HEADER OXIDOREDUCTASE 23-MAR-15 4UH1
TITLE STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX
TITLE 2 WITH N1-(5-(2-(6-AMINO-4-METHYLPYRIDIN-2-YL)ETHYL)PYRIDIN-3- YL)-N1,
TITLE 3 N2-DIMETHYLETHANE-1,2-DIAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN, RESIDUES 297-718;
COMPND 5 SYNONYM: BNOS, CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS, N
COMPND 6 -NOS, NNOS, PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1, NEURONAL NITRIC
COMPND 7 OXIDE SYNTHASE;
COMPND 8 EC: 1.14.13.39;
COMPND 9 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, NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 3 10-JAN-24 4UH1 1 REMARK LINK
REVDAT 2 05-AUG-15 4UH1 1 JRNL
REVDAT 1 15-JUL-15 4UH1 0
JRNL AUTH S.KANG,H.LI,W.TANG,P.MARTASEK,L.J.ROMAN,T.L.POULOS,
JRNL AUTH 2 R.B.SILVERMAN
JRNL TITL 2-AMINOPYRIDINES WITH A TRUNCATED SIDE CHAIN TO IMPROVE
JRNL TITL 2 HUMAN NEURONAL NITRIC OXIDE SYNTHASE INHIBITORY POTENCY AND
JRNL TITL 3 SELECTIVITY.
JRNL REF J.MED.CHEM. V. 58 5548 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26120733
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00573
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 83951
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4392
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5930
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.45
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE SET COUNT : 341
REMARK 3 BIN FREE R VALUE : 0.3070
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 : 173
REMARK 3 SOLVENT ATOMS : 456
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.89000
REMARK 3 B22 (A**2) : 1.14000
REMARK 3 B33 (A**2) : -6.04000
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): 0.134
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.589
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7049 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6518 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9596 ; 1.757 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14998 ; 0.897 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 822 ; 6.117 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 331 ;34.421 ;23.837
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1170 ;14.865 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;19.009 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 996 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7941 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1722 ; 0.007 ; 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 11.4740 4.7500 22.4410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0031 T22: 0.1960
REMARK 3 T33: 0.3662 T12: -0.0089
REMARK 3 T13: 0.0076 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.4421 L22: 0.6061
REMARK 3 L33: 2.3147 L12: -0.0249
REMARK 3 L13: -0.1641 L23: -0.1660
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: 0.0811 S13: 0.0150
REMARK 3 S21: -0.0180 S22: -0.0023 S23: 0.0531
REMARK 3 S31: -0.0216 S32: -0.1072 S33: 0.0273
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): 12.1560 4.6280 59.6500
REMARK 3 T TENSOR
REMARK 3 T11: 0.0226 T22: 0.1554
REMARK 3 T33: 0.3678 T12: 0.0082
REMARK 3 T13: 0.0141 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.5784 L22: 0.6529
REMARK 3 L33: 1.8318 L12: -0.0773
REMARK 3 L13: -0.1230 L23: 0.2782
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: -0.0222 S13: 0.0515
REMARK 3 S21: -0.0834 S22: -0.0142 S23: -0.0180
REMARK 3 S31: 0.0978 S32: 0.0489 S33: 0.0378
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 RIDING
REMARK 3 POSITIONS. U VALUES WITH TLS ADDED RESIDUES 339 TO 349 IN CHAIN
REMARK 3 A AND 339 TO 347 IN CHAIN B ARE DISORDERED.
REMARK 4
REMARK 4 4UH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290060799.
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
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88754
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 : 3.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1OM4
REMARK 200
REMARK 200 REMARK: RPIM 0.285 CC ONE HALF 0.925
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-22% PEG3350 0.1M MES, PH5.8 140-200
REMARK 280 MM AMMONIUM ACETATE 10% ETHYLENE GLYCOL 5 MM GSH 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 26.07750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.04950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.54950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.04950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.07750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.54950
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: 9720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.3 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
REMARK 470 LYS A 717 NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2048 O HOH A 2062 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER B 413 CB SER B 413 OG -0.086
REMARK 500
REMARK 500 REMARK: NULL
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 B 371 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 TYR B 441 CB - CG - CD2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 481 CG - CD - NE ANGL. DEV. = 13.1 DEGREES
REMARK 500 ASP B 675 CB - CG - OD1 ANGL. DEV. = 6.0 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 ASP A 309 -6.81 69.38
REMARK 500 LYS A 423 74.01 -104.54
REMARK 500 THR A 466 -97.21 -111.33
REMARK 500 ASP A 489 -22.52 -26.32
REMARK 500 CYS A 582 57.69 -154.38
REMARK 500 ARG A 603 -133.91 -115.48
REMARK 500 CYS A 672 104.90 -161.41
REMARK 500 THR B 321 -62.85 -131.58
REMARK 500 LEU B 322 -179.93 -57.94
REMARK 500 SER B 392 -3.29 73.48
REMARK 500 THR B 466 -82.74 -113.22
REMARK 500 CYS B 582 58.55 -151.32
REMARK 500 ARG B 603 -135.35 -119.13
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 B 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS A 331 SG 110.2
REMARK 620 3 CYS B 326 SG 121.1 104.2
REMARK 620 4 CYS B 331 SG 104.2 102.6 113.2
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 89.2
REMARK 620 3 HEM A 750 NB 90.0 88.8
REMARK 620 4 HEM A 750 NC 93.6 177.2 91.3
REMARK 620 5 HEM A 750 ND 93.0 90.8 177.0 89.0
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 CYS B 415 SG
REMARK 620 2 HEM B 750 NA 88.8
REMARK 620 3 HEM B 750 NB 91.4 87.3
REMARK 620 4 HEM B 750 NC 94.4 176.7 91.8
REMARK 620 5 HEM B 750 ND 91.5 92.7 177.1 88.2
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 H4B A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EXI 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 EXI 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 B 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UGZ RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
REMARK 900 COMPLEX WITH N1-(3-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)PHENYL)-
REMARK 900 N1,N2-DIMETHYLETHANE- 1,2-DIAMINE
REMARK 900 RELATED ID: 4UH0 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
REMARK 900 COMPLEX WITH N1-(6-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)PYRIDIN-
REMARK 900 2-YL)-N1,N2- DIMETHYLETHANE-1,2-DIAMINE
REMARK 900 RELATED ID: 4UH2 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
REMARK 900 COMPLEX WITH N1-(3-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)-5-
REMARK 900 (TRIFLUOROMETHYL)PHENYL)-N1 ,N2-DIMETHYLETHANE-1,2-DIAMINE
REMARK 900 RELATED ID: 4UH3 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
REMARK 900 COMPLEX WITH N1-(3-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)-5-
REMARK 900 FLUOROPHENYL)-N1,N2- DIMETHYLETHANE-1,2-DIAMINE
REMARK 900 RELATED ID: 4UH4 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
REMARK 900 COMPLEX WITH 3-(2-(6-AMINO-4-METHYLPYRIDIN -2-YL)ETHYL)-5-(METHYL(2-
REMARK 900 (METHYLAMINO)ETHYL)AMINO) BENZONITRILE
REMARK 900 RELATED ID: 4UH5 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN IN COMPLEX
REMARK 900 WITH N1-(5-(2-(6-AMINO-4-METHYLPYRIDIN -2-YL)ETHYL)PYRIDIN-3-YL)-N1,
REMARK 900 N2-DIMETHYLETHANE-1, 2-DIAMINE
REMARK 900 RELATED ID: 4UH6 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN IN COMPLEX
REMARK 900 WITH 3-(2-(6-AMINO-4-METHYLPYRIDIN-2- YL)ETHYL)-5-(METHYL(2-
REMARK 900 (METHYLAMINO)ETHYL)AMINO) BENZONITRILE
REMARK 900 RELATED ID: 4UH7 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN
REMARK 900 IN COMPLEX WITH N1-(3-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)
REMARK 900 PHENYL)-N1,N2-DIMETHYLETHANE- 1,2-DIAMINE
REMARK 900 RELATED ID: 4UH8 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN
REMARK 900 IN COMPLEX WITH N1-(5-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)
REMARK 900 PYRIDIN-3-YL)-N1,N2- DIMETHYLETHANE-1,2-DIAMINE
REMARK 900 RELATED ID: 4UH9 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN
REMARK 900 IN COMPLEX WITH N1-(3-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)-5-
REMARK 900 FLUOROPHENYL)-N1,N2- DIMETHYLETHANE-1,2-DIAMINE
REMARK 900 RELATED ID: 4UHA RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN
REMARK 900 IN COMPLEX WITH 3-(2-(6-AMINO-4- METHYLPYRIDIN-2-YL)ETHYL)-5-
REMARK 900 (METHYL(2-(METHYLAMINO) ETHYL)AMINO)BENZONITRILE
DBREF 4UH1 A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 4UH1 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 EXI A 800 22
HET ACT A 860 4
HET HEM B 750 43
HET H4B B 760 17
HET EXI B 800 22
HET ACT B 860 4
HET ZN B 900 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM EXI N1-(5-(2-(6-AMINO-4-METHYLPYRIDIN-2-YL)ETHYL)PYRIDIN-3-
HETNAM 2 EXI YL)-N1,N2-DIMETHYLETHANE-1,2-DIAMINE
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 EXI 2(C17 H25 N5)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 11 ZN ZN 2+
FORMUL 12 HOH *456(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 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 ASP B 615 1 10
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 326 ZN ZN B 900 1555 1555 2.44
LINK SG CYS A 331 ZN ZN B 900 1555 1555 2.40
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.53
LINK SG CYS B 326 ZN ZN B 900 1555 1555 2.34
LINK SG CYS B 331 ZN ZN B 900 1555 1555 2.42
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.52
CISPEP 1 THR A 701 PRO A 702 0 -5.81
CISPEP 2 THR B 701 PRO B 702 0 -2.39
SITE 1 AC1 17 TRP A 409 CYS A 415 VAL A 416 SER A 457
SITE 2 AC1 17 PHE A 584 SER A 585 TRP A 587 GLU A 592
SITE 3 AC1 17 TRP A 678 TYR A 706 H4B A 760 EXI A 800
SITE 4 AC1 17 HOH A2195 HOH A2196 HOH A2197 HOH A2198
SITE 5 AC1 17 HOH A2199
SITE 1 AC2 15 SER A 334 ARG A 596 VAL A 677 TRP A 678
SITE 2 AC2 15 HEM A 750 HOH A2017 HOH A2146 HOH A2147
SITE 3 AC2 15 HOH A2180 HOH A2198 TRP B 676 PHE B 691
SITE 4 AC2 15 HIS B 692 GLN B 693 GLU B 694
SITE 1 AC3 10 GLN A 478 ARG A 481 TYR A 562 PHE A 584
SITE 2 AC3 10 GLY A 586 TRP A 587 TYR A 588 GLU A 592
SITE 3 AC3 10 HEM A 750 HOH A2198
SITE 1 AC4 2 TRP A 587 HOH A2058
SITE 1 AC5 18 TRP B 409 CYS B 415 SER B 457 PHE B 584
SITE 2 AC5 18 SER B 585 GLY B 586 TRP B 587 GLU B 592
SITE 3 AC5 18 TRP B 678 TYR B 706 H4B B 760 EXI B 800
SITE 4 AC5 18 HOH B2073 HOH B2248 HOH B2253 HOH B2254
SITE 5 AC5 18 HOH B2255 HOH B2256
SITE 1 AC6 13 TRP A 676 PHE A 691 HIS A 692 GLU A 694
SITE 2 AC6 13 SER B 334 ARG B 596 VAL B 677 TRP B 678
SITE 3 AC6 13 HEM B 750 HOH B2018 HOH B2216 HOH B2242
SITE 4 AC6 13 HOH B2256
SITE 1 AC7 14 GLN B 478 ARG B 481 TYR B 562 PRO B 565
SITE 2 AC7 14 VAL B 567 PHE B 584 TRP B 587 TYR B 588
SITE 3 AC7 14 GLU B 592 ARG B 603 HEM B 750 HOH B2019
SITE 4 AC7 14 HOH B2214 HOH B2256
SITE 1 AC8 6 TRP B 587 VAL B 649 HOH B2075 HOH B2080
SITE 2 AC8 6 HOH B2232 HOH B2257
SITE 1 AC9 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
CRYST1 52.155 111.099 164.099 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 0.019174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006094 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
