 -1 O PHE B 534 N LEU B 522
SHEET 1 K 2 GLY B 484 LYS B 486 0
SHEET 2 K 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 L 2 GLU B 543 PRO B 545 0
SHEET 2 L 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 M 3 LEU B 577 PHE B 579 0
SHEET 2 M 3 MET B 570 ILE B 574 -1 N LEU B 572 O PHE B 579
SHEET 3 M 3 SER B 703 TYR B 706 -1 O GLU B 705 N LEU B 571
SHEET 1 N 2 TYR B 588 MET B 589 0
SHEET 2 N 2 ILE B 648 VAL B 649 1 O VAL B 649 N TYR B 588
LINK SG CYS A 326 ZN ZN A 900 1555 1555 2.45
LINK SG CYS A 331 ZN ZN A 900 1555 1555 2.39
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.52
LINK OD1 ASP A 600 ZN ZN A 901 1555 1555 2.03
LINK NE2 HIS A 692 ZN ZN A 719 1555 1555 2.12
LINK ZN ZN A 719 OD1 ASP B 600 1555 1555 2.05
LINK ZN ZN A 719 N11 XFJ B 805 1555 1555 2.04
LINK N11 XFJ A 805 ZN ZN A 901 1555 1555 1.98
LINK ZN ZN A 900 SG CYS B 326 1555 1555 2.42
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.44
LINK ZN ZN A 901 NE2 HIS B 692 1555 1555 2.14
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.52
CISPEP 1 THR A 701 PRO A 702 0 0.17
CISPEP 2 THR B 701 PRO B 702 0 -2.36
SITE 1 AC1 16 TRP A 409 CYS A 415 SER A 457 MET A 570
SITE 2 AC1 16 PHE A 584 SER A 585 TRP A 587 MET A 589
SITE 3 AC1 16 GLU A 592 ARG A 596 TRP A 678 XFJ A 800
SITE 4 AC1 16 XFJ A 805 HOH A1007 HOH A1090 HOH A1124
SITE 1 AC2 12 ARG A 414 GLN A 478 VAL A 567 PHE A 584
SITE 2 AC2 12 TRP A 587 GLU A 592 ARG A 596 TYR A 706
SITE 3 AC2 12 HEM A 750 HOH A1055 HOH A1075 TRP B 306
SITE 1 AC3 11 ASP A 600 VAL A 677 TRP A 678 VAL A 680
SITE 2 AC3 11 HEM A 750 ZN A 901 CL A 910 TRP B 306
SITE 3 AC3 11 ASP B 309 PHE B 691 HIS B 692
SITE 1 AC4 5 TRP A 587 VAL A 649 HOH A1091 HOH A1138
SITE 2 AC4 5 HOH A1193
SITE 1 AC5 4 ASP A 600 XFJ A 805 ZN A 901 HIS B 692
SITE 1 AC6 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC7 4 ASP A 600 XFJ A 805 CL A 910 HIS B 692
SITE 1 AC8 4 HIS A 692 ASP B 600 XFJ B 805 CL B 910
SITE 1 AC9 15 TRP B 409 CYS B 415 SER B 457 MET B 570
SITE 2 AC9 15 PHE B 584 SER B 585 TRP B 587 GLU B 592
SITE 3 AC9 15 ARG B 596 TRP B 678 XFJ B 800 XFJ B 805
SITE 4 AC9 15 HOH B1284 HOH B1368 HOH B1411
SITE 1 BC1 12 TRP A 306 ARG B 414 GLN B 478 VAL B 567
SITE 2 BC1 12 PHE B 584 TRP B 587 GLU B 592 ARG B 596
SITE 3 BC1 12 TYR B 706 HEM B 750 HOH B1347 HOH B1348
SITE 1 BC2 12 TRP A 306 ASP A 309 PHE A 691 HIS A 692
SITE 2 BC2 12 ZN A 719 ASP B 600 VAL B 677 TRP B 678
SITE 3 BC2 12 VAL B 680 HEM B 750 CL B 910 HOH B1465
SITE 1 BC3 6 TRP B 587 VAL B 649 HOH B1344 HOH B1420
SITE 2 BC3 6 HOH B1441 HOH B1498
SITE 1 BC4 6 SER A 686 HIS A 692 ZN A 719 ARG B 596
SITE 2 BC4 6 ASP B 600 XFJ B 805
CRYST1 52.340 111.210 164.820 90.00 90.00 90.00 P 21 21 21 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 0.019106 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006067 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
