HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18 6NG4
TITLE STRUCTURE OF HUMAN NEURONAL NITRIC OXIDE SYNTHASE R354A/G357D MUTANT
TITLE 2 HEME DOMAIN IN COMPLEX WITH (R)-6-(3-FLUORO-5-(2-(PYRROLIDIN-2-YL)
TITLE 3 ETHYL)PHENETHYL)-4-METHYLPYRIDIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 302-722;
COMPND 5 SYNONYM: CONSTITUTIVE NOS,NC-NOS,NOS TYPE I,NEURONAL NOS,NNOS,
COMPND 6 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1,BNOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 GENE: NOS1;
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 11-OCT-23 6NG4 1 LINK
REVDAT 3 04-DEC-19 6NG4 1 REMARK
REVDAT 2 27-MAR-19 6NG4 1 JRNL
REVDAT 1 13-MAR-19 6NG4 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. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.870
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 100431
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 9446
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 38.8628 - 5.5124 1.00 6223 280 0.1598 0.1849
REMARK 3 2 5.5124 - 4.3772 1.00 6189 311 0.1296 0.1560
REMARK 3 3 4.3772 - 3.8245 1.00 6195 326 0.1329 0.1654
REMARK 3 4 3.8245 - 3.4750 1.00 6140 348 0.1399 0.1778
REMARK 3 5 3.4750 - 3.2261 1.00 6241 312 0.1588 0.2265
REMARK 3 6 3.2261 - 3.0360 1.00 6204 309 0.1738 0.2151
REMARK 3 7 3.0360 - 2.8840 1.00 6163 310 0.1681 0.2257
REMARK 3 8 2.8840 - 2.7585 1.00 6184 293 0.1678 0.2008
REMARK 3 9 2.7585 - 2.6523 1.00 6257 308 0.1717 0.1966
REMARK 3 10 2.6523 - 2.5608 1.00 6189 333 0.1665 0.2374
REMARK 3 11 2.5608 - 2.4807 1.00 6136 327 0.1633 0.1897
REMARK 3 12 2.4807 - 2.4098 1.00 6193 350 0.1734 0.2297
REMARK 3 13 2.4098 - 2.3464 1.00 6121 352 0.1800 0.2240
REMARK 3 14 2.3464 - 2.2892 1.00 6174 308 0.1848 0.2436
REMARK 3 15 2.2892 - 2.2371 1.00 6254 308 0.1903 0.2331
REMARK 3 16 2.2371 - 2.1895 1.00 6167 303 0.1942 0.2346
REMARK 3 17 2.1895 - 2.1457 1.00 6192 291 0.2142 0.2558
REMARK 3 18 2.1457 - 2.1052 1.00 6108 333 0.2418 0.2824
REMARK 3 19 2.1052 - 2.0677 1.00 6224 336 0.2636 0.3096
REMARK 3 20 2.0677 - 2.0326 1.00 6182 309 0.2732 0.3127
REMARK 3 21 2.0326 - 1.9998 0.99 6127 308 0.2964 0.3161
REMARK 3 22 1.9998 - 1.9691 0.99 6123 369 0.3095 0.3266
REMARK 3 23 1.9691 - 1.9401 0.99 6102 348 0.3395 0.3743
REMARK 3 24 1.9401 - 1.9128 0.99 6199 261 0.3696 0.3829
REMARK 3 25 1.9128 - 1.8869 0.99 6199 302 0.3844 0.3728
REMARK 3 26 1.8869 - 1.8624 0.99 6082 357 0.4096 0.4039
REMARK 3 27 1.8624 - 1.8391 0.98 6125 327 0.4381 0.4744
REMARK 3 28 1.8391 - 1.8170 0.97 5952 320 0.4859 0.4896
REMARK 3 29 1.8170 - 1.7959 0.97 6060 286 0.4893 0.5383
REMARK 3 30 1.7959 - 1.7757 0.66 4074 221 0.5146 0.5226
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.210
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 7146
REMARK 3 ANGLE : 1.134 9724
REMARK 3 CHIRALITY : 0.042 1003
REMARK 3 PLANARITY : 0.005 1226
REMARK 3 DIHEDRAL : 15.391 2615
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 302:722)
REMARK 3 ORIGIN FOR THE GROUP (A): 117.7342 248.3164 358.7407
REMARK 3 T TENSOR
REMARK 3 T11: 0.2502 T22: 0.3287
REMARK 3 T33: 0.3247 T12: -0.0076
REMARK 3 T13: 0.0260 T23: 0.0310
REMARK 3 L TENSOR
REMARK 3 L11: 0.4325 L22: 0.6329
REMARK 3 L33: 2.2013 L12: -0.2075
REMARK 3 L13: -0.0750 L23: 0.2676
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: -0.0323 S13: 0.0382
REMARK 3 S21: -0.0427 S22: -0.0835 S23: 0.0041
REMARK 3 S31: 0.1144 S32: 0.1387 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 304:722)
REMARK 3 ORIGIN FOR THE GROUP (A): 116.0960 246.8301 321.5555
REMARK 3 T TENSOR
REMARK 3 T11: 0.3332 T22: 0.3682
REMARK 3 T33: 0.3501 T12: -0.0049
REMARK 3 T13: 0.0139 T23: -0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 0.1866 L22: 0.4100
REMARK 3 L33: 3.2970 L12: -0.2930
REMARK 3 L13: -0.2956 L23: 0.0924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0281 S12: 0.0760 S13: -0.0125
REMARK 3 S21: -0.0498 S22: -0.0795 S23: 0.0334
REMARK 3 S31: 0.0187 S32: -0.1505 S33: -0.0004
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 6NG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000236879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101601
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.776
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 4.25100
REMARK 200 R SYM FOR SHELL (I) : 4.25100
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: PDB ENTRY 1OM4
REMARK 200
REMARK 200 REMARK: PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG3350, 35 MM CITRIC ACID, 65 MM
REMARK 280 BIS-TRIS PROPANE, 10% GLYCEROL, 5 MM TCEP, PH 7.2, VAPOR
REMARK 280 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 26.19650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.00350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.81450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.00350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.19650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.81450
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: 9990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 SER A 344
REMARK 465 GLN A 345
REMARK 465 HIS A 346
REMARK 465 ALA A 347
REMARK 465 ARG A 348
REMARK 465 ARG A 349
REMARK 465 PRO A 350
REMARK 465 CYS B 302
REMARK 465 PRO B 303
REMARK 465 GLN B 345
REMARK 465 HIS B 346
REMARK 465 ALA B 347
REMARK 465 ARG B 348
REMARK 465 ARG B 349
REMARK 465 PRO B 350
REMARK 465 GLU B 351
REMARK 465 ASP B 352
REMARK 465 VAL B 353
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 1081 O HOH B 1132 2.13
REMARK 500 O HOH A 1218 O HOH A 1233 2.17
REMARK 500 O HOH A 1021 O HOH A 1178 2.18
REMARK 500 O HOH A 1006 O HOH A 1215 2.18
REMARK 500 O HOH B 982 O HOH B 1041 2.18
REMARK 500 O HOH A 1057 O HOH A 1148 2.19
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 THR A 326 -88.66 -117.80
REMARK 500 VAL A 353 117.15 39.26
REMARK 500 LYS A 428 73.65 -105.56
REMARK 500 THR A 471 -86.44 -111.75
REMARK 500 CYS A 587 56.95 -149.88
REMARK 500 ARG A 608 -134.86 -117.19
REMARK 500 CYS A 677 99.46 -160.83
REMARK 500 THR B 326 -74.89 -134.39
REMARK 500 THR B 471 -76.77 -114.51
REMARK 500 LYS B 555 -38.93 -133.22
REMARK 500 CYS B 587 59.95 -149.08
REMARK 500 ARG B 608 -131.71 -117.13
REMARK 500 CYS B 677 104.55 -160.41
REMARK 500 TRP B 721 174.28 -59.68
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 B1156 DISTANCE = 6.30 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 803 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 331 SG
REMARK 620 2 CYS A 336 SG 108.9
REMARK 620 3 CYS B 331 SG 125.1 103.7
REMARK 620 4 CYS B 336 SG 101.4 100.7 114.5
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 420 SG
REMARK 620 2 HEM A 801 NA 101.2
REMARK 620 3 HEM A 801 NB 100.9 88.4
REMARK 620 4 HEM A 801 NC 97.8 161.0 88.6
REMARK 620 5 HEM A 801 ND 100.6 87.8 158.5 88.1
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 420 SG
REMARK 620 2 HEM B 801 NA 99.6
REMARK 620 3 HEM B 801 NB 98.5 84.8
REMARK 620 4 HEM B 801 NC 97.9 162.4 90.9
REMARK 620 5 HEM B 801 ND 102.1 92.2 159.4 85.8
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 ZN A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KMA B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 804
DBREF 6NG4 A 302 722 UNP P29475 NOS1_HUMAN 302 722
DBREF 6NG4 B 302 722 UNP P29475 NOS1_HUMAN 302 722
SEQADV 6NG4 ALA A 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 6NG4 ASP A 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQADV 6NG4 ALA B 354 UNP P29475 ARG 354 ENGINEERED MUTATION
SEQADV 6NG4 ASP B 357 UNP P29475 GLY 357 ENGINEERED MUTATION
SEQRES 1 A 421 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU
SEQRES 2 A 421 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 421 GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE
SEQRES 4 A 421 MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL
SEQRES 5 A 421 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 421 ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 421 LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 421 ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 421 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 421 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 421 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 421 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 421 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 421 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 421 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 421 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 421 CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE
SEQRES 18 A 421 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 421 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 421 VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP
SEQRES 21 A 421 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 421 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 421 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 421 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 421 GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR
SEQRES 26 A 421 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 421 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 421 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 421 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 421 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 421 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 421 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 421 THR HIS VAL TRP LYS
SEQRES 1 B 421 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR GLU
SEQRES 2 B 421 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 421 GLU THR GLY CYS THR GLU TYR ILE CYS MET GLY SER ILE
SEQRES 4 B 421 MET HIS PRO SER GLN HIS ALA ARG ARG PRO GLU ASP VAL
SEQRES 5 B 421 ALA THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 421 ILE ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 421 LYS ALA HIS MET GLU ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 421 ILE ASP THR THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 421 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 421 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 421 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 421 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 421 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 421 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 421 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 421 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 421 CYS ILE GLN GLN GLY TRP LYS PRO PRO ARG GLY ARG PHE
SEQRES 18 B 421 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 421 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 421 VAL PRO ILE ARG HIS PRO LYS PHE GLU TRP PHE LYS ASP
SEQRES 21 B 421 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 421 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 421 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 421 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 421 GLU VAL ALA LYS LYS MET ASN LEU ASP MET ARG LYS THR
SEQRES 26 B 421 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 421 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 421 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 421 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 421 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 421 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 421 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 421 THR HIS VAL TRP LYS
HET HEM A 801 43
HET H4B A 802 17
HET ZN A 803 1
HET KMA A 804 24
HET GOL A 805 6
HET GOL A 806 6
HET HEM B 801 43
HET H4B B 802 17
HET KMA B 803 24
HET GOL B 804 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM ZN ZINC ION
HETNAM KMA 6-[2-(3-FLUORO-5-{2-[(2R)-PYRROLIDIN-2-
HETNAM 2 KMA YL]ETHYL}PHENYL)ETHYL]-4-METHYLPYRIDIN-2-AMINE
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 ZN ZN 2+
FORMUL 6 KMA 2(C20 H26 F N3)
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 13 HOH *612(H2 O)
HELIX 1 AA1 THR A 320 SER A 325 5 6
HELIX 2 AA2 THR A 355 ILE A 374 1 20
HELIX 3 AA3 SER A 379 SER A 397 1 19
HELIX 4 AA4 LYS A 402 ASN A 416 1 15
HELIX 5 AA5 GLY A 422 TRP A 426 5 5
HELIX 6 AA6 THR A 439 ASN A 456 1 18
HELIX 7 AA7 LYS A 457 ASN A 459 5 3
HELIX 8 AA8 ASN A 503 GLN A 513 1 11
HELIX 9 AA9 PRO A 542 VAL A 546 5 5
HELIX 10 AB1 PHE A 556 GLY A 563 5 8
HELIX 11 AB2 GLY A 595 VAL A 600 1 6
HELIX 12 AB3 VAL A 600 ASP A 605 1 6
HELIX 13 AB4 ILE A 611 MET A 619 1 9
HELIX 14 AB5 LYS A 625 SER A 628 5 4
HELIX 15 AB6 LEU A 629 ASP A 649 1 21
HELIX 16 AB7 ASP A 655 GLY A 675 1 21
HELIX 17 AB8 ASP A 680 VAL A 685 1 6
HELIX 18 AB9 SER A 689 THR A 693 5 5
HELIX 19 AC1 ASP A 714 HIS A 719 1 6
HELIX 20 AC2 THR B 320 SER B 325 5 6
HELIX 21 AC3 THR B 355 ILE B 374 1 20
HELIX 22 AC4 SER B 379 SER B 397 1 19
HELIX 23 AC5 LYS B 402 ASN B 416 1 15
HELIX 24 AC6 GLY B 422 TRP B 426 5 5
HELIX 25 AC7 THR B 439 ASN B 456 1 18
HELIX 26 AC8 LYS B 457 ASN B 459 5 3
HELIX 27 AC9 ASN B 503 GLN B 513 1 11
HELIX 28 AD1 PRO B 542 VAL B 546 5 5
HELIX 29 AD2 PHE B 556 GLY B 563 5 8
HELIX 30 AD3 GLY B 595 VAL B 600 1 6
HELIX 31 AD4 VAL B 600 ASP B 605 1 6
HELIX 32 AD5 ILE B 611 MET B 619 1 9
HELIX 33 AD6 LYS B 625 SER B 628 5 4
HELIX 34 AD7 LEU B 629 ASP B 649 1 21
HELIX 35 AD8 ASP B 655 GLY B 675 1 21
HELIX 36 AD9 ASP B 680 VAL B 685 1 6
HELIX 37 AE1 SER B 689 GLN B 698 5 10
HELIX 38 AE2 ASP B 714 HIS B 719 1 6
SHEET 1 AA1 2 LEU A 306 LYS A 309 0
SHEET 2 AA1 2 VAL A 316 ASP A 319 -1 O ASP A 319 N LEU A 306
SHEET 1 AA2 4 GLN A 430 ASP A 433 0
SHEET 2 AA2 4 ALA A 463 ILE A 466 1 O ILE A 464 N PHE A 432
SHEET 3 AA2 4 PHE A 589 SER A 590 -1 O SER A 590 N ALA A 463
SHEET 4 AA2 4 ALA A 571 VAL A 572 -1 N VAL A 572 O PHE A 589
SHEET 1 AA3 3 ARG A 478 VAL A 479 0
SHEET 2 AA3 3 LEU A 527 GLN A 530 -1 O GLN A 530 N ARG A 478
SHEET 3 AA3 3 GLU A 537 PHE A 539 -1 O PHE A 539 N LEU A 527
SHEET 1 AA4 2 GLY A 489 LYS A 491 0
SHEET 2 AA4 2 THR A 497 GLY A 499 -1 O LEU A 498 N TYR A 490
SHEET 1 AA5 2 GLU A 548 PRO A 550 0
SHEET 2 AA5 2 LYS A 565 TYR A 567 -1 O TRP A 566 N VAL A 549
SHEET 1 AA6 3 LEU A 582 PHE A 584 0
SHEET 2 AA6 3 LEU A 576 ILE A 579 -1 N LEU A 577 O PHE A 584
SHEET 3 AA6 3 SER A 708 GLU A 710 -1 O GLU A 710 N LEU A 576
SHEET 1 AA7 2 TYR A 593 MET A 594 0
SHEET 2 AA7 2 ILE A 653 VAL A 654 1 O VAL A 654 N TYR A 593
SHEET 1 AA8 2 LEU B 306 LYS B 309 0
SHEET 2 AA8 2 VAL B 316 ASP B 319 -1 O ASP B 319 N LEU B 306
SHEET 1 AA9 4 GLN B 430 ASP B 433 0
SHEET 2 AA9 4 ALA B 463 ILE B 466 1 O ILE B 464 N PHE B 432
SHEET 3 AA9 4 PHE B 589 SER B 590 -1 O SER B 590 N ALA B 463
SHEET 4 AA9 4 ALA B 571 VAL B 572 -1 N VAL B 572 O PHE B 589
SHEET 1 AB1 3 ARG B 478 VAL B 479 0
SHEET 2 AB1 3 LEU B 527 GLN B 530 -1 O GLN B 530 N ARG B 478
SHEET 3 AB1 3 GLU B 537 PHE B 539 -1 O PHE B 539 N LEU B 527
SHEET 1 AB2 2 GLY B 489 LYS B 491 0
SHEET 2 AB2 2 THR B 497 GLY B 499 -1 O LEU B 498 N TYR B 490
SHEET 1 AB3 2 GLU B 548 PRO B 550 0
SHEET 2 AB3 2 LYS B 565 TYR B 567 -1 O TRP B 566 N VAL B 549
SHEET 1 AB4 3 LEU B 582 PHE B 584 0
SHEET 2 AB4 3 LEU B 576 ILE B 579 -1 N LEU B 577 O PHE B 584
SHEET 3 AB4 3 SER B 708 GLU B 710 -1 O SER B 708 N GLU B 578
SHEET 1 AB5 2 TYR B 593 MET B 594 0
SHEET 2 AB5 2 ILE B 653 VAL B 654 1 O VAL B 654 N TYR B 593
LINK SG CYS A 331 ZN ZN A 803 1555 1555 2.36
LINK SG CYS A 336 ZN ZN A 803 1555 1555 2.37
LINK SG CYS A 420 FE HEM A 801 1555 1555 2.38
LINK ZN ZN A 803 SG CYS B 331 1555 1555 2.34
LINK ZN ZN A 803 SG CYS B 336 1555 1555 2.34
LINK SG CYS B 420 FE HEM B 801 1555 1555 2.35
CISPEP 1 THR A 706 PRO A 707 0 0.68
CISPEP 2 THR B 706 PRO B 707 0 2.07
SITE 1 AC1 15 TRP A 414 CYS A 420 PHE A 589 SER A 590
SITE 2 AC1 15 TRP A 592 GLU A 597 TRP A 683 PHE A 709
SITE 3 AC1 15 TYR A 711 H4B A 802 KMA A 804 HOH A 929
SITE 4 AC1 15 HOH A 972 HOH A 975 HOH A1000
SITE 1 AC2 15 SER A 339 ARG A 601 VAL A 682 TRP A 683
SITE 2 AC2 15 HEM A 801 HOH A 929 HOH A 936 HOH A1003
SITE 3 AC2 15 HOH A1012 HOH A1073 TRP B 681 PHE B 696
SITE 4 AC2 15 HIS B 697 GLN B 698 GLU B 699
SITE 1 AC3 4 CYS A 331 CYS A 336 CYS B 331 CYS B 336
SITE 1 AC4 9 GLN A 483 ARG A 486 TYR A 567 GLY A 591
SITE 2 AC4 9 TRP A 592 TYR A 593 GLU A 597 HEM A 801
SITE 3 AC4 9 HOH A 929
SITE 1 AC5 4 LYS A 324 GLN A 369 ARG A 674 HOH A1076
SITE 1 AC6 1 ARG A 415
SITE 1 AC7 18 TRP B 414 ARG B 419 CYS B 420 SER B 462
SITE 2 AC7 18 PHE B 589 SER B 590 GLY B 591 TRP B 592
SITE 3 AC7 18 GLU B 597 TRP B 683 PHE B 709 TYR B 711
SITE 4 AC7 18 H4B B 802 KMA B 803 HOH B 902 HOH B 903
SITE 5 AC7 18 HOH B1070 HOH B1090
SITE 1 AC8 16 TRP A 681 PHE A 696 HIS A 697 GLN A 698
SITE 2 AC8 16 GLU A 699 SER B 339 ARG B 601 VAL B 682
SITE 3 AC8 16 TRP B 683 HEM B 801 KMA B 803 HOH B 902
SITE 4 AC8 16 HOH B 961 HOH B 965 HOH B 995 HOH B1027
SITE 1 AC9 12 GLN B 483 ARG B 486 TYR B 567 VAL B 572
SITE 2 AC9 12 PHE B 589 GLY B 591 TRP B 592 GLU B 597
SITE 3 AC9 12 TRP B 683 HEM B 801 H4B B 802 HOH B 902
SITE 1 AD1 2 GLN B 369 ARG B 674
CRYST1 52.393 121.629 164.007 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 0.019087 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008222 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006097 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
