HEADER OXIDOREDUCTASE 20-OCT-14 4D2Y
TITLE STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN
TITLE 2 IN COMPLEX WITH (1R,2R)-2-(3-FLUOROBENZYL)-N-{2-[2-(1H-IMIDAZOL-
TITLE 3 1-YL)PYRIMIDIN-4-YL]ETHYL}CYCLOPROPANAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME DOMAIN, UNP RESIDUES 297-718;
COMPND 5 SYNONYM: BNOS, CONSTITUTIVE NOS, NC-NOS, NOS TYPE I, NEURONAL NOS,
COMPND 6 N-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 2 04-MAR-15 4D2Y 1 JRNL
REVDAT 1 24-DEC-14 4D2Y 0
JRNL AUTH P.MUKHERJEE,H.LI,I.SEVRIOUKOVA,G.CHREIFI,P.MARTASEK,
JRNL AUTH 2 L.J.ROMAN,T.L.POULOS,R.B.SILVERMAN
JRNL TITL NOVEL 2,4-DISUBSTITUTED PYRIMIDINES AS POTENT, SELECTIVE,
JRNL TITL 2 AND CELL-PERMEABLE INHIBITORS OF NEURONAL NITRIC OXIDE
JRNL TITL 3 SYNTHASE.
JRNL REF J.MED.CHEM. V. 58 1067 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25489882
JRNL DOI 10.1021/JM501719E
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.981
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.840
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.34
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.82
REMARK 3 NUMBER OF REFLECTIONS : 65093
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1724
REMARK 3 R VALUE (WORKING SET) : 0.1705
REMARK 3 FREE R VALUE : 0.2083
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9
REMARK 3 FREE R VALUE TEST SET COUNT : 3217
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.8506 - 5.6297 0.98 2935 150 0.1621 0.1737
REMARK 3 2 5.6297 - 4.4699 0.99 2790 164 0.1385 0.1521
REMARK 3 3 4.4699 - 3.9053 0.99 2790 142 0.1353 0.1546
REMARK 3 4 3.9053 - 3.5484 0.99 2739 151 0.1438 0.2017
REMARK 3 5 3.5484 - 3.2941 0.99 2734 148 0.1633 0.1731
REMARK 3 6 3.2941 - 3.1000 0.99 2751 129 0.1820 0.2349
REMARK 3 7 3.1000 - 2.9448 0.99 2719 155 0.1894 0.2411
REMARK 3 8 2.9448 - 2.8166 0.99 2721 142 0.1860 0.2319
REMARK 3 9 2.8166 - 2.7082 0.99 2682 138 0.1795 0.2420
REMARK 3 10 2.7082 - 2.6147 0.99 2704 130 0.1906 0.2155
REMARK 3 11 2.6147 - 2.5330 0.99 2713 149 0.1831 0.2508
REMARK 3 12 2.5330 - 2.4606 0.98 2662 130 0.1780 0.2531
REMARK 3 13 2.4606 - 2.3958 0.98 2705 129 0.1893 0.2579
REMARK 3 14 2.3958 - 2.3374 0.98 2688 140 0.1839 0.2310
REMARK 3 15 2.3374 - 2.2842 0.98 2659 148 0.1876 0.2463
REMARK 3 16 2.2842 - 2.2356 0.98 2614 169 0.2114 0.3043
REMARK 3 17 2.2356 - 2.1909 0.98 2671 140 0.2237 0.2900
REMARK 3 18 2.1909 - 2.1496 0.98 2654 124 0.2254 0.3192
REMARK 3 19 2.1496 - 2.1112 0.98 2673 127 0.2130 0.2649
REMARK 3 20 2.1112 - 2.0754 0.97 2609 116 0.2208 0.2862
REMARK 3 21 2.0754 - 2.0419 0.95 2601 148 0.2369 0.2881
REMARK 3 22 2.0419 - 2.0105 0.94 2537 133 0.2419 0.2968
REMARK 3 23 2.0105 - 1.9809 0.93 2525 115 0.2657 0.3562
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.23
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 7065
REMARK 3 ANGLE : 1.155 9620
REMARK 3 CHIRALITY : 0.075 996
REMARK 3 PLANARITY : 0.005 1215
REMARK 3 DIHEDRAL : 15.164 2572
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 299:716)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2908 4.7847 22.5231
REMARK 3 T TENSOR
REMARK 3 T11: 0.1940 T22: 0.2178
REMARK 3 T33: 0.2384 T12: -0.0180
REMARK 3 T13: 0.0161 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.9538 L22: 1.2139
REMARK 3 L33: 6.9325 L12: -0.1713
REMARK 3 L13: -0.4977 L23: 0.1068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0264 S12: 0.1611 S13: -0.0103
REMARK 3 S21: 0.0451 S22: -0.1083 S23: 0.0442
REMARK 3 S31: 0.1173 S32: -0.4302 S33: 0.0626
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 299:718)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3507 4.8332 59.9018
REMARK 3 T TENSOR
REMARK 3 T11: 0.1667 T22: 0.2009
REMARK 3 T33: 0.2413 T12: 0.0121
REMARK 3 T13: 0.0369 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.9753 L22: 1.2296
REMARK 3 L33: 3.2081 L12: -0.2144
REMARK 3 L13: -0.0890 L23: 0.3459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0078 S12: -0.0277 S13: 0.0671
REMARK 3 S21: -0.1203 S22: -0.0528 S23: -0.0585
REMARK 3 S31: 0.1572 S32: 0.0862 S33: 0.0466
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 339 TO 349 IN CHAIN A AND 339
REMARK 3 TO 347 IN CHAIN B ARE DISORDERED.
REMARK 4
REMARK 4 4D2Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-14.
REMARK 100 THE PDBE ID CODE IS EBI-62002.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-14
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 (QUANTUM 315R)
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 : 65187
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.98
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.0
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.9
REMARK 200 R MERGE FOR SHELL (I) : 1.00
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.80
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: RMERGE GREATER THAN 1.0 RPIM 0.744 CC ONE HALF 0.
REMARK 200 317
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: 20-24% PEG3350, 0.1M MES, 10%
REMARK 280 ETHYLENE GLYCOL, 140-200 MM AMMONIUM ACETATE, 5 MM GSH, 35UM
REMARK 280 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 25.92600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.09600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.23250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.09600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.92600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.23250
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: 9600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.2 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 LYS A 423 46.90 -108.12
REMARK 500 THR A 466 -77.22 -110.83
REMARK 500 SER A 491 -154.77 -75.25
REMARK 500 ARG A 514 61.29 25.35
REMARK 500 LYS A 550 -53.59 -137.25
REMARK 500 CYS A 582 59.57 -151.45
REMARK 500 ARG A 603 -135.20 -124.25
REMARK 500 ASP B 352 -75.66 -36.11
REMARK 500 THR B 466 -87.45 -111.91
REMARK 500 CYS B 582 59.75 -147.66
REMARK 500 ARG B 603 -137.61 -121.38
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 L5Z A 800 N01 87.3
REMARK 620 3 HEM A 750 NA 92.8 89.6
REMARK 620 4 HEM A 750 NB 174.7 87.5 88.2
REMARK 620 5 HEM A 750 NC 87.5 88.9 178.5 91.5
REMARK 620 6 CYS A 415 SG 95.5 176.6 92.2 89.7 89.3
REMARK 620 N 1 2 3 4 5
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 HEM B 750 NA 85.6
REMARK 620 3 CYS B 415 SG 91.2 91.1
REMARK 620 4 HEM B 750 ND 175.0 93.7 93.8
REMARK 620 5 HEM B 750 NC 93.9 178.1 90.7 86.7
REMARK 620 6 L5Z B 800 N01 84.1 87.9 175.3 90.9 90.2
REMARK 620 N 1 2 3 4 5
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 331 SG
REMARK 620 2 CYS A 326 SG 113.9
REMARK 620 3 CYS B 331 SG 101.9 102.2
REMARK 620 4 CYS B 326 SG 103.9 118.3 115.7
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 L5Z 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 L5Z 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: 4D2Z RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)ETHYL-(R,S)-2-(3-FLUOROBENZYL)
REMARK 900 CYCLOPROPAN-1-AMINE
REMARK 900 RELATED ID: 4D30 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)ETHYL-3-(PYRIDIN-3-YL)PROPAN-1-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4D31 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)-N-(3-CYANOBENZYL)ETHAN-1-AMINE
REMARK 900 RELATED ID: 4D32 RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 3-(3-FLUOROPHENYL)-N-2-(2-(
REMARK 900 5-METHYL-1H-IMIDAZOL-1-YL)PYRIMIDIN-4-YL)ETHYLPROPAN
REMARK 900 -1-AMINE
REMARK 900 RELATED ID: 4D33 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH (N1-(2-(1H-IMIDAZOL-1-
REMARK 900 YL)PYRIMIDIN-4-YL)-N2-(3-FLUOROPHENETHYL)ETHANE-1,2
REMARK 900 -DIAMINE
REMARK 900 RELATED ID: 4D34 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 2-(2-(1H-IMIDAZOL-1-YL
REMARK 900 )PYRIMIDIN-4-YL)-N-(3-FLUOROPHENETHYL)ETHAN-1-AMINE
REMARK 900 RELATED ID: 4D35 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1
REMARK 900 -YL)PYRIMIDIN-4-YL)ETHYL-3-(3-FLUOROPHENYL)PROPAN-1
REMARK 900 -AMINE
REMARK 900 RELATED ID: 4D36 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1
REMARK 900 -YL)PYRIMIDIN-4-YL)ETHYL-3-(3-CHLOROPHENYL)PROPAN-1
REMARK 900 -AMINE
REMARK 900 RELATED ID: 4D37 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITHN-{[(1R,2R)-2-(3-
REMARK 900 FLUOROPHENYL)CYCLOPROPYL]METHYL}-2-[2-(1H-IMIDAZOL-1-
REMARK 900 YL)PYRIMIDIN-4-YL]ETHANAMINE
REMARK 900 RELATED ID: 4D38 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1
REMARK 900 -YL)PYRIMIDIN-4-YL)ETHYL-(S,R)-2-(3-FLUOROBENZYL)
REMARK 900 CYCLOPROPAN-1-AMINE
REMARK 900 RELATED ID: 4D39 RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)-N-(3-CYANOBENZYL)ETHAN-1-AMINE
REMARK 900 RELATED ID: 4D3A RELATED DB: PDB
REMARK 900 STRUCTURE OF BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE
REMARK 900 HEME DOMAIN IN COMPLEX WITH 3-(3-FLUOROPHENYL)-N-2
REMARK 900 -(2-(5-METHYL-1H-IMIDAZOL-1-YL)PYRIMIDIN-4-YL)
REMARK 900 ETHYLPROPAN-1-AMINE
REMARK 900 RELATED ID: 4D3B RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N1-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)-N2-(3-FLUOROPHENETHYL)ETHANE-1,2-
REMARK 900 DIAMINE
REMARK 900 RELATED ID: 4V3U RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN NNOS R354A G357D MUTANT HEME DOMAIN
REMARK 900 IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)ETHYL-3-(PYRIDIN-3-YL)PROPAN-1-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4V3V RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N-(2-(1H-IMIDAZOL-1-YL)-4-
REMARK 900 PYRIMIDYLMETHYL)-3-(3-FLUOROPHENYL)PROPAN-1-AMINE
REMARK 900 RELATED ID: 4V3W RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)-N-(3-FLUOROPHENETHYL)ETHAN-1-AMINE
REMARK 900 RELATED ID: 4V3X RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)ETHYL-3-(3-FLUOROPHENYL)PROPAN-1-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4V3Y RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH N-2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)ETHYL-3-(3-CHLOROPHENYL)PROPAN-1-
REMARK 900 AMINE
REMARK 900 RELATED ID: 4V3Z RELATED DB: PDB
REMARK 900 STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME
REMARK 900 DOMAIN IN COMPLEX WITH 2-(2-(1H-IMIDAZOL-1-YL)
REMARK 900 PYRIMIDIN-4-YL)-N-(2-(3-FLUOROPHENYL)CYCLOPROPYLMETHYL)
REMARK 900 ETHAN-1-AMINE
DBREF 4D2Y A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 4D2Y 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 L5Z A 800 25
HET ACT A 860 4
HET HEM B 750 43
HET H4B B 760 17
HET L5Z B 800 25
HET ACT B 860 4
HET ZN A1717 1
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM L5Z (1R,2R)-2-(3-FLUOROBENZYL)-N-{2-[2-(1H-
HETNAM 2 L5Z IMIDAZOL-1-YL)PYRIMIDIN-4-YL]ETHYL}
HETNAM 3 L5Z CYCLOPROPANAMINE
HETNAM ZN ZINC ION
HETNAM ACT ACETATE ION
HETSYN HEM HEME
FORMUL 3 H4B 2(C9 H15 N5 O3)
FORMUL 4 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 L5Z 2(C19 H20 F N5)
FORMUL 6 ZN ZN 2+
FORMUL 7 ACT 2(C2 H3 O2 1-)
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 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 2.43
LINK FE HEM A 750 N01 L5Z A 800 1555 1555 2.28
LINK ZN ZN A1717 SG CYS B 331 1555 1555 2.41
LINK ZN ZN A1717 SG CYS B 326 1555 1555 2.40
LINK ZN ZN A1717 SG CYS A 331 1555 1555 2.37
LINK ZN ZN A1717 SG CYS A 326 1555 1555 2.40
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.50
LINK FE HEM B 750 N01 L5Z B 800 1555 1555 2.27
CISPEP 1 THR A 701 PRO A 702 0 -0.17
CISPEP 2 THR B 701 PRO B 702 0 -0.70
SITE 1 AC1 19 TRP A 409 ARG A 414 CYS A 415 GLY A 417
SITE 2 AC1 19 SER A 457 PHE A 584 SER A 585 GLY A 586
SITE 3 AC1 19 TRP A 587 MET A 589 GLU A 592 TRP A 678
SITE 4 AC1 19 PHE A 704 TYR A 706 H4B A 760 L5Z A 800
SITE 5 AC1 19 HOH A2128 HOH A2129 HOH A2130
SITE 1 AC2 15 SER A 334 ARG A 596 VAL A 677 TRP A 678
SITE 2 AC2 15 HEM A 750 HOH A2012 HOH A2098 HOH A2118
SITE 3 AC2 15 HOH A2129 HOH A2132 TRP B 676 PHE B 691
SITE 4 AC2 15 HIS B 692 GLN B 693 GLU B 694
SITE 1 AC3 7 MET A 336 LEU A 337 GLN A 478 PRO A 565
SITE 2 AC3 7 VAL A 567 HEM A 750 TRP B 306
SITE 1 AC4 2 TRP A 587 SER A 657
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 GLY B 586 TRP B 587
SITE 3 AC5 17 GLU B 592 TRP B 678 PHE B 704 TYR B 706
SITE 4 AC5 17 H4B B 760 L5Z B 800 HOH B2173 HOH B2174
SITE 5 AC5 17 HOH B2175
SITE 1 AC6 15 TRP A 676 PHE A 691 HIS A 692 GLN A 693
SITE 2 AC6 15 GLU A 694 HOH A2122 SER B 334 ARG B 596
SITE 3 AC6 15 VAL B 677 TRP B 678 HEM B 750 HOH B2010
SITE 4 AC6 15 HOH B2142 HOH B2163 HOH B2175
SITE 1 AC7 8 TRP A 306 MET B 336 LEU B 337 GLN B 478
SITE 2 AC7 8 PRO B 565 VAL B 567 TYR B 706 HEM B 750
SITE 1 AC8 2 TRP B 587 HOH B2154
SITE 1 AC9 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
CRYST1 51.852 110.465 164.192 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 0.019286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006090 0.00000
(ATOM LINES ARE NOT SHOWN.)
END