HEADER OXIDOREDUCTASE 17-JUN-14 4UPM
TITLE STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN
TITLE 2 IN COMPLEX WITH N',N'-{[(2R)-3-AMINOPROPANE-1,2-DIYL]
TITLE 3 BIS(OXYMETHANEDIYLBENZENE-3,1-DIYL)}DITHIOPHENE-2-CARBOXIMIDAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURONAL NITRIC OXIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN, RESIDUES 297-718;
COMPND 5 EC: 1.14.13.39;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCWORI
KEYWDS OXIDOREDUCTASE, INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 3 24-SEP-14 4UPM 1 JRNL
REVDAT 2 03-SEP-14 4UPM 1 JRNL
REVDAT 1 20-AUG-14 4UPM 0
JRNL AUTH Q.JING,H.LI,L.J.ROMAN,P.MARTASEK,T.L.POULOS,R.B.SILVERMAN
JRNL TITL COMBINATION OF CHIRAL LINKERS WITH THIOPHENECARBOXIMIDAMIDE
JRNL TITL 2 HEADS TO IMPROVE THE SELECTIVITY OF INHIBITORS OF NEURONAL
JRNL TITL 3 NITRIC OXIDE SYNTHASE.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 4504 2014
JRNL REFN ISSN 0960-894X
JRNL PMID 25149509
JRNL DOI 10.1016/J.BMCL.2014.07.079
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 92.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.95
REMARK 3 NUMBER OF REFLECTIONS : 71853
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) : 0.17869
REMARK 3 R VALUE (WORKING SET) : 0.17703
REMARK 3 FREE R VALUE : 0.21018
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3746
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) : 1.903
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.952
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4781
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.274
REMARK 3 BIN FREE R VALUE SET COUNT : 248
REMARK 3 BIN FREE R VALUE : 0.280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6659
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 201
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.69
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.990
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.86
REMARK 3 B22 (A**2) : 0.59
REMARK 3 B33 (A**2) : -2.45
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.129
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7065 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4801 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9610 ; 2.017 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11622 ; 0.938 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 814 ; 5.881 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 331 ;33.985 ;23.837
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1166 ;14.345 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;16.134 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 990 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7805 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1548 ; 0.011 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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): 11.3570 4.7100 22.6810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: 0.1500
REMARK 3 T33: 0.0203 T12: -0.0042
REMARK 3 T13: 0.0199 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.5479 L22: 0.8186
REMARK 3 L33: 5.4458 L12: -0.1456
REMARK 3 L13: -0.4705 L23: -0.2806
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: 0.1236 S13: 0.0160
REMARK 3 S21: -0.0115 S22: -0.0456 S23: 0.0544
REMARK 3 S31: 0.0438 S32: -0.3949 S33: 0.1025
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): 12.3290 4.7900 60.1890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0741 T22: 0.0987
REMARK 3 T33: 0.0191 T12: 0.0215
REMARK 3 T13: 0.0232 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.7662 L22: 0.8606
REMARK 3 L33: 2.3826 L12: -0.1140
REMARK 3 L13: -0.1944 L23: 0.3825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0191 S12: -0.0413 S13: 0.0791
REMARK 3 S21: -0.0973 S22: -0.0410 S23: -0.0215
REMARK 3 S31: 0.0736 S32: 0.0810 S33: 0.0601
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. U VALUES WITH TLS ADDED.
REMARK 3 RESIDUES 339 TO 349 IN CHAIN A AND 339 TO 347 IN CHAIN B
REMARK 3 ARE DISORDERED.
REMARK 4
REMARK 4 4UPM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-14.
REMARK 100 THE PDBE ID CODE IS EBI-60963.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-12
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (Q315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75569
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.90
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.56
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-22% PEG3350 0.1M MES, PH5.8
REMARK 280 140-200 MM AMMONIUM ACETATE 10% ETHYLENE GLYCOL 5 MM GSH
REMARK 280 30UM SDS
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 26.03200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.62600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.67900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.62600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.03200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.67900
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: 10120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.6 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 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 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 717 CA C O CB CG CD CE NZ
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 -2.40 63.23
REMARK 500 THR A 466 -89.36 -116.61
REMARK 500 ASP A 489 -42.39 -26.20
REMARK 500 PHE A 517 55.09 -141.31
REMARK 500 CYS A 582 56.25 -150.07
REMARK 500 ARG A 603 -138.43 -112.78
REMARK 500 THR B 466 -87.04 -115.74
REMARK 500 CYS B 582 54.41 -151.32
REMARK 500 ARG B 603 -134.04 -117.31
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 A 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEM A 750 ND
REMARK 620 2 HEM A 750 NB 162.2
REMARK 620 3 HEM A 750 NC 90.1 88.1
REMARK 620 4 CYS A 415 SG 101.2 96.6 100.7
REMARK 620 5 HEM A 750 NA 87.3 86.7 154.6 104.6
REMARK 620 N 1 2 3 4
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 HEM B 750 NB
REMARK 620 2 CYS B 415 SG 99.4
REMARK 620 3 HEM B 750 NC 90.2 102.7
REMARK 620 4 HEM B 750 ND 161.0 99.6 86.6
REMARK 620 5 HEM B 750 NA 85.7 105.8 151.5 88.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1717 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS B 331 SG 104.6
REMARK 620 3 CYS A 331 SG 114.8 99.8
REMARK 620 4 CYS B 326 SG 120.1 112.3 103.6
REMARK 620 N 1 2 3
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 H4B A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I5U A 800
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 HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I5U B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1717
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UPN RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH (S)-1,2-BIS(N-(3-(
REMARK 900 METHOXYPHENYL)THIOPHENE-2-CARBOXIMIDAMIDE))-PROPANE-3-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4UPO RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N-[3-({[(3S,5S)-5-{[(3-{[(Z
REMARK 900 )-IMINO(THIOPHEN-2-YL)METHYL]AMINO}BENZYL)OXY]METHYL
REMARK 900 }PYRROLIDIN-3-YL]OXY}METHYL)PHENYL]THIOPHENE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UPP RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N'-[4-[[(2S,4R)-4-[3-[(C-
REMARK 900 THIOPHEN-2-YLCARBONIMIDOYL)AMINO]PHENOXY]PYRROLIDIN-2-YL
REMARK 900 ]METHOXY]PHENYL]THIOPHENE-2-CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UPQ RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH (R)-1,2-BIS(N-(3-(
REMARK 900 METHOXYPHENYL)THIOPHENE-2-CARBOXIMIDAMIDE))-PROPANE-3-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4UPR RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH (S)-1,2-BIS(N-(3-(
REMARK 900 METHOXYPHENYL)THIOPHENE-2-CARBOXIMIDAMIDE))-PROPANE-3-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4UPS RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH N-(3-((((2S,4S)-4-(((3
REMARK 900 -(THIOPHENE-2-CARBOXIMIDAMIDO)BENZYL)OXY)METHYL)
REMARK 900 PYRROLIDIN-2-YL)OXY)METHYL)PHENYL)THIOPHENE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UPT RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH N'-[4-[[(2S,4R)-4-[3
REMARK 900 -[(C-THIOPHEN-2-YLCARBONIMIDOYL)AMINO]PHENOXY]PYRROLIDIN
REMARK 900 -2-YL]METHOXY]PHENYL]THIOPHENE-2-CARBOXIMIDAMIDE
DBREF 4UPM A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 4UPM 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 H4B A 760 17
HET I5U A 800 36
HET ACT A 860 4
HET HEM B 750 43
HET H4B B 760 17
HET I5U B 800 36
HET ACT B 860 4
HET ZN A1717 1
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM I5U N',N'-{[(2R)-3-AMINOPROPANE-1,2-DIYL]
HETNAM 2 I5U BIS(OXYMETHANEDIYLBENZENE-3,1-DIYL)}DITHIOPHENE-2-
HETNAM 3 I5U CARBOXIMIDAMIDE
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETSYN HEM HEME
FORMUL 2 H4B 2(C9 H15 N5 O3)
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 I5U 2(C27 H29 N5 O2 S2)
FORMUL 5 ZN ZN 2+
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 7 HOH *331(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 GLY A 509 1 12
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 ASP A 615 1 10
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 THR A 688 HIS A 692 5 5
HELIX 20 20 ASP A 709 HIS A 714 1 6
HELIX 21 21 THR B 315 SER B 320 5 6
HELIX 22 22 THR B 350 ILE B 369 1 20
HELIX 23 23 SER B 374 SER B 392 1 19
HELIX 24 24 LYS B 397 ASN B 411 1 15
HELIX 25 25 GLY B 417 TRP B 421 5 5
HELIX 26 26 THR B 434 ASN B 451 1 18
HELIX 27 27 LYS B 452 ASN B 454 5 3
HELIX 28 28 ASN B 498 GLN B 508 1 11
HELIX 29 29 PRO B 537 VAL B 541 5 5
HELIX 30 30 PHE B 551 GLY B 558 5 8
HELIX 31 31 GLY B 590 VAL B 595 1 6
HELIX 32 32 VAL B 595 ASP B 600 1 6
HELIX 33 33 ILE B 606 MET B 614 1 9
HELIX 34 34 LYS B 620 SER B 623 5 4
HELIX 35 35 LEU B 624 ASP B 644 1 21
HELIX 36 36 ASP B 650 GLY B 670 1 21
HELIX 37 37 ASP B 675 VAL B 680 1 6
HELIX 38 38 SER B 684 THR B 688 5 5
HELIX 39 39 THR B 688 HIS B 692 5 5
HELIX 40 40 ASP B 709 HIS B 714 1 6
SHEET 1 AA 2 LEU A 301 LYS A 304 0
SHEET 2 AA 2 VAL A 311 ASP A 314 -1 O LEU A 312 N VAL A 303
SHEET 1 AB 4 GLN A 425 ASP A 428 0
SHEET 2 AB 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 AB 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 AB 4 ALA A 566 VAL A 567 -1 O VAL A 567 N PHE A 584
SHEET 1 AC 3 ARG A 473 VAL A 474 0
SHEET 2 AC 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 AC 3 GLU A 532 PHE A 534 -1 O GLU A 532 N LEU A 524
SHEET 1 AD 2 GLY A 484 LYS A 486 0
SHEET 2 AD 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 AE 2 GLU A 543 PRO A 545 0
SHEET 2 AE 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 AF 3 LEU A 577 PHE A 579 0
SHEET 2 AF 3 LEU A 571 ILE A 574 -1 O LEU A 572 N PHE A 579
SHEET 3 AF 3 SER A 703 GLU A 705 -1 O SER A 703 N GLU A 573
SHEET 1 AG 2 TYR A 588 MET A 589 0
SHEET 2 AG 2 ILE A 648 VAL A 649 1 N VAL A 649 O TYR A 588
SHEET 1 BA 2 LEU B 301 LYS B 304 0
SHEET 2 BA 2 VAL B 311 ASP B 314 -1 O LEU B 312 N VAL B 303
SHEET 1 BB 4 GLN B 425 ASP B 428 0
SHEET 2 BB 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 BB 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 BB 4 ALA B 566 VAL B 567 -1 O VAL B 567 N PHE B 584
SHEET 1 BC 3 ARG B 473 VAL B 474 0
SHEET 2 BC 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 BC 3 GLU B 532 PHE B 534 -1 O GLU B 532 N LEU B 524
SHEET 1 BD 2 GLY B 484 LYS B 486 0
SHEET 2 BD 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 BE 2 GLU B 543 PRO B 545 0
SHEET 2 BE 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 BF 3 LEU B 577 PHE B 579 0
SHEET 2 BF 3 LEU B 571 ILE B 574 -1 O LEU B 572 N PHE B 579
SHEET 3 BF 3 SER B 703 GLU B 705 -1 O SER B 703 N GLU B 573
SHEET 1 BG 2 TYR B 588 MET B 589 0
SHEET 2 BG 2 ILE B 648 VAL B 649 1 N VAL B 649 O TYR B 588
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.39
LINK ZN ZN A1717 SG CYS B 326 1555 1555 2.39
LINK ZN ZN A1717 SG CYS A 326 1555 1555 2.33
LINK ZN ZN A1717 SG CYS B 331 1555 1555 2.43
LINK ZN ZN A1717 SG CYS A 331 1555 1555 2.39
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.38
CISPEP 1 THR A 701 PRO A 702 0 -3.80
CISPEP 2 THR B 701 PRO B 702 0 -1.04
SITE 1 AC1 16 TRP A 409 ARG A 414 CYS A 415 SER A 457
SITE 2 AC1 16 PHE A 584 SER A 585 TRP A 587 GLU A 592
SITE 3 AC1 16 TRP A 678 TYR A 706 H4B A 760 I5U A 800
SITE 4 AC1 16 HOH A2040 HOH A2098 HOH A2142 HOH A2143
SITE 1 AC2 14 SER A 334 ARG A 596 VAL A 677 TRP A 678
SITE 2 AC2 14 HEM A 750 HOH A2041 HOH A2110 HOH A2132
SITE 3 AC2 14 HOH A2142 TRP B 676 PHE B 691 HIS B 692
SITE 4 AC2 14 GLN B 693 GLU B 694
SITE 1 AC3 11 PRO A 565 VAL A 567 PHE A 584 SER A 585
SITE 2 AC3 11 GLY A 586 TRP A 587 GLU A 592 SER A 602
SITE 3 AC3 11 TYR A 706 HEM A 750 TRP B 306
SITE 1 AC4 2 TRP A 587 HOH A2145
SITE 1 AC5 17 TRP B 409 ARG B 414 CYS B 415 SER B 457
SITE 2 AC5 17 PHE B 584 SER B 585 TRP B 587 GLU B 592
SITE 3 AC5 17 TRP B 678 PHE B 704 TYR B 706 H4B B 760
SITE 4 AC5 17 I5U B 800 HOH B2143 HOH B2183 HOH B2184
SITE 5 AC5 17 HOH B2185
SITE 1 AC6 14 TRP A 676 PHE A 691 HIS A 692 GLU A 694
SITE 2 AC6 14 HOH A2137 SER B 334 ARG B 596 VAL B 677
SITE 3 AC6 14 TRP B 678 HEM B 750 HOH B2045 HOH B2152
SITE 4 AC6 14 HOH B2175 HOH B2185
SITE 1 AC7 12 TRP A 306 PRO B 565 VAL B 567 PHE B 584
SITE 2 AC7 12 SER B 585 GLY B 586 TRP B 587 GLU B 592
SITE 3 AC7 12 TRP B 678 TYR B 706 HEM B 750 HOH B2104
SITE 1 AC8 5 TRP B 587 VAL B 649 HOH B2047 HOH B2166
SITE 2 AC8 5 HOH B2186
SITE 1 AC9 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
CRYST1 52.064 111.358 165.252 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 0.019207 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008980 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006051 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
