HEADER OXIDOREDUCTASE 01-SEP-17 6AV6
TITLE STRUCTURE OF HUMAN ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN
TITLE 2 COMPLEX WITH 6-(3-FLUORO-5-(3-(METHYLAMINO)PROPYL)PHENETHYL)-4-
TITLE 3 METHYLPYRIDIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 41-480;
COMPND 5 SYNONYM: CONSTITUTIVE NOS,CNOS,EC-NOS,ENDOTHELIAL NOS,ENOS,NOS TYPE
COMPND 6 III,NOSIII;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: RESIDUES 108 TO 119 ARE DISORDERED. THE N-TERMINAL
COMPND 10 RESIDUES 41 TO 67 ARE INVISIBLE IN DENSITY.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL: ENDOTHELIAL;
SOURCE 6 GENE: NOS3;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 4 04-OCT-23 6AV6 1 LINK
REVDAT 3 25-DEC-19 6AV6 1 REMARK
REVDAT 2 20-FEB-19 6AV6 1 REMARK
REVDAT 1 11-JUL-18 6AV6 0
JRNL AUTH H.T.DO,H.Y.WANG,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN
JRNL TITL IMPROVEMENT OF CELL PERMEABILITY OF HUMAN NEURONAL NITRIC
JRNL TITL 2 OXIDE SYNTHASE INHIBITORS USING POTENT AND SELECTIVE
JRNL TITL 3 2-AMINOPYRIDINE-BASED SCAFFOLDS WITH A FLUOROBENZENE LINKER.
JRNL REF J. MED. CHEM. V. 60 9360 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 29091437
JRNL DOI 10.1021/ACS.JMEDCHEM.7B01356
REMARK 2
REMARK 2 RESOLUTION. 2.08 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 115661
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 5817
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 39.1377 - 6.4537 0.99 7288 350 0.1797 0.1716
REMARK 3 2 6.4537 - 5.1262 1.00 7333 372 0.1585 0.2023
REMARK 3 3 5.1262 - 4.4792 0.99 7258 378 0.1352 0.1800
REMARK 3 4 4.4792 - 4.0702 1.00 7322 368 0.1430 0.1797
REMARK 3 5 4.0702 - 3.7787 1.00 7269 386 0.1540 0.1871
REMARK 3 6 3.7787 - 3.5561 1.00 7306 396 0.1765 0.2276
REMARK 3 7 3.5561 - 3.3781 1.00 7271 399 0.1920 0.2422
REMARK 3 8 3.3781 - 3.2311 0.99 7207 396 0.2086 0.2761
REMARK 3 9 3.2311 - 3.1068 0.99 7267 358 0.2180 0.2763
REMARK 3 10 3.1068 - 2.9996 1.00 7292 336 0.2158 0.3063
REMARK 3 11 2.9996 - 2.9058 0.99 7335 352 0.2234 0.2696
REMARK 3 12 2.9058 - 2.8228 1.00 7249 420 0.2259 0.2661
REMARK 3 13 2.8228 - 2.7485 0.99 7247 353 0.2240 0.2978
REMARK 3 14 2.7485 - 2.6815 0.99 7245 384 0.2179 0.2627
REMARK 3 15 2.6815 - 2.6205 0.99 7216 444 0.2225 0.2772
REMARK 3 16 2.6205 - 2.5648 0.99 7208 411 0.2244 0.2883
REMARK 3 17 2.5648 - 2.5135 1.00 7325 354 0.2285 0.2705
REMARK 3 18 2.5135 - 2.4661 0.98 7114 395 0.2539 0.3036
REMARK 3 19 2.4661 - 2.4220 0.99 7196 409 0.2666 0.3409
REMARK 3 20 2.4220 - 2.3810 0.99 7193 402 0.2536 0.3232
REMARK 3 21 2.3810 - 2.3426 0.99 7351 335 0.2405 0.2734
REMARK 3 22 2.3426 - 2.3065 0.99 7115 425 0.2473 0.3010
REMARK 3 23 2.3065 - 2.2726 0.99 7334 384 0.2485 0.2923
REMARK 3 24 2.2726 - 2.2406 0.99 7248 331 0.2632 0.2849
REMARK 3 25 2.2406 - 2.2103 0.99 7129 429 0.2559 0.3126
REMARK 3 26 2.2103 - 2.1816 0.99 7341 349 0.2596 0.3325
REMARK 3 27 2.1816 - 2.1544 0.99 7253 389 0.2635 0.3211
REMARK 3 28 2.1544 - 2.1284 0.99 7140 379 0.2852 0.3442
REMARK 3 29 2.1284 - 2.1037 0.99 7247 413 0.2738 0.3055
REMARK 3 30 2.1037 - 2.0800 0.99 7218 420 0.2885 0.3306
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.880
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 : 0.008 13762
REMARK 3 ANGLE : 1.104 18767
REMARK 3 CHIRALITY : 0.043 1945
REMARK 3 PLANARITY : 0.005 2417
REMARK 3 DIHEDRAL : 16.236 5004
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 68:480)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.3465 31.9883-185.4252
REMARK 3 T TENSOR
REMARK 3 T11: 0.6441 T22: 0.6225
REMARK 3 T33: 0.4923 T12: 0.2527
REMARK 3 T13: 0.2095 T23: 0.3089
REMARK 3 L TENSOR
REMARK 3 L11: 0.9132 L22: 1.6667
REMARK 3 L33: 1.7066 L12: 0.2658
REMARK 3 L13: -0.5248 L23: -0.3953
REMARK 3 S TENSOR
REMARK 3 S11: 0.2956 S12: 0.5136 S13: 0.3446
REMARK 3 S21: 0.1797 S22: 0.2336 S23: 0.3010
REMARK 3 S31: -0.6808 S32: -0.6493 S33: -0.0934
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 68:480)
REMARK 3 ORIGIN FOR THE GROUP (A): 74.4181 8.5564-157.7531
REMARK 3 T TENSOR
REMARK 3 T11: 0.3316 T22: 0.2157
REMARK 3 T33: 0.2364 T12: -0.0575
REMARK 3 T13: -0.0156 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 1.0795 L22: 1.4527
REMARK 3 L33: 2.3383 L12: -0.2699
REMARK 3 L13: -0.4239 L23: -0.8201
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: -0.0321 S13: 0.0395
REMARK 3 S21: 0.3684 S22: 0.0912 S23: 0.0478
REMARK 3 S31: -0.1802 S32: -0.1041 S33: -0.1047
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESID 68:480)
REMARK 3 ORIGIN FOR THE GROUP (A): 93.1498 -34.0901-195.4905
REMARK 3 T TENSOR
REMARK 3 T11: 0.6854 T22: 0.4018
REMARK 3 T33: 0.4054 T12: -0.0340
REMARK 3 T13: -0.1136 T23: 0.1112
REMARK 3 L TENSOR
REMARK 3 L11: 0.6752 L22: 1.6646
REMARK 3 L33: 1.5860 L12: -0.1270
REMARK 3 L13: 0.2704 L23: 0.0433
REMARK 3 S TENSOR
REMARK 3 S11: 0.1623 S12: -0.2632 S13: -0.2588
REMARK 3 S21: 0.1193 S22: 0.0324 S23: 0.1431
REMARK 3 S31: 0.6513 S32: -0.2514 S33: -0.0923
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN D AND RESID 67:480)
REMARK 3 ORIGIN FOR THE GROUP (A): 103.4708 -10.4329-222.9055
REMARK 3 T TENSOR
REMARK 3 T11: 0.3282 T22: 0.1948
REMARK 3 T33: 0.2434 T12: 0.0558
REMARK 3 T13: -0.0349 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.0694 L22: 0.7926
REMARK 3 L33: 2.2890 L12: 0.3006
REMARK 3 L13: 0.3392 L23: -0.0289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0366 S12: 0.0422 S13: -0.0266
REMARK 3 S21: -0.1568 S22: 0.0725 S23: -0.0221
REMARK 3 S31: -0.0598 S32: 0.1124 S33: -0.0274
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 6AV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000223187.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
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 : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS OCT 15, 2015
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116007
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.16900
REMARK 200 R SYM (I) : 0.16900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 2.91600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.8.0049
REMARK 200 STARTING MODEL: 4DIP
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12-15% PEG3350, 0.1M BIS-TRIS 0.2-0.3M
REMARK 280 MG ACETATE, 0.1M GDCL3 10% GLYCEROL, 5 MM TCEP, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 76.39000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 10970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -152.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 10920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ALA A 41
REMARK 465 PRO A 42
REMARK 465 ALA A 43
REMARK 465 SER A 44
REMARK 465 LEU A 45
REMARK 465 LEU A 46
REMARK 465 PRO A 47
REMARK 465 PRO A 48
REMARK 465 ALA A 49
REMARK 465 PRO A 50
REMARK 465 GLU A 51
REMARK 465 HIS A 52
REMARK 465 SER A 53
REMARK 465 PRO A 54
REMARK 465 PRO A 55
REMARK 465 SER A 56
REMARK 465 SER A 57
REMARK 465 PRO A 58
REMARK 465 LEU A 59
REMARK 465 THR A 60
REMARK 465 GLN A 61
REMARK 465 PRO A 62
REMARK 465 PRO A 63
REMARK 465 GLU A 64
REMARK 465 GLY A 65
REMARK 465 PRO A 66
REMARK 465 LYS A 67
REMARK 465 LYS A 108
REMARK 465 LEU A 109
REMARK 465 GLN A 110
REMARK 465 GLY A 111
REMARK 465 ARG A 112
REMARK 465 PRO A 113
REMARK 465 SER A 114
REMARK 465 PRO A 115
REMARK 465 GLY A 116
REMARK 465 PRO A 117
REMARK 465 PRO A 118
REMARK 465 ALA A 119
REMARK 465 ALA B 41
REMARK 465 PRO B 42
REMARK 465 ALA B 43
REMARK 465 SER B 44
REMARK 465 LEU B 45
REMARK 465 LEU B 46
REMARK 465 PRO B 47
REMARK 465 PRO B 48
REMARK 465 ALA B 49
REMARK 465 PRO B 50
REMARK 465 GLU B 51
REMARK 465 HIS B 52
REMARK 465 SER B 53
REMARK 465 PRO B 54
REMARK 465 PRO B 55
REMARK 465 SER B 56
REMARK 465 SER B 57
REMARK 465 PRO B 58
REMARK 465 LEU B 59
REMARK 465 THR B 60
REMARK 465 GLN B 61
REMARK 465 PRO B 62
REMARK 465 PRO B 63
REMARK 465 GLU B 64
REMARK 465 GLY B 65
REMARK 465 PRO B 66
REMARK 465 LYS B 67
REMARK 465 ARG B 107
REMARK 465 LYS B 108
REMARK 465 LEU B 109
REMARK 465 GLN B 110
REMARK 465 GLY B 111
REMARK 465 ARG B 112
REMARK 465 PRO B 113
REMARK 465 SER B 114
REMARK 465 PRO B 115
REMARK 465 GLY B 116
REMARK 465 PRO B 117
REMARK 465 PRO B 118
REMARK 465 ALA C 41
REMARK 465 PRO C 42
REMARK 465 ALA C 43
REMARK 465 SER C 44
REMARK 465 LEU C 45
REMARK 465 LEU C 46
REMARK 465 PRO C 47
REMARK 465 PRO C 48
REMARK 465 ALA C 49
REMARK 465 PRO C 50
REMARK 465 GLU C 51
REMARK 465 HIS C 52
REMARK 465 SER C 53
REMARK 465 PRO C 54
REMARK 465 PRO C 55
REMARK 465 SER C 56
REMARK 465 SER C 57
REMARK 465 PRO C 58
REMARK 465 LEU C 59
REMARK 465 THR C 60
REMARK 465 GLN C 61
REMARK 465 PRO C 62
REMARK 465 PRO C 63
REMARK 465 GLU C 64
REMARK 465 GLY C 65
REMARK 465 PRO C 66
REMARK 465 LYS C 67
REMARK 465 ARG C 107
REMARK 465 LYS C 108
REMARK 465 LEU C 109
REMARK 465 GLN C 110
REMARK 465 GLY C 111
REMARK 465 ARG C 112
REMARK 465 PRO C 113
REMARK 465 SER C 114
REMARK 465 PRO C 115
REMARK 465 GLY C 116
REMARK 465 PRO C 117
REMARK 465 PRO C 118
REMARK 465 ALA D 41
REMARK 465 PRO D 42
REMARK 465 ALA D 43
REMARK 465 SER D 44
REMARK 465 LEU D 45
REMARK 465 LEU D 46
REMARK 465 PRO D 47
REMARK 465 PRO D 48
REMARK 465 ALA D 49
REMARK 465 PRO D 50
REMARK 465 GLU D 51
REMARK 465 HIS D 52
REMARK 465 SER D 53
REMARK 465 PRO D 54
REMARK 465 PRO D 55
REMARK 465 SER D 56
REMARK 465 SER D 57
REMARK 465 PRO D 58
REMARK 465 LEU D 59
REMARK 465 THR D 60
REMARK 465 GLN D 61
REMARK 465 PRO D 62
REMARK 465 PRO D 63
REMARK 465 GLU D 64
REMARK 465 GLY D 65
REMARK 465 PRO D 66
REMARK 465 ARG D 107
REMARK 465 LYS D 108
REMARK 465 LEU D 109
REMARK 465 GLN D 110
REMARK 465 GLY D 111
REMARK 465 ARG D 112
REMARK 465 PRO D 113
REMARK 465 SER D 114
REMARK 465 PRO D 115
REMARK 465 GLY D 116
REMARK 465 PRO D 117
REMARK 465 PRO D 118
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 O4 BTB A 503 O HOH A 601 2.10
REMARK 500 O PRO A 93 NH2 ARG A 98 2.11
REMARK 500 NH2 ARG D 365 OD2 ASP D 369 2.11
REMARK 500 O HOH D 692 O HOH D 693 2.11
REMARK 500 OH TYR D 475 O1D HEM D 501 2.11
REMARK 500 OH TYR A 475 O1D HEM A 501 2.13
REMARK 500 OE2 GLU C 347 O HOH C 601 2.15
REMARK 500 O HOH D 639 O HOH D 693 2.18
REMARK 500 OE2 GLU D 298 O3 BTB D 505 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 GLN A 89 -72.79 -98.99
REMARK 500 GLN A 90 95.48 -42.05
REMARK 500 ASP A 200 37.22 -88.74
REMARK 500 ARG A 202 -2.21 -147.06
REMARK 500 ARG A 238 137.27 65.17
REMARK 500 ASP A 258 -121.03 -90.10
REMARK 500 ASN A 267 60.03 -117.14
REMARK 500 ASN A 283 -77.41 -86.31
REMARK 500 PRO A 296 134.52 -37.96
REMARK 500 ASP A 297 -79.28 64.29
REMARK 500 PRO A 299 170.26 -58.36
REMARK 500 ALA A 351 67.10 -152.24
REMARK 500 ARG A 372 -131.69 -114.27
REMARK 500 PRO A 479 49.40 -67.37
REMARK 500 GLN B 256 -161.30 -109.12
REMARK 500 ASN B 283 11.02 -140.24
REMARK 500 ALA B 351 79.20 -156.03
REMARK 500 ARG B 372 -132.39 -112.06
REMARK 500 GLN C 89 -94.93 -66.84
REMARK 500 GLN C 144 5.17 -57.06
REMARK 500 SER C 260 -177.07 -67.26
REMARK 500 HIS C 277 40.30 -73.49
REMARK 500 ASN C 283 -11.77 -142.74
REMARK 500 ASP C 297 -38.24 70.79
REMARK 500 ALA C 351 65.90 -155.40
REMARK 500 ARG C 372 -137.52 -113.98
REMARK 500 ARG D 202 11.63 -141.80
REMARK 500 ASN D 283 26.38 -142.61
REMARK 500 ALA D 351 68.41 -158.90
REMARK 500 ARG D 372 -133.23 -120.23
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 A 647 DISTANCE = 5.83 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 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 94 SG
REMARK 620 2 CYS A 99 SG 103.8
REMARK 620 3 CYS B 94 SG 125.6 106.5
REMARK 620 4 CYS B 99 SG 108.7 104.9 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 184 SG
REMARK 620 2 HEM A 501 NA 98.7
REMARK 620 3 HEM A 501 NB 96.3 89.3
REMARK 620 4 HEM A 501 NC 86.9 174.3 89.9
REMARK 620 5 HEM A 501 ND 93.3 90.8 170.3 89.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD A 508 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BTB A 503 O3
REMARK 620 2 BTB A 503 O4 50.6
REMARK 620 3 BTB A 503 N 74.4 64.8
REMARK 620 4 BTB A 503 O6 113.5 127.0 62.2
REMARK 620 5 BTB A 503 O8 117.0 74.2 54.1 74.4
REMARK 620 6 HOH A 601 O 60.0 43.4 108.1 170.3 101.5
REMARK 620 7 HOH A 644 O 157.9 141.2 125.9 75.1 84.6 113.7
REMARK 620 8 HOH D 690 O 80.5 128.5 122.1 82.8 155.4 102.4 80.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 502 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 184 SG
REMARK 620 2 HEM B 502 NA 100.2
REMARK 620 3 HEM B 502 NB 98.0 89.8
REMARK 620 4 HEM B 502 NC 96.4 163.4 87.4
REMARK 620 5 HEM B 502 ND 101.6 88.3 160.3 88.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD B 508 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 319 O
REMARK 620 2 GLU B 321 OE1 84.5
REMARK 620 3 BTB B 505 O3 89.7 73.1
REMARK 620 4 BTB B 505 O4 84.1 127.1 55.3
REMARK 620 5 BTB B 505 N 147.5 102.7 63.2 66.1
REMARK 620 6 BTB B 505 O6 140.5 58.3 91.5 127.6 62.6
REMARK 620 7 BTB B 505 O8 139.0 115.2 129.5 106.9 66.5 61.2
REMARK 620 8 HOH B 674 O 72.8 130.7 146.7 94.0 120.1 120.2 67.2
REMARK 620 9 HOH C 603 O 79.4 71.9 144.1 153.5 133.1 76.8 74.1 61.4
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD C 508 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 BTB B 509 O3
REMARK 620 2 BTB B 509 O4 66.5
REMARK 620 3 BTB B 509 N 64.5 57.0
REMARK 620 4 BTB B 509 O6 55.7 109.9 64.2
REMARK 620 5 BTB B 509 O8 108.0 47.4 58.1 120.0
REMARK 620 6 HOH B 678 O 80.7 138.9 129.4 66.0 171.1
REMARK 620 7 HOH B 707 O 149.2 118.0 145.4 132.1 92.5 78.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 94 SG
REMARK 620 2 CYS C 99 SG 105.6
REMARK 620 3 CYS D 94 SG 123.1 106.8
REMARK 620 4 CYS D 99 SG 104.4 105.2 110.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 184 SG
REMARK 620 2 HEM C 501 NA 100.7
REMARK 620 3 HEM C 501 NB 102.1 86.2
REMARK 620 4 HEM C 501 NC 94.0 165.3 91.0
REMARK 620 5 HEM C 501 ND 94.3 92.1 163.5 86.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 184 SG
REMARK 620 2 HEM D 501 NA 100.7
REMARK 620 3 HEM D 501 NB 99.2 92.3
REMARK 620 4 HEM D 501 NC 96.9 162.4 85.4
REMARK 620 5 HEM D 501 ND 100.2 86.6 160.4 89.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD D 506 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 319 O
REMARK 620 2 GLU D 321 OE1 77.7
REMARK 620 3 GLU D 321 OE2 87.4 50.4
REMARK 620 4 BTB D 504 O3 84.5 97.1 48.5
REMARK 620 5 BTB D 504 O4 86.5 152.1 106.7 58.3
REMARK 620 6 BTB D 504 N 135.8 115.9 74.7 53.3 61.9
REMARK 620 7 BTB D 504 O6 129.9 66.2 43.0 67.7 109.9 50.6
REMARK 620 8 BTB D 504 O8 145.2 106.3 122.4 127.9 99.9 74.7 80.2
REMARK 620 N 1 2 3 4 5 6 7
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue W68 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GD A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue W68 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GD B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue W68 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GD C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue W68 D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GD D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6AUR RELATED DB: PDB
REMARK 900 RELATED ID: 6AUT RELATED DB: PDB
REMARK 900 RELATED ID: 6AUQ RELATED DB: PDB
REMARK 900 RELATED ID: 6AUS RELATED DB: PDB
REMARK 900 RELATED ID: 6AUZ RELATED DB: PDB
REMARK 900 RELATED ID: 6AV1 RELATED DB: PDB
REMARK 900 RELATED ID: 6AUY RELATED DB: PDB
REMARK 900 RELATED ID: 6AV0 RELATED DB: PDB
REMARK 900 RELATED ID: 6AV2 RELATED DB: PDB
REMARK 900 RELATED ID: 6AV7 RELATED DB: PDB
REMARK 900 RELATED ID: 6AUU RELATED DB: PDB
REMARK 900 RELATED ID: 6AUV RELATED DB: PDB
REMARK 900 RELATED ID: 6AUW RELATED DB: PDB
REMARK 900 RELATED ID: 6AUX RELATED DB: PDB
REMARK 900 RELATED ID: 6AV3 RELATED DB: PDB
REMARK 900 RELATED ID: 6AV4 RELATED DB: PDB
REMARK 900 RELATED ID: 6AV5 RELATED DB: PDB
DBREF 6AV6 A 41 480 UNP P29474 NOS3_HUMAN 41 480
DBREF 6AV6 B 41 480 UNP P29474 NOS3_HUMAN 41 480
DBREF 6AV6 C 41 480 UNP P29474 NOS3_HUMAN 41 480
DBREF 6AV6 D 41 480 UNP P29474 NOS3_HUMAN 41 480
SEQRES 1 A 440 ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER
SEQRES 2 A 440 PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO
SEQRES 3 A 440 LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE
SEQRES 4 A 440 THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY
SEQRES 5 A 440 PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE
SEQRES 6 A 440 PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO
SEQRES 7 A 440 ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE
SEQRES 8 A 440 ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN
SEQRES 9 A 440 ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL
SEQRES 10 A 440 ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU
SEQRES 11 A 440 VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG
SEQRES 12 A 440 CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE
SEQRES 13 A 440 ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR
SEQRES 14 A 440 TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY
SEQRES 15 A 440 ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS
SEQRES 16 A 440 PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU
SEQRES 17 A 440 VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL
SEQRES 18 A 440 ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS
SEQRES 19 A 440 ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP
SEQRES 20 A 440 VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO
SEQRES 21 A 440 GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL
SEQRES 22 A 440 PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU
SEQRES 23 A 440 GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET
SEQRES 24 A 440 LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO
SEQRES 25 A 440 PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG
SEQRES 26 A 440 ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP
SEQRES 27 A 440 VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER
SEQRES 28 A 440 SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL
SEQRES 29 A 440 ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE
SEQRES 30 A 440 VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS
SEQRES 31 A 440 LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA
SEQRES 32 A 440 ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU
SEQRES 33 A 440 THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU
SEQRES 34 A 440 SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP
SEQRES 1 B 440 ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER
SEQRES 2 B 440 PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO
SEQRES 3 B 440 LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE
SEQRES 4 B 440 THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY
SEQRES 5 B 440 PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE
SEQRES 6 B 440 PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO
SEQRES 7 B 440 ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE
SEQRES 8 B 440 ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN
SEQRES 9 B 440 ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL
SEQRES 10 B 440 ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU
SEQRES 11 B 440 VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG
SEQRES 12 B 440 CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE
SEQRES 13 B 440 ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR
SEQRES 14 B 440 TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY
SEQRES 15 B 440 ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS
SEQRES 16 B 440 PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU
SEQRES 17 B 440 VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL
SEQRES 18 B 440 ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS
SEQRES 19 B 440 ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP
SEQRES 20 B 440 VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO
SEQRES 21 B 440 GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL
SEQRES 22 B 440 PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU
SEQRES 23 B 440 GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET
SEQRES 24 B 440 LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO
SEQRES 25 B 440 PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG
SEQRES 26 B 440 ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP
SEQRES 27 B 440 VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER
SEQRES 28 B 440 SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL
SEQRES 29 B 440 ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE
SEQRES 30 B 440 VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS
SEQRES 31 B 440 LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA
SEQRES 32 B 440 ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU
SEQRES 33 B 440 THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU
SEQRES 34 B 440 SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP
SEQRES 1 C 440 ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER
SEQRES 2 C 440 PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO
SEQRES 3 C 440 LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE
SEQRES 4 C 440 THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY
SEQRES 5 C 440 PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE
SEQRES 6 C 440 PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO
SEQRES 7 C 440 ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE
SEQRES 8 C 440 ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN
SEQRES 9 C 440 ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL
SEQRES 10 C 440 ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU
SEQRES 11 C 440 VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG
SEQRES 12 C 440 CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE
SEQRES 13 C 440 ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR
SEQRES 14 C 440 TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY
SEQRES 15 C 440 ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS
SEQRES 16 C 440 PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU
SEQRES 17 C 440 VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL
SEQRES 18 C 440 ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS
SEQRES 19 C 440 ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP
SEQRES 20 C 440 VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO
SEQRES 21 C 440 GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL
SEQRES 22 C 440 PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU
SEQRES 23 C 440 GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET
SEQRES 24 C 440 LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO
SEQRES 25 C 440 PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG
SEQRES 26 C 440 ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP
SEQRES 27 C 440 VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER
SEQRES 28 C 440 SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL
SEQRES 29 C 440 ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE
SEQRES 30 C 440 VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS
SEQRES 31 C 440 LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA
SEQRES 32 C 440 ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU
SEQRES 33 C 440 THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU
SEQRES 34 C 440 SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP
SEQRES 1 D 440 ALA PRO ALA SER LEU LEU PRO PRO ALA PRO GLU HIS SER
SEQRES 2 D 440 PRO PRO SER SER PRO LEU THR GLN PRO PRO GLU GLY PRO
SEQRES 3 D 440 LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER ILE
SEQRES 4 D 440 THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP GLY
SEQRES 5 D 440 PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL PHE
SEQRES 6 D 440 PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO PRO
SEQRES 7 D 440 ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE ILE
SEQRES 8 D 440 ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER GLN
SEQRES 9 D 440 ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU VAL
SEQRES 10 D 440 ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU LEU
SEQRES 11 D 440 VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO ARG
SEQRES 12 D 440 CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL PHE
SEQRES 13 D 440 ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE THR
SEQRES 14 D 440 TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG GLY
SEQRES 15 D 440 ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG CYS
SEQRES 16 D 440 PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN LEU
SEQRES 17 D 440 VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER VAL
SEQRES 18 D 440 ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU CYS
SEQRES 19 D 440 ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE ASP
SEQRES 20 D 440 VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO PRO
SEQRES 21 D 440 GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU VAL
SEQRES 22 D 440 PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA LEU
SEQRES 23 D 440 GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN MET
SEQRES 24 D 440 LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA PRO
SEQRES 25 D 440 PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR ARG
SEQRES 26 D 440 ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU ASP
SEQRES 27 D 440 VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR SER
SEQRES 28 D 440 SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN VAL
SEQRES 29 D 440 ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR ILE
SEQRES 30 D 440 VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS HIS
SEQRES 31 D 440 LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO ALA
SEQRES 32 D 440 ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER LEU
SEQRES 33 D 440 THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE LEU
SEQRES 34 D 440 SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP
HET HEM A 501 43
HET W68 A 502 22
HET BTB A 503 14
HET BTB A 504 14
HET ZN A 505 1
HET GOL A 506 6
HET CL A 507 1
HET GD A 508 1
HET H4B B 501 17
HET HEM B 502 43
HET H4B B 503 17
HET W68 B 504 22
HET BTB B 505 14
HET BTB B 506 14
HET CL B 507 1
HET GD B 508 1
HET BTB B 509 14
HET BTB B 510 14
HET HEM C 501 43
HET H4B C 502 17
HET W68 C 503 22
HET BTB C 504 14
HET ZN C 505 1
HET GOL C 506 6
HET CL C 507 1
HET GD C 508 1
HET HEM D 501 43
HET H4B D 502 17
HET W68 D 503 22
HET BTB D 504 14
HET BTB D 505 14
HET GD D 506 1
HET CL D 507 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM W68 6-(2-{3-FLUORO-5-[3-(METHYLAMINO)PROPYL]PHENYL}ETHYL)-
HETNAM 2 W68 4-METHYLPYRIDIN-2-AMINE
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM GD GADOLINIUM ATOM
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETSYN HEM HEME
HETSYN BTB BIS-TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 HEM 4(C34 H32 FE N4 O4)
FORMUL 6 W68 4(C18 H24 F N3)
FORMUL 7 BTB 9(C8 H19 N O5)
FORMUL 9 ZN 2(ZN 2+)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 11 CL 4(CL 1-)
FORMUL 12 GD 4(GD)
FORMUL 13 H4B 4(C9 H15 N5 O3)
FORMUL 38 HOH *326(H2 O)
HELIX 1 AA1 THR A 83 ALA A 88 5 6
HELIX 2 AA2 GLU A 121 ILE A 138 1 18
HELIX 3 AA3 GLN A 144 GLY A 161 1 18
HELIX 4 AA4 ARG A 166 ALA A 181 1 16
HELIX 5 AA5 GLY A 186 TRP A 190 5 5
HELIX 6 AA6 SER A 203 ASN A 220 1 18
HELIX 7 AA7 ARG A 221 ASN A 223 5 3
HELIX 8 AA8 PRO A 265 ASN A 267 5 3
HELIX 9 AA9 VAL A 268 GLN A 276 1 9
HELIX 10 AB1 LEU A 320 GLY A 327 5 8
HELIX 11 AB2 SER A 359 THR A 364 1 6
HELIX 12 AB3 THR A 364 ASP A 369 1 6
HELIX 13 AB4 ILE A 375 MET A 383 1 9
HELIX 14 AB5 THR A 389 SER A 392 5 4
HELIX 15 AB6 LEU A 393 ALA A 413 1 21
HELIX 16 AB7 ASP A 419 GLY A 439 1 21
HELIX 17 AB8 ASP A 444 VAL A 449 1 6
HELIX 18 AB9 SER A 453 GLN A 462 5 10
HELIX 19 AC1 THR B 83 ALA B 88 5 6
HELIX 20 AC2 PRO B 120 ILE B 138 1 19
HELIX 21 AC3 SER B 143 GLY B 161 1 19
HELIX 22 AC4 ARG B 166 ASN B 180 1 15
HELIX 23 AC5 GLY B 186 TRP B 190 5 5
HELIX 24 AC6 SER B 203 ASN B 220 1 18
HELIX 25 AC7 ARG B 221 ASN B 223 5 3
HELIX 26 AC8 ASN B 267 HIS B 277 1 11
HELIX 27 AC9 PRO B 306 VAL B 310 5 5
HELIX 28 AD1 LEU B 320 GLY B 327 5 8
HELIX 29 AD2 MET B 358 THR B 364 1 7
HELIX 30 AD3 THR B 364 ASP B 369 1 6
HELIX 31 AD4 ILE B 375 MET B 383 1 9
HELIX 32 AD5 THR B 389 SER B 392 5 4
HELIX 33 AD6 LEU B 393 ALA B 413 1 21
HELIX 34 AD7 ASP B 419 GLY B 439 1 21
HELIX 35 AD8 ASP B 444 VAL B 449 1 6
HELIX 36 AD9 SER B 453 THR B 457 5 5
HELIX 37 AE1 THR C 83 ALA C 88 5 6
HELIX 38 AE2 PRO C 120 ILE C 138 1 19
HELIX 39 AE3 SER C 143 GLY C 161 1 19
HELIX 40 AE4 ARG C 166 ASN C 180 1 15
HELIX 41 AE5 GLY C 186 TRP C 190 5 5
HELIX 42 AE6 SER C 203 ASN C 220 1 18
HELIX 43 AE7 ARG C 221 ASN C 223 5 3
HELIX 44 AE8 ASN C 267 HIS C 277 1 11
HELIX 45 AE9 LEU C 320 GLY C 327 5 8
HELIX 46 AF1 MET C 358 THR C 364 1 7
HELIX 47 AF2 THR C 364 ASP C 369 1 6
HELIX 48 AF3 ILE C 375 MET C 383 1 9
HELIX 49 AF4 THR C 389 SER C 392 5 4
HELIX 50 AF5 LEU C 393 ALA C 413 1 21
HELIX 51 AF6 ASP C 419 GLY C 439 1 21
HELIX 52 AF7 ASP C 444 VAL C 449 1 6
HELIX 53 AF8 SER C 453 THR C 457 5 5
HELIX 54 AF9 THR D 83 ALA D 88 5 6
HELIX 55 AG1 PRO D 120 ILE D 138 1 19
HELIX 56 AG2 SER D 143 GLY D 161 1 19
HELIX 57 AG3 ARG D 166 ASN D 180 1 15
HELIX 58 AG4 GLY D 186 TRP D 190 5 5
HELIX 59 AG5 SER D 203 ASN D 220 1 18
HELIX 60 AG6 ARG D 221 ASN D 223 5 3
HELIX 61 AG7 ASN D 267 HIS D 277 1 11
HELIX 62 AG8 PRO D 306 VAL D 310 5 5
HELIX 63 AG9 LEU D 320 GLY D 327 5 8
HELIX 64 AH1 MET D 358 THR D 364 1 7
HELIX 65 AH2 THR D 364 ASP D 369 1 6
HELIX 66 AH3 ILE D 375 MET D 383 1 9
HELIX 67 AH4 THR D 389 SER D 392 5 4
HELIX 68 AH5 LEU D 393 LYS D 414 1 22
HELIX 69 AH6 ASP D 419 GLY D 439 1 21
HELIX 70 AH7 ASP D 444 VAL D 449 1 6
HELIX 71 AH8 SER D 453 GLN D 462 5 10
SHEET 1 AA1 2 ARG A 70 LYS A 72 0
SHEET 2 AA1 2 ILE A 79 TYR A 81 -1 O THR A 80 N VAL A 71
SHEET 1 AA2 4 GLN A 194 ASP A 197 0
SHEET 2 AA2 4 ALA A 227 VAL A 230 1 O ILE A 228 N PHE A 196
SHEET 3 AA2 4 PHE A 353 SER A 354 -1 O SER A 354 N ALA A 227
SHEET 4 AA2 4 ALA A 335 VAL A 336 -1 N VAL A 336 O PHE A 353
SHEET 1 AA3 2 ARG A 242 ILE A 243 0
SHEET 2 AA3 2 LEU A 293 GLN A 294 -1 O GLN A 294 N ARG A 242
SHEET 1 AA4 2 GLY A 253 ARG A 255 0
SHEET 2 AA4 2 VAL A 261 GLY A 263 -1 O ARG A 262 N TYR A 254
SHEET 1 AA5 2 GLU A 312 PRO A 314 0
SHEET 2 AA5 2 ARG A 329 TYR A 331 -1 O TRP A 330 N VAL A 313
SHEET 1 AA6 3 LEU A 346 PHE A 348 0
SHEET 2 AA6 3 LEU A 340 ILE A 343 -1 N LEU A 341 O PHE A 348
SHEET 3 AA6 3 ALA A 472 ARG A 474 -1 O ARG A 474 N LEU A 340
SHEET 1 AA7 2 TYR A 357 MET A 358 0
SHEET 2 AA7 2 ILE A 417 VAL A 418 1 O VAL A 418 N TYR A 357
SHEET 1 AA8 2 ARG B 70 LYS B 72 0
SHEET 2 AA8 2 ILE B 79 TYR B 81 -1 O THR B 80 N VAL B 71
SHEET 1 AA9 4 GLN B 194 ASP B 197 0
SHEET 2 AA9 4 ALA B 227 VAL B 230 1 O ILE B 228 N PHE B 196
SHEET 3 AA9 4 PHE B 353 SER B 354 -1 O SER B 354 N ALA B 227
SHEET 4 AA9 4 ALA B 335 VAL B 336 -1 N VAL B 336 O PHE B 353
SHEET 1 AB1 3 ARG B 242 ILE B 243 0
SHEET 2 AB1 3 LEU B 291 GLN B 294 -1 O GLN B 294 N ARG B 242
SHEET 3 AB1 3 GLU B 301 PHE B 303 -1 O PHE B 303 N LEU B 291
SHEET 1 AB2 2 GLY B 253 ARG B 255 0
SHEET 2 AB2 2 VAL B 261 GLY B 263 -1 O ARG B 262 N TYR B 254
SHEET 1 AB3 2 GLU B 312 PRO B 314 0
SHEET 2 AB3 2 ARG B 329 TYR B 331 -1 O TRP B 330 N VAL B 313
SHEET 1 AB4 3 LEU B 346 PHE B 348 0
SHEET 2 AB4 3 LEU B 340 ILE B 343 -1 N LEU B 341 O PHE B 348
SHEET 3 AB4 3 ALA B 472 ARG B 474 -1 O ARG B 474 N LEU B 340
SHEET 1 AB5 2 ARG C 70 LYS C 72 0
SHEET 2 AB5 2 ILE C 79 TYR C 81 -1 O THR C 80 N VAL C 71
SHEET 1 AB6 4 GLN C 194 ASP C 197 0
SHEET 2 AB6 4 ALA C 227 VAL C 230 1 O ILE C 228 N PHE C 196
SHEET 3 AB6 4 PHE C 353 SER C 354 -1 O SER C 354 N ALA C 227
SHEET 4 AB6 4 ALA C 335 VAL C 336 -1 N VAL C 336 O PHE C 353
SHEET 1 AB7 3 ARG C 242 ILE C 243 0
SHEET 2 AB7 3 LEU C 291 GLN C 294 -1 O GLN C 294 N ARG C 242
SHEET 3 AB7 3 GLU C 301 PHE C 303 -1 O PHE C 303 N LEU C 291
SHEET 1 AB8 2 GLY C 253 ARG C 255 0
SHEET 2 AB8 2 VAL C 261 GLY C 263 -1 O ARG C 262 N TYR C 254
SHEET 1 AB9 2 GLU C 312 PRO C 314 0
SHEET 2 AB9 2 ARG C 329 TYR C 331 -1 O TRP C 330 N VAL C 313
SHEET 1 AC1 3 LEU C 346 PHE C 348 0
SHEET 2 AC1 3 LEU C 340 ILE C 343 -1 N LEU C 341 O PHE C 348
SHEET 3 AC1 3 ALA C 472 ARG C 474 -1 O ARG C 474 N LEU C 340
SHEET 1 AC2 2 ARG D 70 LYS D 72 0
SHEET 2 AC2 2 ILE D 79 TYR D 81 -1 O THR D 80 N VAL D 71
SHEET 1 AC3 4 GLN D 194 ASP D 197 0
SHEET 2 AC3 4 ALA D 227 VAL D 230 1 O ILE D 228 N PHE D 196
SHEET 3 AC3 4 PHE D 353 SER D 354 -1 O SER D 354 N ALA D 227
SHEET 4 AC3 4 ALA D 335 VAL D 336 -1 N VAL D 336 O PHE D 353
SHEET 1 AC4 3 ARG D 242 ILE D 243 0
SHEET 2 AC4 3 LEU D 291 GLN D 294 -1 O GLN D 294 N ARG D 242
SHEET 3 AC4 3 GLU D 301 PHE D 303 -1 O GLU D 301 N LEU D 293
SHEET 1 AC5 2 GLY D 253 ARG D 255 0
SHEET 2 AC5 2 VAL D 261 GLY D 263 -1 O ARG D 262 N TYR D 254
SHEET 1 AC6 2 GLU D 312 PRO D 314 0
SHEET 2 AC6 2 ARG D 329 TYR D 331 -1 O TRP D 330 N VAL D 313
SHEET 1 AC7 3 LEU D 346 PHE D 348 0
SHEET 2 AC7 3 LEU D 340 ILE D 343 -1 N LEU D 341 O PHE D 348
SHEET 3 AC7 3 ALA D 472 ARG D 474 -1 O ARG D 474 N LEU D 340
LINK SG CYS A 94 ZN ZN A 505 1555 1555 2.37
LINK SG CYS A 99 ZN ZN A 505 1555 1555 2.30
LINK SG CYS A 184 FE HEM A 501 1555 1555 2.32
LINK O3 BTB A 503 GD GD A 508 1555 1555 2.74
LINK O4 BTB A 503 GD GD A 508 1555 1555 2.75
LINK N BTB A 503 GD GD A 508 1555 1555 2.88
LINK O6 BTB A 503 GD GD A 508 1555 1555 2.78
LINK O8 BTB A 503 GD GD A 508 1555 1555 2.74
LINK ZN ZN A 505 SG CYS B 94 1555 1555 2.37
LINK ZN ZN A 505 SG CYS B 99 1555 1555 2.45
LINK GD GD A 508 O HOH A 601 1555 1555 2.91
LINK GD GD A 508 O HOH A 644 1555 1555 2.76
LINK GD GD A 508 O HOH D 690 1555 1455 3.21
LINK SG CYS B 184 FE HEM B 502 1555 1555 2.31
LINK O THR B 319 GD GD B 508 1555 1555 2.64
LINK OE1 GLU B 321 GD GD B 508 1555 1555 2.72
LINK O3 BTB B 505 GD GD B 508 1555 1555 2.64
LINK O4 BTB B 505 GD GD B 508 1555 1555 2.70
LINK N BTB B 505 GD GD B 508 1555 1555 2.75
LINK O6 BTB B 505 GD GD B 508 1555 1555 2.75
LINK O8 BTB B 505 GD GD B 508 1555 1555 2.77
LINK GD GD B 508 O HOH B 674 1555 1555 2.62
LINK GD GD B 508 O HOH C 603 1555 1555 2.75
LINK O3 BTB B 509 GD GD C 508 1555 1555 2.56
LINK O4 BTB B 509 GD GD C 508 1555 1555 2.81
LINK N BTB B 509 GD GD C 508 1555 1555 2.91
LINK O6 BTB B 509 GD GD C 508 1555 1555 2.77
LINK O8 BTB B 509 GD GD C 508 1555 1555 3.22
LINK O HOH B 678 GD GD C 508 1555 1555 2.74
LINK O HOH B 707 GD GD C 508 1555 1555 2.78
LINK SG CYS C 94 ZN ZN C 505 1555 1555 2.28
LINK SG CYS C 99 ZN ZN C 505 1555 1555 2.37
LINK SG CYS C 184 FE HEM C 501 1555 1555 2.34
LINK ZN ZN C 505 SG CYS D 94 1555 1555 2.51
LINK ZN ZN C 505 SG CYS D 99 1555 1555 2.43
LINK SG CYS D 184 FE HEM D 501 1555 1555 2.21
LINK O THR D 319 GD GD D 506 1555 1555 2.59
LINK OE1 GLU D 321 GD GD D 506 1555 1555 2.57
LINK OE2 GLU D 321 GD GD D 506 1555 1555 2.62
LINK O3 BTB D 504 GD GD D 506 1555 1555 2.72
LINK O4 BTB D 504 GD GD D 506 1555 1555 2.71
LINK N BTB D 504 GD GD D 506 1555 1555 3.01
LINK O6 BTB D 504 GD GD D 506 1555 1555 3.41
LINK O8 BTB D 504 GD GD D 506 1555 1555 2.81
CISPEP 1 SER A 470 PRO A 471 0 -1.15
CISPEP 2 SER B 470 PRO B 471 0 -0.66
CISPEP 3 SER C 470 PRO C 471 0 0.97
CISPEP 4 SER D 470 PRO D 471 0 -2.45
SITE 1 AC1 11 TRP A 178 CYS A 184 SER A 226 PHE A 353
SITE 2 AC1 11 SER A 354 TRP A 356 GLU A 361 TRP A 447
SITE 3 AC1 11 TYR A 475 W68 A 502 H4B B 501
SITE 1 AC2 7 PHE A 105 VAL A 336 PHE A 353 TRP A 356
SITE 2 AC2 7 TYR A 357 GLU A 361 HEM A 501
SITE 1 AC3 8 TRP A 322 CYS A 382 ASP A 384 GD A 508
SITE 2 AC3 8 HOH A 601 ALA D 325 LEU D 326 ASP D 378
SITE 1 AC4 4 GLU A 377 THR A 387 ARG A 388 ASP D 384
SITE 1 AC5 4 CYS A 94 CYS A 99 CYS B 94 CYS B 99
SITE 1 AC6 1 GLU A 167
SITE 1 AC7 3 GLN A 247 TYR A 357 ASN A 366
SITE 1 AC8 3 BTB A 503 HOH A 601 HOH A 644
SITE 1 AC9 11 SER A 102 ARG A 365 ALA A 446 TRP A 447
SITE 2 AC9 11 HEM A 501 TRP B 445 PHE B 460 HIS B 461
SITE 3 AC9 11 GLN B 462 GLU B 463 HOH B 673
SITE 1 AD1 15 TRP B 178 ARG B 183 CYS B 184 SER B 226
SITE 2 AD1 15 PHE B 353 SER B 354 GLY B 355 TRP B 356
SITE 3 AD1 15 MET B 358 GLU B 361 TRP B 447 PHE B 473
SITE 4 AD1 15 TYR B 475 H4B B 503 W68 B 504
SITE 1 AD2 9 TRP A 445 PHE A 460 GLU A 463 SER B 102
SITE 2 AD2 9 ARG B 365 ALA B 446 TRP B 447 HEM B 502
SITE 3 AD2 9 HOH B 613
SITE 1 AD3 8 PHE B 105 VAL B 336 TRP B 356 GLU B 361
SITE 2 AD3 8 TYR B 475 HEM B 502 CL B 507 HOH B 676
SITE 1 AD4 8 THR B 319 GLU B 321 GD B 508 HOH B 674
SITE 2 AD4 8 VAL C 261 TYR C 373 ASN C 374 ASP C 378
SITE 1 AD5 5 ASP B 297 GLU B 298 HOH B 603 HOH B 670
SITE 2 AD5 5 GLU D 167
SITE 1 AD6 5 GLN B 247 TYR B 357 ASN B 366 W68 B 504
SITE 2 AD6 5 HOH B 676
SITE 1 AD7 5 THR B 319 GLU B 321 BTB B 505 HOH B 674
SITE 2 AD7 5 HOH C 603
SITE 1 AD8 8 ALA B 325 LEU B 326 ASP B 378 HOH B 678
SITE 2 AD8 8 VAL C 381 CYS C 382 ASP C 384 GD C 508
SITE 1 AD9 2 ASP B 384 GLU C 377
SITE 1 AE1 13 TRP C 178 CYS C 184 SER C 226 PHE C 353
SITE 2 AE1 13 SER C 354 GLY C 355 TRP C 356 GLU C 361
SITE 3 AE1 13 TRP C 447 PHE C 473 TYR C 475 H4B C 502
SITE 4 AE1 13 W68 C 503
SITE 1 AE2 10 SER C 102 ARG C 365 ALA C 446 TRP C 447
SITE 2 AE2 10 HEM C 501 HOH C 645 TRP D 445 PHE D 460
SITE 3 AE2 10 HIS D 461 GLU D 463
SITE 1 AE3 8 PHE C 105 VAL C 336 PHE C 353 TRP C 356
SITE 2 AE3 8 GLU C 361 TRP C 447 HEM C 501 HOH C 652
SITE 1 AE4 1 GLU C 298
SITE 1 AE5 4 CYS C 94 CYS C 99 CYS D 94 CYS D 99
SITE 1 AE6 1 GLU C 167
SITE 1 AE7 3 GLN C 247 TYR C 357 ASN C 366
SITE 1 AE8 3 BTB B 509 HOH B 678 HOH B 707
SITE 1 AE9 14 TRP D 178 ARG D 183 CYS D 184 VAL D 185
SITE 2 AE9 14 SER D 226 PHE D 353 SER D 354 TRP D 356
SITE 3 AE9 14 GLU D 361 TRP D 447 PHE D 473 TYR D 475
SITE 4 AE9 14 H4B D 502 W68 D 503
SITE 1 AF1 12 TRP C 445 PHE C 460 HIS C 461 GLN C 462
SITE 2 AF1 12 GLU C 463 SER D 102 ARG D 365 ALA D 446
SITE 3 AF1 12 TRP D 447 HEM D 501 HOH D 627 HOH D 670
SITE 1 AF2 10 PHE D 105 GLN D 247 VAL D 336 PHE D 353
SITE 2 AF2 10 TRP D 356 GLU D 361 TRP D 447 HEM D 501
SITE 3 AF2 10 CL D 507 HOH D 660
SITE 1 AF3 7 VAL A 261 TYR A 373 ASN A 374 ASP A 378
SITE 2 AF3 7 THR D 319 GLU D 321 GD D 506
SITE 1 AF4 2 ASP D 297 GLU D 298
SITE 1 AF5 3 THR D 319 GLU D 321 BTB D 504
SITE 1 AF6 6 GLN D 247 ARG D 250 TYR D 357 ASN D 366
SITE 2 AF6 6 W68 D 503 HOH D 660
CRYST1 59.643 152.780 108.882 90.00 90.78 90.00 P 1 21 1 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 0.016766 0.000000 0.000229 0.00000
SCALE2 0.000000 0.006545 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009185 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
