HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18 6NGN
TITLE STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX
TITLE 2 WITH (S)-6-(3-FLUORO-5-(2-(PYRROLIDIN-2-YL)ETHYL)PHENETHYL)-4-
TITLE 3 METHYLPYRIDIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BNOS,CONSTITUTIVE NOS,NC-NOS,NOS TYPE I,NEURONAL NOS,NNOS,
COMPND 5 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 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_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE INHIBITOR COMPLEX HEME ENZYME, OXIDOREDUCTASE,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 4 11-OCT-23 6NGN 1 REMARK
REVDAT 3 04-DEC-19 6NGN 1 REMARK
REVDAT 2 27-MAR-19 6NGN 1 JRNL
REVDAT 1 13-MAR-19 6NGN 0
JRNL AUTH H.T.DO,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN
JRNL TITL OPTIMIZATION OF BLOOD-BRAIN BARRIER PERMEABILITY WITH POTENT
JRNL TITL 2 AND SELECTIVE HUMAN NEURONAL NITRIC OXIDE SYNTHASE
JRNL TITL 3 INHIBITORS HAVING A 2-AMINOPYRIDINE SCAFFOLD.
JRNL REF J. MED. CHEM. V. 62 2690 2019
JRNL REFN ISSN 1520-4804
JRNL PMID 30802056
JRNL DOI 10.1021/ACS.JMEDCHEM.8B02032
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1-2575_1496: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 75796
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 7169
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 49.3777 - 5.8996 1.00 4658 222 0.1469 0.1527
REMARK 3 2 5.8996 - 4.6838 1.00 4622 289 0.1377 0.1841
REMARK 3 3 4.6838 - 4.0921 1.00 4673 254 0.1377 0.1676
REMARK 3 4 4.0921 - 3.7181 1.00 4648 253 0.1514 0.2010
REMARK 3 5 3.7181 - 3.4517 1.00 4656 250 0.1762 0.2173
REMARK 3 6 3.4517 - 3.2482 1.00 4648 212 0.2015 0.2262
REMARK 3 7 3.2482 - 3.0856 1.00 4658 259 0.2131 0.2358
REMARK 3 8 3.0856 - 2.9513 1.00 4640 278 0.2114 0.2517
REMARK 3 9 2.9513 - 2.8377 1.00 4668 239 0.2372 0.3290
REMARK 3 10 2.8377 - 2.7397 1.00 4616 230 0.2551 0.3113
REMARK 3 11 2.7397 - 2.6541 1.00 4714 235 0.2450 0.3010
REMARK 3 12 2.6541 - 2.5782 0.99 4574 246 0.2424 0.2935
REMARK 3 13 2.5782 - 2.5103 1.00 4667 241 0.2443 0.3145
REMARK 3 14 2.5103 - 2.4491 1.00 4681 232 0.2459 0.3129
REMARK 3 15 2.4491 - 2.3934 0.99 4591 240 0.2395 0.3096
REMARK 3 16 2.3934 - 2.3425 1.00 4700 221 0.2534 0.3249
REMARK 3 17 2.3425 - 2.2956 0.99 4610 265 0.2601 0.2982
REMARK 3 18 2.2956 - 2.2523 0.99 4581 279 0.3331 0.4035
REMARK 3 19 2.2523 - 2.2121 0.98 4579 264 0.3248 0.4069
REMARK 3 20 2.2121 - 2.1746 0.99 4634 195 0.2985 0.4221
REMARK 3 21 2.1746 - 2.1395 0.99 4696 209 0.3218 0.4032
REMARK 3 22 2.1395 - 2.1066 0.99 4629 206 0.3272 0.3677
REMARK 3 23 2.1066 - 2.0756 0.99 4599 252 0.3317 0.3889
REMARK 3 24 2.0756 - 2.0464 0.99 4674 245 0.3291 0.3736
REMARK 3 25 2.0464 - 2.0187 0.98 4551 218 0.3262 0.3988
REMARK 3 26 2.0187 - 1.9925 0.96 4490 219 0.3568 0.3921
REMARK 3 27 1.9925 - 1.9676 0.94 4374 289 0.3574 0.4148
REMARK 3 28 1.9676 - 1.9439 0.93 4303 212 0.3802 0.4425
REMARK 3 29 1.9439 - 1.9213 0.89 4114 253 0.4072 0.4340
REMARK 3 30 1.9213 - 1.8997 0.79 3741 162 0.4056 0.4435
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) : 36.820
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 7085
REMARK 3 ANGLE : 0.957 9638
REMARK 3 CHIRALITY : 0.050 998
REMARK 3 PLANARITY : 0.006 1215
REMARK 3 DIHEDRAL : 17.559 4134
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): 11.3628 4.8128 22.6326
REMARK 3 T TENSOR
REMARK 3 T11: 0.3096 T22: 0.3344
REMARK 3 T33: 0.3500 T12: 0.0144
REMARK 3 T13: 0.0081 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 0.6659 L22: 1.1232
REMARK 3 L33: 7.1025 L12: -0.2220
REMARK 3 L13: -0.3837 L23: 0.0966
REMARK 3 S TENSOR
REMARK 3 S11: -0.0303 S12: 0.1090 S13: -0.0007
REMARK 3 S21: 0.1128 S22: -0.1054 S23: 0.0340
REMARK 3 S31: -0.0581 S32: -0.3344 S33: 0.0946
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 299:718)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3866 4.8579 60.2115
REMARK 3 T TENSOR
REMARK 3 T11: 0.2782 T22: 0.3335
REMARK 3 T33: 0.3873 T12: 0.0092
REMARK 3 T13: 0.0469 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.9038 L22: 1.0294
REMARK 3 L33: 3.7096 L12: -0.2524
REMARK 3 L13: -0.0755 L23: 0.3939
REMARK 3 S TENSOR
REMARK 3 S11: 0.0265 S12: -0.0036 S13: 0.0814
REMARK 3 S21: -0.1646 S22: -0.0874 S23: -0.0330
REMARK 3 S31: 0.1319 S32: 0.0978 S33: 0.0526
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6NGN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000236847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-17
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 : 5.0.2
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 : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76983
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 16.70
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : 0.13700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
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) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 4.82700
REMARK 200 R SYM FOR SHELL (I) : 4.82700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1OM4
REMARK 200
REMARK 200 REMARK: BRICKS
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, 0.1M MES 0.14-0.20M
REMARK 280 AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 30UM 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 26.10600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.50950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.92950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.50950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.10600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.92950
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: 9860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 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 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 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 O2D HEM B 801 2.00
REMARK 500 OE1 GLN B 364 O HOH B 901 2.12
REMARK 500 O HOH B 1003 O HOH B 1029 2.13
REMARK 500 O PHE A 517 O HOH A 901 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 PHE A 300 78.96 -113.30
REMARK 500 THR A 321 -56.94 -135.13
REMARK 500 ASP A 489 -38.39 -24.20
REMARK 500 SER A 491 -164.82 -74.01
REMARK 500 ILE A 504 -9.50 -57.77
REMARK 500 GLN A 507 -4.29 -58.51
REMARK 500 PHE A 517 57.89 -115.53
REMARK 500 LYS A 550 -15.07 -143.10
REMARK 500 CYS A 582 55.42 -155.37
REMARK 500 ARG A 603 -131.77 -133.83
REMARK 500 CYS A 672 103.59 -160.39
REMARK 500 VAL A 715 91.01 -59.91
REMARK 500 ASP B 309 11.61 57.81
REMARK 500 THR B 321 -78.55 -121.40
REMARK 500 ARG B 349 133.41 -173.48
REMARK 500 SER B 392 -8.96 75.08
REMARK 500 LYS B 423 70.92 -109.24
REMARK 500 THR B 466 -76.00 -121.31
REMARK 500 CYS B 582 54.27 -149.95
REMARK 500 ARG B 603 -136.87 -124.01
REMARK 500 ASP B 617 94.83 -66.74
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 805 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS A 331 SG 109.7
REMARK 620 3 CYS B 326 SG 117.5 108.4
REMARK 620 4 CYS B 331 SG 107.4 101.7 111.1
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 103.5
REMARK 620 3 HEM A 801 NB 101.0 88.2
REMARK 620 4 HEM A 801 NC 97.0 159.6 87.7
REMARK 620 5 HEM A 801 ND 103.2 86.3 155.7 89.3
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 102.6
REMARK 620 3 HEM B 801 NB 103.5 84.2
REMARK 620 4 HEM B 801 NC 97.4 160.0 91.1
REMARK 620 5 HEM B 801 ND 100.5 85.6 155.4 90.9
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 KL4 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 HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KL4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 805
DBREF 6NGN A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 6NGN 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 KL4 A 803 24
HET ACT A 804 4
HET HEM B 801 43
HET H4B B 802 17
HET KL4 B 803 24
HET ACT B 804 4
HET ZN B 805 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM KL4 6-[2-(3-FLUORO-5-{2-[(2S)-PYRROLIDIN-2-
HETNAM 2 KL4 YL]ETHYL}PHENYL)ETHYL]-4-METHYLPYRIDIN-2-AMINE
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 KL4 2(C20 H26 F N3)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 11 ZN ZN 2+
FORMUL 12 HOH *256(H2 O)
HELIX 1 AA1 THR A 315 SER A 320 5 6
HELIX 2 AA2 THR A 350 ILE A 369 1 20
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 LEU A 424 5 8
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 GLN A 507 1 10
HELIX 9 AA9 PRO A 537 VAL A 541 5 5
HELIX 10 AB1 PHE A 554 GLY A 558 5 5
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 ASP A 615 1 10
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 ARG A 669 1 20
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 PHE B 551 GLY B 558 5 8
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 ASP B 615 1 10
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 THR B 688 5 5
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 LEU B 572 O PHE B 579
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 B 805 1555 1555 2.43
LINK SG CYS A 331 ZN ZN B 805 1555 1555 2.45
LINK SG CYS A 415 FE HEM A 801 1555 1555 2.33
LINK SG CYS B 326 ZN ZN B 805 1555 1555 2.41
LINK SG CYS B 331 ZN ZN B 805 1555 1555 2.43
LINK SG CYS B 415 FE HEM B 801 1555 1555 2.35
CISPEP 1 THR A 701 PRO A 702 0 6.43
CISPEP 2 THR B 701 PRO B 702 0 1.63
SITE 1 AC1 14 TRP A 409 ALA A 412 ARG A 414 CYS A 415
SITE 2 AC1 14 PHE A 584 SER A 585 TRP A 587 GLU A 592
SITE 3 AC1 14 TYR A 706 H4B A 802 KL4 A 803 ACT A 804
SITE 4 AC1 14 HOH A 914 HOH A 920
SITE 1 AC2 12 SER A 334 MET A 336 ARG A 596 VAL A 677
SITE 2 AC2 12 TRP A 678 HEM A 801 HOH A 920 HOH A 961
SITE 3 AC2 12 TRP B 676 PHE B 691 HIS B 692 GLU B 694
SITE 1 AC3 10 PRO A 565 VAL A 567 MET A 570 PHE A 584
SITE 2 AC3 10 GLY A 586 TRP A 587 GLU A 592 TYR A 706
SITE 3 AC3 10 HEM A 801 HOH A 920
SITE 1 AC4 2 TRP A 587 HEM A 801
SITE 1 AC5 15 TRP B 409 ALA B 412 ARG B 414 CYS B 415
SITE 2 AC5 15 PHE B 584 SER B 585 TRP B 587 GLU B 592
SITE 3 AC5 15 TRP B 678 PHE B 704 TYR B 706 H4B B 802
SITE 4 AC5 15 KL4 B 803 HOH B 906 HOH B 909
SITE 1 AC6 13 TRP A 676 PHE A 691 HIS A 692 GLN A 693
SITE 2 AC6 13 GLU A 694 SER B 334 MET B 336 ARG B 596
SITE 3 AC6 13 VAL B 677 TRP B 678 HEM B 801 HOH B 906
SITE 4 AC6 13 HOH B 987
SITE 1 AC7 8 VAL B 567 MET B 570 GLY B 586 TRP B 587
SITE 2 AC7 8 GLU B 592 TYR B 706 HEM B 801 HOH B 906
SITE 1 AC8 3 ILE B 419 TRP B 587 VAL B 649
SITE 1 AC9 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
CRYST1 52.212 111.859 165.019 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 0.019153 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008940 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
