HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 19-MAY-17 5VUR
TITLE STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX
TITLE 2 WITH 4-(2-(((2-AMINOQUINOLIN-7-YL)METHYL)AMINO)ETHYL)-2-
TITLE 3 METHYLBENZONITRILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 297-718;
COMPND 5 SYNONYM: NEURONAL NITRIC OXIDE SYNTHASE, BNOS, CONSTITUTIVE NOS, NC-
COMPND 6 NOS, NOS TYPE I, NEURONAL NOS, NNOS, PEPTIDYL-CYSTEINE S-NITROSYLASE
COMPND 7 NOS1;
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: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 GENE: NOS1, BNOS;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE, INHIBITOR COMPLEX, HEME ENZYME,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 4 04-OCT-23 5VUR 1 LINK
REVDAT 3 25-DEC-19 5VUR 1 REMARK
REVDAT 2 06-SEP-17 5VUR 1 JRNL
REVDAT 1 16-AUG-17 5VUR 0
JRNL AUTH A.V.PENSA,M.A.CINELLI,H.LI,G.CHREIFI,P.MUKHERJEE,L.J.ROMAN,
JRNL AUTH 2 P.MARTASEK,T.L.POULOS,R.B.SILVERMAN
JRNL TITL HYDROPHILIC, POTENT, AND SELECTIVE 7-SUBSTITUTED
JRNL TITL 2 2-AMINOQUINOLINES AS IMPROVED HUMAN NEURONAL NITRIC OXIDE
JRNL TITL 3 SYNTHASE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 7146 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28776992
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00835
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 65.1
REMARK 3 NUMBER OF REFLECTIONS : 44459
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2183
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 45.9496 - 4.9624 1.00 4349 228 0.1381 0.1577
REMARK 3 2 4.9624 - 3.9395 1.00 4117 229 0.1071 0.1743
REMARK 3 3 3.9395 - 3.4417 1.00 4112 220 0.1347 0.2131
REMARK 3 4 3.4417 - 3.1271 1.00 4107 198 0.1720 0.2374
REMARK 3 5 3.1271 - 2.9030 1.00 4021 231 0.2138 0.2518
REMARK 3 6 2.9030 - 2.7319 1.00 4059 208 0.2251 0.2957
REMARK 3 7 2.7319 - 2.5951 0.94 3806 191 0.2426 0.3046
REMARK 3 8 2.5951 - 2.4821 0.81 3266 174 0.2441 0.3510
REMARK 3 9 2.4821 - 2.3866 0.68 2767 132 0.2682 0.3589
REMARK 3 10 2.3866 - 2.3042 0.55 2222 112 0.2702 0.2813
REMARK 3 11 2.3042 - 2.2322 0.39 1571 97 0.2712 0.3775
REMARK 3 12 2.2322 - 2.1684 0.31 1239 47 0.2632 0.3054
REMARK 3 13 2.1684 - 2.1113 0.24 964 41 0.2639 0.3549
REMARK 3 14 2.1113 - 2.0598 0.18 736 28 0.2752 0.3707
REMARK 3 15 2.0598 - 2.0129 0.14 545 25 0.2496 0.2668
REMARK 3 16 2.0129 - 1.9701 0.10 395 22 0.2356 0.3417
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.007 7071
REMARK 3 ANGLE : 1.165 9621
REMARK 3 CHIRALITY : 0.074 993
REMARK 3 PLANARITY : 0.005 1214
REMARK 3 DIHEDRAL : 15.493 2569
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): 11.3927 4.8214 22.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.2286 T22: 0.1458
REMARK 3 T33: 0.1816 T12: -0.0545
REMARK 3 T13: -0.0010 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.6288 L22: 0.4842
REMARK 3 L33: 5.0497 L12: -0.1190
REMARK 3 L13: -0.4903 L23: -0.0684
REMARK 3 S TENSOR
REMARK 3 S11: -0.1264 S12: 0.1637 S13: -0.0209
REMARK 3 S21: 0.0420 S22: -0.0279 S23: 0.0213
REMARK 3 S31: 0.2039 S32: -0.2542 S33: 0.0675
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 299:718)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3694 4.8247 60.2297
REMARK 3 T TENSOR
REMARK 3 T11: 0.1661 T22: 0.1446
REMARK 3 T33: 0.1705 T12: 0.0398
REMARK 3 T13: 0.0262 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.5537 L22: 0.5652
REMARK 3 L33: 2.6001 L12: -0.1452
REMARK 3 L13: -0.0618 L23: 0.2593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: -0.0394 S13: 0.0417
REMARK 3 S21: -0.0838 S22: -0.0317 S23: -0.0099
REMARK 3 S31: 0.1934 S32: 0.1180 S33: 0.0480
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFLECTION FILE WAS TREATED WITH THE
REMARK 3 DIFFRACTION ANISOTROPY CORRECTION. (HTTPS://
REMARK 3 SERVICES.MBI.UCLA.EDU/ANISOSCALE/).
REMARK 4
REMARK 4 5VUR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000223510.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-15
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 : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.2.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68329
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.26300
REMARK 200 R SYM (I) : 0.26300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : 2.51500
REMARK 200 R SYM FOR SHELL (I) : 2.51500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4
REMARK 200
REMARK 200 REMARK: BRICK
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350, 0.1 M MES, 0.14-0.20 M
REMARK 280 AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 30 UM SDS, 5 MM GSH, PH
REMARK 280 5.8, VAPOR DIFFUSION, 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 26.02500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.59500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.27500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.59500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.02500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.27500
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: 9760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 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: 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 OH TYR B 706 O1D HEM B 801 2.18
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 SER A 392 -1.93 61.73
REMARK 500 ALA A 412 95.66 -68.98
REMARK 500 THR A 466 -83.26 -115.62
REMARK 500 PRO A 513 4.81 -68.42
REMARK 500 ARG A 514 53.86 29.88
REMARK 500 PRO A 549 35.80 -82.50
REMARK 500 LYS A 550 -49.17 -166.14
REMARK 500 CYS A 582 61.51 -154.10
REMARK 500 ARG A 603 -135.49 -128.05
REMARK 500 ASN A 605 62.24 39.80
REMARK 500 ASP B 309 8.59 56.86
REMARK 500 ASP B 352 -71.90 -44.69
REMARK 500 ALA B 412 95.78 -68.66
REMARK 500 LYS B 452 13.70 57.11
REMARK 500 THR B 466 -84.25 -110.15
REMARK 500 CYS B 582 52.07 -151.87
REMARK 500 ARG B 603 -135.92 -116.04
REMARK 500 ASP B 615 70.47 51.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1037 DISTANCE = 5.81 ANGSTROMS
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 805 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS A 331 SG 113.1
REMARK 620 3 CYS B 326 SG 122.0 105.1
REMARK 620 4 CYS B 331 SG 104.4 100.8 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 415 SG
REMARK 620 2 HEM A 801 NA 99.9
REMARK 620 3 HEM A 801 NB 101.6 86.0
REMARK 620 4 HEM A 801 NC 100.2 159.9 88.5
REMARK 620 5 HEM A 801 ND 101.8 88.4 156.6 89.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 415 SG
REMARK 620 2 HEM B 801 NA 97.6
REMARK 620 3 HEM B 801 NB 99.6 86.4
REMARK 620 4 HEM B 801 NC 97.7 164.6 89.0
REMARK 620 5 HEM B 801 ND 97.9 88.6 162.2 91.4
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9P7 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9P7 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 804
DBREF 5VUR A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 5VUR 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 801 43
HET H4B A 802 17
HET 9P7 A 803 24
HET ACT A 804 4
HET ZN A 805 1
HET HEM B 801 43
HET H4B B 802 17
HET 9P7 B 803 24
HET ACT B 804 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM 9P7 4-(2-{[(2-AMINOQUINOLIN-7-YL)METHYL]AMINO}ETHYL)-2-
HETNAM 2 9P7 METHYLBENZONITRILE
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 9P7 2(C20 H20 N4)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 7 ZN ZN 2+
FORMUL 12 HOH *309(H2 O)
HELIX 1 AA1 THR A 315 SER A 320 5 6
HELIX 2 AA2 LYS A 351 ILE A 369 1 19
HELIX 3 AA3 SER A 374 SER A 392 1 19
HELIX 4 AA4 LYS A 397 ASN A 411 1 15
HELIX 5 AA5 GLY A 417 TRP A 421 5 5
HELIX 6 AA6 THR A 434 ASN A 451 1 18
HELIX 7 AA7 LYS A 452 ASN A 454 5 3
HELIX 8 AA8 ASN A 498 GLY A 509 1 12
HELIX 9 AA9 PRO A 537 VAL A 541 5 5
HELIX 10 AB1 PHE A 551 GLY A 558 5 8
HELIX 11 AB2 MET A 589 VAL A 595 1 7
HELIX 12 AB3 VAL A 595 ASP A 600 1 6
HELIX 13 AB4 ILE A 606 MET A 614 1 9
HELIX 14 AB5 LYS A 620 SER A 623 5 4
HELIX 15 AB6 LEU A 624 ASP A 644 1 21
HELIX 16 AB7 ASP A 650 GLY A 670 1 21
HELIX 17 AB8 ASP A 675 VAL A 680 1 6
HELIX 18 AB9 SER A 684 GLN A 693 5 10
HELIX 19 AC1 ASP A 709 THR A 713 5 5
HELIX 20 AC2 THR B 315 SER B 320 5 6
HELIX 21 AC3 THR B 350 ILE B 369 1 20
HELIX 22 AC4 SER B 374 SER B 392 1 19
HELIX 23 AC5 LYS B 397 ASN B 411 1 15
HELIX 24 AC6 GLY B 417 TRP B 421 5 5
HELIX 25 AC7 THR B 434 ASN B 451 1 18
HELIX 26 AC8 LYS B 452 ASN B 454 5 3
HELIX 27 AC9 ASN B 498 GLN B 508 1 11
HELIX 28 AD1 PRO B 537 VAL B 541 5 5
HELIX 29 AD2 TRP B 553 GLY B 558 5 6
HELIX 30 AD3 GLY B 590 VAL B 595 1 6
HELIX 31 AD4 VAL B 595 ASP B 600 1 6
HELIX 32 AD5 ILE B 606 MET B 614 1 9
HELIX 33 AD6 LYS B 620 SER B 623 5 4
HELIX 34 AD7 LEU B 624 ASP B 644 1 21
HELIX 35 AD8 ASP B 650 GLY B 670 1 21
HELIX 36 AD9 ASP B 675 VAL B 680 1 6
HELIX 37 AE1 SER B 684 GLN B 693 5 10
HELIX 38 AE2 ASP B 709 HIS B 714 1 6
SHEET 1 AA1 2 LEU A 301 LYS A 304 0
SHEET 2 AA1 2 VAL A 311 ASP A 314 -1 O ASP A 314 N LEU A 301
SHEET 1 AA2 4 GLN A 425 ASP A 428 0
SHEET 2 AA2 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 AA2 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 AA2 4 ALA A 566 VAL A 567 -1 N VAL A 567 O PHE A 584
SHEET 1 AA3 3 ARG A 473 VAL A 474 0
SHEET 2 AA3 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 AA3 3 GLU A 532 PHE A 534 -1 O PHE A 534 N LEU A 522
SHEET 1 AA4 2 GLY A 484 LYS A 486 0
SHEET 2 AA4 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 AA5 2 GLU A 543 PRO A 545 0
SHEET 2 AA5 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 AA6 3 LEU A 577 PHE A 579 0
SHEET 2 AA6 3 LEU A 571 ILE A 574 -1 N LEU A 572 O PHE A 579
SHEET 3 AA6 3 SER A 703 GLU A 705 -1 O GLU A 705 N LEU A 571
SHEET 1 AA7 2 LEU B 301 LYS B 304 0
SHEET 2 AA7 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 AA8 4 GLN B 425 ASP B 428 0
SHEET 2 AA8 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 AA8 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 AA8 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 AA9 3 ARG B 473 VAL B 474 0
SHEET 2 AA9 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 AA9 3 GLU B 532 PHE B 534 -1 O PHE B 534 N LEU B 522
SHEET 1 AB1 2 GLY B 484 LYS B 486 0
SHEET 2 AB1 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 AB2 2 GLU B 543 PRO B 545 0
SHEET 2 AB2 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 AB3 3 LEU B 577 PHE B 579 0
SHEET 2 AB3 3 LEU B 571 ILE B 574 -1 N ILE B 574 O LEU B 577
SHEET 3 AB3 3 SER B 703 GLU B 705 -1 O GLU B 705 N LEU B 571
SHEET 1 AB4 2 TYR B 588 MET B 589 0
SHEET 2 AB4 2 ILE B 648 VAL B 649 1 O VAL B 649 N TYR B 588
LINK SG CYS A 326 ZN ZN A 805 1555 1555 2.30
LINK SG CYS A 331 ZN ZN A 805 1555 1555 2.33
LINK SG CYS A 415 FE HEM A 801 1555 1555 2.32
LINK ZN ZN A 805 SG CYS B 326 1555 1555 2.41
LINK ZN ZN A 805 SG CYS B 331 1555 1555 2.44
LINK SG CYS B 415 FE HEM B 801 1555 1555 2.34
CISPEP 1 THR A 701 PRO A 702 0 -1.25
CISPEP 2 THR B 701 PRO B 702 0 -2.91
SITE 1 AC1 17 TRP A 409 ALA A 412 ARG A 414 CYS A 415
SITE 2 AC1 17 SER A 457 PHE A 584 SER A 585 GLY A 586
SITE 3 AC1 17 TRP A 587 GLU A 592 PHE A 704 TYR A 706
SITE 4 AC1 17 H4B A 802 9P7 A 803 ACT A 804 HOH A 912
SITE 5 AC1 17 HOH A 957
SITE 1 AC2 13 SER A 334 MET A 336 ARG A 596 VAL A 677
SITE 2 AC2 13 TRP A 678 HEM A 801 HOH A 912 HOH A 920
SITE 3 AC2 13 HOH A 968 TRP B 676 PHE B 691 HIS B 692
SITE 4 AC2 13 GLN B 693
SITE 1 AC3 7 LEU A 337 VAL A 567 TRP A 587 GLU A 592
SITE 2 AC3 7 TRP A 678 HEM A 801 TRP B 306
SITE 1 AC4 3 TRP A 587 VAL A 649 HEM A 801
SITE 1 AC5 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC6 13 TRP B 409 ARG B 414 CYS B 415 PHE B 584
SITE 2 AC6 13 SER B 585 TRP B 587 GLU B 592 TYR B 706
SITE 3 AC6 13 H4B B 802 9P7 B 803 ACT B 804 HOH B 922
SITE 4 AC6 13 HOH B 994
SITE 1 AC7 11 TRP A 676 PHE A 691 SER B 334 MET B 336
SITE 2 AC7 11 ARG B 596 VAL B 677 TRP B 678 HEM B 801
SITE 3 AC7 11 HOH B 931 HOH B1003 HOH B1015
SITE 1 AC8 6 TRP A 306 VAL B 567 TRP B 587 GLU B 592
SITE 2 AC8 6 TRP B 678 HEM B 801
SITE 1 AC9 3 TRP B 587 HEM B 801 HOH B 942
CRYST1 52.050 110.550 165.190 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 0.019212 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009046 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006054 0.00000
(ATOM LINES ARE NOT SHOWN.)
END