HEADER IMMUNE SYSTEM/OXIDOREDUCTASE 18-JUL-13 3WFE
TITLE REDUCED AND CYANIDE-BOUND CYTOCHROME C-DEPENDENT NITRIC OXIDE
TITLE 2 REDUCTASE (CNOR) FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH ANTIBODY
TITLE 3 FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT CHAIN;
COMPND 3 CHAIN: L;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN;
COMPND 6 CHAIN: H;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: NITRIC OXIDE REDUCTASE SUBUNIT B;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: NOR LARGE SUBUNIT, NITRIC OXIDE REDUCTASE CYTOCHROME B
COMPND 11 SUBUNIT;
COMPND 12 EC: 1.7.2.5;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: NITRIC OXIDE REDUCTASE SUBUNIT C;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: NOR SMALL SUBUNIT, NITRIC OXIDE REDUCTASE CYTOCHROME C
COMPND 17 SUBUNIT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_TAXID: 10090;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 6 ORGANISM_TAXID: 10090;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 9 ORGANISM_TAXID: 208964;
SOURCE 10 STRAIN: PAO1;
SOURCE 11 MOL_ID: 4;
SOURCE 12 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 13 ORGANISM_TAXID: 208964;
SOURCE 14 STRAIN: PAO1
KEYWDS METAL-BINDING, MEMBRANE PROTEIN, IMMUNE SYSTEM-OXIDOREDUCTASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.SATO,S.ISHII,T.HINO,H.SUGIMOTO,Y.FUKUMORI,Y.SHIRO,T.TOSHA
REVDAT 4 08-NOV-23 3WFE 1 REMARK
REVDAT 3 24-AUG-22 3WFE 1 JRNL REMARK SEQADV LINK
REVDAT 2 22-NOV-17 3WFE 1 REMARK
REVDAT 1 28-MAY-14 3WFE 0
JRNL AUTH N.SATO,S.ISHII,H.SUGIMOTO,T.HINO,Y.FUKUMORI,Y.SAKO,Y.SHIRO,
JRNL AUTH 2 T.TOSHA
JRNL TITL STRUCTURES OF REDUCED AND LIGAND-BOUND NITRIC OXIDE
JRNL TITL 2 REDUCTASE PROVIDE INSIGHTS INTO FUNCTIONAL DIFFERENCES IN
JRNL TITL 3 RESPIRATORY ENZYMES.
JRNL REF PROTEINS V. 82 1258 2014
JRNL REFN ESSN 1097-0134
JRNL PMID 24338896
JRNL DOI 10.1002/PROT.24492
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.HINO,Y.MATSUMOTO,S.NAGANO,H.SUGIMOTO,Y.FUKUMORI,T.MURATA,
REMARK 1 AUTH 2 S.IWATA,Y.SHIRO
REMARK 1 TITL STRUCTURAL BASIS OF BIOLOGICAL N2O GENERATION BY BACTERIAL
REMARK 1 TITL 2 NITRIC OXIDE REDUCTASE
REMARK 1 REF SCIENCE V. 330 1666 2010
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 21109633
REMARK 1 DOI 10.1126/SCIENCE.1195591
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 66111
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3358
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4392
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 222
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 201
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.83000
REMARK 3 B22 (A**2) : -0.70000
REMARK 3 B33 (A**2) : 1.53000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.262
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.146
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.756
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8527 ; 0.015 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7955 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11632 ; 1.808 ; 2.036
REMARK 3 BOND ANGLES OTHERS (DEGREES): 18133 ; 0.980 ; 3.023
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1025 ; 6.646 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 334 ;36.476 ;23.204
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1304 ;20.202 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;21.612 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1269 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9644 ; 0.012 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): 2020 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 108
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1344 -16.2270 -0.5563
REMARK 3 T TENSOR
REMARK 3 T11: 0.2223 T22: 0.4339
REMARK 3 T33: 0.2555 T12: -0.0370
REMARK 3 T13: 0.0278 T23: -0.1173
REMARK 3 L TENSOR
REMARK 3 L11: 0.9292 L22: 1.1308
REMARK 3 L33: 0.0603 L12: -0.7317
REMARK 3 L13: 0.1724 L23: -0.0390
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: 0.1182 S13: 0.0136
REMARK 3 S21: -0.0343 S22: 0.1023 S23: -0.0447
REMARK 3 S31: -0.0305 S32: 0.1131 S33: -0.0453
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 124
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4466 -12.5445 -0.6053
REMARK 3 T TENSOR
REMARK 3 T11: 0.2498 T22: 0.3811
REMARK 3 T33: 0.2668 T12: -0.0045
REMARK 3 T13: -0.0311 T23: -0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 0.7976 L22: 0.6646
REMARK 3 L33: 1.0111 L12: 0.3553
REMARK 3 L13: 0.4583 L23: 0.7936
REMARK 3 S TENSOR
REMARK 3 S11: -0.0566 S12: 0.0064 S13: 0.0955
REMARK 3 S21: -0.0782 S22: -0.0282 S23: 0.0873
REMARK 3 S31: -0.0375 S32: -0.0513 S33: 0.0848
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 458
REMARK 3 RESIDUE RANGE : B 801 B 806
REMARK 3 RESIDUE RANGE : C 201 C 201
REMARK 3 RESIDUE RANGE : B 807 B 807
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1637 24.2822 35.0160
REMARK 3 T TENSOR
REMARK 3 T11: 0.4353 T22: 0.2704
REMARK 3 T33: 0.1529 T12: -0.0315
REMARK 3 T13: 0.0321 T23: -0.0936
REMARK 3 L TENSOR
REMARK 3 L11: 0.1975 L22: 1.8271
REMARK 3 L33: 1.2178 L12: -0.3597
REMARK 3 L13: -0.3431 L23: 1.4471
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: -0.0486 S13: -0.0362
REMARK 3 S21: -0.1731 S22: 0.0372 S23: -0.0611
REMARK 3 S31: -0.2608 S32: 0.0725 S33: -0.0849
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 37
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1520 16.2542 56.6246
REMARK 3 T TENSOR
REMARK 3 T11: 0.5776 T22: 0.3851
REMARK 3 T33: 0.0335 T12: 0.0055
REMARK 3 T13: 0.0799 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 1.3210 L22: 15.2824
REMARK 3 L33: 1.5164 L12: -3.7948
REMARK 3 L13: -0.5945 L23: 3.9906
REMARK 3 S TENSOR
REMARK 3 S11: -0.0481 S12: -0.1390 S13: 0.1123
REMARK 3 S21: 0.9475 S22: -0.0623 S23: -0.0151
REMARK 3 S31: 0.4603 S32: -0.0381 S33: 0.1103
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 109 L 213
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1782 -45.0608 -21.9802
REMARK 3 T TENSOR
REMARK 3 T11: 0.3683 T22: 0.3264
REMARK 3 T33: 0.1995 T12: 0.0197
REMARK 3 T13: -0.0319 T23: -0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 2.6696 L22: 0.6007
REMARK 3 L33: 1.5703 L12: 0.6224
REMARK 3 L13: 0.9058 L23: 0.9292
REMARK 3 S TENSOR
REMARK 3 S11: -0.0266 S12: -0.0365 S13: 0.0413
REMARK 3 S21: -0.1359 S22: 0.0319 S23: 0.0082
REMARK 3 S31: -0.0048 S32: 0.0705 S33: -0.0053
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 125 H 225
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2684 -48.0988 -10.7864
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.3799
REMARK 3 T33: 0.2586 T12: 0.0137
REMARK 3 T13: -0.0035 T23: -0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 1.9648 L22: 1.4548
REMARK 3 L33: 0.3394 L12: -0.9806
REMARK 3 L13: -0.5691 L23: 0.2039
REMARK 3 S TENSOR
REMARK 3 S11: -0.0463 S12: -0.2046 S13: -0.1674
REMARK 3 S21: -0.0535 S22: -0.0616 S23: 0.1214
REMARK 3 S31: 0.0681 S32: -0.0094 S33: 0.1079
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 38 C 146
REMARK 3 ORIGIN FOR THE GROUP (A): 31.2456 -3.7481 28.2846
REMARK 3 T TENSOR
REMARK 3 T11: 0.3264 T22: 0.3535
REMARK 3 T33: 0.2575 T12: 0.0350
REMARK 3 T13: -0.0745 T23: -0.1225
REMARK 3 L TENSOR
REMARK 3 L11: 0.3248 L22: 1.6939
REMARK 3 L33: 1.8238 L12: -0.4788
REMARK 3 L13: -0.7337 L23: 1.4192
REMARK 3 S TENSOR
REMARK 3 S11: -0.1104 S12: 0.0268 S13: 0.0233
REMARK 3 S21: 0.3871 S22: 0.2077 S23: -0.0144
REMARK 3 S31: 0.2607 S32: 0.1416 S33: -0.0973
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3WFE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000096266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66399
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.2310
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.52600
REMARK 200 R SYM FOR SHELL (I) : 0.52600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.684
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3O0R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CITRATE, PH 6.0, VAPOR
REMARK 280 DIFFUSION, 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 45.34400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.64400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.69050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.64400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.34400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.69050
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -179.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, B, C
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 MET B 1
REMARK 465 MET B 2
REMARK 465 SER B 3
REMARK 465 PRO B 4
REMARK 465 ASN B 5
REMARK 465 GLY B 6
REMARK 465 SER B 7
REMARK 465 LEU B 8
REMARK 465 LYS B 9
REMARK 465 ARG B 459
REMARK 465 ARG B 460
REMARK 465 GLY B 461
REMARK 465 LYS B 462
REMARK 465 ALA B 463
REMARK 465 ALA B 464
REMARK 465 ALA B 465
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 THR C 4
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 C CYN B 804 N CYN B 805 1.62
REMARK 500 N CYN B 804 C CYN B 805 1.67
REMARK 500 C CYN B 804 C CYN B 805 1.72
REMARK 500 NA HEM B 802 C CYN B 804 2.07
REMARK 500 FE HEM B 802 N CYN B 805 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG H 199 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
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 ARG L 30 -117.36 47.20
REMARK 500 ALA L 84 176.64 179.37
REMARK 500 ASP L 151 46.10 39.49
REMARK 500 THR L 200 3.91 -63.94
REMARK 500 SER L 201 127.74 -175.91
REMARK 500 GLN H 43 -5.23 -141.15
REMARK 500 ASN H 55 11.20 -147.04
REMARK 500 VAL H 106 48.40 -87.84
REMARK 500 ASP H 141 41.32 -96.50
REMARK 500 THR H 143 -61.26 -125.15
REMARK 500 SER H 167 18.93 56.51
REMARK 500 SER H 183 -121.95 64.52
REMARK 500 TYR B 89 -39.25 -37.38
REMARK 500 SER B 90 103.72 -164.37
REMARK 500 PRO B 116 139.00 -38.35
REMARK 500 PHE B 136 -6.69 65.15
REMARK 500 PRO B 140 157.98 -49.50
REMARK 500 TRP B 209 -75.40 -64.88
REMARK 500 LEU B 371 -39.63 -160.25
REMARK 500 MET C 45 73.92 -69.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 60 NE2
REMARK 620 2 HEM B 801 NA 88.6
REMARK 620 3 HEM B 801 NB 92.2 91.5
REMARK 620 4 HEM B 801 NC 93.4 177.7 89.6
REMARK 620 5 HEM B 801 ND 89.9 88.4 177.9 90.5
REMARK 620 6 HIS B 349 NE2 177.2 94.2 88.0 83.8 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 808 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 135 OE1
REMARK 620 2 GLU B 135 OE2 50.9
REMARK 620 3 HEM B 801 O2D 80.2 125.6
REMARK 620 4 HEM B 802 O2A 98.3 80.5 85.4
REMARK 620 5 HOH B 905 O 131.4 82.2 147.7 83.7
REMARK 620 6 GLY C 71 O 82.5 84.5 114.7 159.7 80.8
REMARK 620 7 TYR C 73 OH 149.4 155.1 79.3 102.4 73.6 85.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 803 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 207 ND1
REMARK 620 2 GLU B 211 OE1 91.8
REMARK 620 3 GLU B 211 OE2 71.7 59.7
REMARK 620 4 HIS B 258 NE2 95.1 88.2 143.9
REMARK 620 5 HIS B 259 NE2 90.9 170.4 129.8 82.4
REMARK 620 6 CYN B 805 N 156.2 82.5 85.6 107.7 98.5
REMARK 620 7 CYN B 805 C 126.7 93.6 66.0 137.9 92.1 31.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 802 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 347 NE2
REMARK 620 2 HEM B 802 NA 84.1
REMARK 620 3 HEM B 802 NB 90.8 86.6
REMARK 620 4 HEM B 802 NC 94.4 177.2 91.1
REMARK 620 5 HEM B 802 ND 86.7 94.4 177.2 87.8
REMARK 620 6 CYN B 804 C 141.9 59.8 76.6 121.2 106.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC C 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 65 NE2
REMARK 620 2 HEC C 201 NA 94.0
REMARK 620 3 HEC C 201 NB 85.3 86.1
REMARK 620 4 HEC C 201 NC 85.0 179.0 93.9
REMARK 620 5 HEC C 201 ND 92.9 96.2 177.2 83.8
REMARK 620 6 MET C 112 SD 177.2 84.2 92.3 96.8 89.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10M B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10M B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC C 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O0R RELATED DB: PDB
REMARK 900 RELATED ID: 3WFB RELATED DB: PDB
REMARK 900 RELATED ID: 3WFC RELATED DB: PDB
REMARK 900 RELATED ID: 3WFD RELATED DB: PDB
DBREF 3WFE L 1 213 PDB 3WFE 3WFE 1 213
DBREF 3WFE H 1 225 PDB 3WFE 3WFE 1 225
DBREF 3WFE B 1 465 UNP Q59647 NORB_PSEAE 1 466
DBREF 3WFE C 1 146 UNP Q59646 NORC_PSEAE 1 146
SEQADV 3WFE B UNP Q59647 ARG 297 DELETION
SEQADV 3WFE LYS C 100 UNP Q59646 ASN 100 CONFLICT
SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO PRO TYR LEU ALA ALA
SEQRES 2 L 213 SER PRO GLY GLU THR ILE THR ILE ASN CYS ARG ALA SER
SEQRES 3 L 213 LYS SER ILE ARG LYS TYR LEU ALA TRP TYR GLN GLU LYS
SEQRES 4 L 213 PRO GLY LYS THR ASN LYS LEU LEU ILE TYR SER GLY SER
SEQRES 5 L 213 THR LEU GLN PHE GLY ILE PRO SER ARG PHE SER GLY SER
SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU
SEQRES 7 L 213 GLU PRO GLU ASP PHE ALA MET TYR TYR CYS GLN GLN HIS
SEQRES 8 L 213 ASN GLU TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU
SEQRES 9 L 213 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 213 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 213 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 213 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 213 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 213 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 213 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 213 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 213 PHE ASN ARG ASN GLU
SEQRES 1 H 225 GLU VAL GLN LEU GLN GLN SER GLY THR VAL LEU ALA ARG
SEQRES 2 H 225 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 H 225 TYR SER PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 H 225 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA VAL TYR
SEQRES 5 H 225 PRO GLY ASN SER ASP THR SER TYR ASN GLN LYS PHE LYS
SEQRES 6 H 225 GLY LYS ALA LYS LEU THR ALA VAL THR SER ALA SER THR
SEQRES 7 H 225 ALA TYR MET GLU LEU SER SER LEU THR ASN GLU ASP SER
SEQRES 8 H 225 ALA VAL TYR TYR CYS SER ARG SER SER LEU ASP GLY TYR
SEQRES 9 H 225 TYR VAL LYS ASN TRP CYS PHE ASP VAL TRP GLY GLN GLY
SEQRES 10 H 225 THR THR VAL THR VAL SER SER ALA LYS THR THR ALA PRO
SEQRES 11 H 225 SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR THR
SEQRES 12 H 225 GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR
SEQRES 13 H 225 PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER
SEQRES 14 H 225 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN
SEQRES 15 H 225 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR
SEQRES 16 H 225 SER SER THR ARG PRO SER GLN SER ILE THR CYS ASN VAL
SEQRES 17 H 225 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE
SEQRES 18 H 225 GLU PRO ARG GLY
SEQRES 1 B 465 MET MET SER PRO ASN GLY SER LEU LYS PHE ALA SER GLN
SEQRES 2 B 465 ALA VAL ALA LYS PRO TYR PHE VAL PHE ALA LEU ILE LEU
SEQRES 3 B 465 PHE VAL GLY GLN ILE LEU PHE GLY LEU ILE MET GLY LEU
SEQRES 4 B 465 GLN TYR VAL VAL GLY ASP PHE LEU PHE PRO ALA ILE PRO
SEQRES 5 B 465 PHE ASN VAL ALA ARG MET VAL HIS THR ASN LEU LEU ILE
SEQRES 6 B 465 VAL TRP LEU LEU PHE GLY PHE MET GLY ALA ALA TYR TYR
SEQRES 7 B 465 LEU VAL PRO GLU GLU SER ASP CYS GLU LEU TYR SER PRO
SEQRES 8 B 465 LYS LEU ALA TRP ILE LEU PHE TRP VAL PHE ALA ALA ALA
SEQRES 9 B 465 GLY VAL LEU THR ILE LEU GLY TYR LEU LEU VAL PRO TYR
SEQRES 10 B 465 ALA GLY LEU ALA ARG LEU THR GLY ASN GLU LEU TRP PRO
SEQRES 11 B 465 THR MET GLY ARG GLU PHE LEU GLU GLN PRO THR ILE SER
SEQRES 12 B 465 LYS ALA GLY ILE VAL ILE VAL ALA LEU GLY PHE LEU PHE
SEQRES 13 B 465 ASN VAL GLY MET THR VAL LEU ARG GLY ARG LYS THR ALA
SEQRES 14 B 465 ILE SER MET VAL LEU MET THR GLY LEU ILE GLY LEU ALA
SEQRES 15 B 465 LEU LEU PHE LEU PHE SER PHE TYR ASN PRO GLU ASN LEU
SEQRES 16 B 465 THR ARG ASP LYS PHE TYR TRP TRP TRP VAL VAL HIS LEU
SEQRES 17 B 465 TRP VAL GLU GLY VAL TRP GLU LEU ILE MET GLY ALA ILE
SEQRES 18 B 465 LEU ALA PHE VAL LEU VAL LYS ILE THR GLY VAL ASP ARG
SEQRES 19 B 465 GLU VAL ILE GLU LYS TRP LEU TYR VAL ILE ILE ALA MET
SEQRES 20 B 465 ALA LEU ILE SER GLY ILE ILE GLY THR GLY HIS HIS TYR
SEQRES 21 B 465 PHE TRP ILE GLY VAL PRO GLY TYR TRP LEU TRP LEU GLY
SEQRES 22 B 465 SER VAL PHE SER ALA LEU GLU PRO LEU PRO PHE PHE ALA
SEQRES 23 B 465 MET VAL LEU PHE ALA PHE ASN THR ILE ASN ARG ARG ARG
SEQRES 24 B 465 ARG ASP TYR PRO ASN ARG ALA VAL ALA LEU TRP ALA MET
SEQRES 25 B 465 GLY THR THR VAL MET ALA PHE LEU GLY ALA GLY VAL TRP
SEQRES 26 B 465 GLY PHE MET HIS THR LEU ALA PRO VAL ASN TYR TYR THR
SEQRES 27 B 465 HIS GLY THR GLN LEU THR ALA ALA HIS GLY HIS MET ALA
SEQRES 28 B 465 PHE TYR GLY ALA TYR ALA MET ILE VAL MET THR ILE ILE
SEQRES 29 B 465 SER TYR ALA MET PRO ARG LEU ARG GLY ILE GLY GLU ALA
SEQRES 30 B 465 MET ASP ASN ARG SER GLN VAL LEU GLU MET TRP GLY PHE
SEQRES 31 B 465 TRP LEU MET THR VAL ALA MET VAL PHE ILE THR LEU PHE
SEQRES 32 B 465 LEU SER ALA ALA GLY VAL LEU GLN VAL TRP LEU GLN ARG
SEQRES 33 B 465 MET PRO ALA ASP GLY ALA ALA MET THR PHE MET ALA THR
SEQRES 34 B 465 GLN ASP GLN LEU ALA ILE PHE TYR TRP LEU ARG GLU GLY
SEQRES 35 B 465 ALA GLY VAL VAL PHE LEU ILE GLY LEU VAL ALA TYR LEU
SEQRES 36 B 465 LEU SER PHE ARG ARG GLY LYS ALA ALA ALA
SEQRES 1 C 146 MET SER GLU THR PHE THR LYS GLY MET ALA ARG ASN ILE
SEQRES 2 C 146 TYR PHE GLY GLY SER VAL PHE PHE ILE LEU LEU PHE LEU
SEQRES 3 C 146 ALA LEU THR TYR HIS THR GLU LYS THR LEU PRO GLU ARG
SEQRES 4 C 146 THR ASN GLU ALA ALA MET SER ALA ALA VAL VAL ARG GLY
SEQRES 5 C 146 LYS LEU VAL TRP GLU GLN ASN ASN CYS VAL GLY CYS HIS
SEQRES 6 C 146 THR LEU LEU GLY GLU GLY ALA TYR PHE ALA PRO GLU LEU
SEQRES 7 C 146 GLY ASN VAL VAL GLY ARG ARG GLY GLY GLU GLU GLY PHE
SEQRES 8 C 146 ASN THR PHE LEU GLN ALA TRP MET LYS ILE GLN PRO LEU
SEQRES 9 C 146 ASN VAL PRO GLY ARG ARG ALA MET PRO GLN PHE HIS LEU
SEQRES 10 C 146 SER GLU GLY GLN VAL ASP ASP LEU ALA GLU PHE LEU LYS
SEQRES 11 C 146 TRP SER SER LYS ILE ASP THR ASN GLN TRP PRO PRO ASN
SEQRES 12 C 146 LYS GLU GLY
HET HEM B 801 43
HET HEM B 802 43
HET FE B 803 1
HET CYN B 804 2
HET CYN B 805 2
HET 10M B 806 33
HET 10M B 807 33
HET CA B 808 1
HET HEC C 201 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FE FE (III) ION
HETNAM CYN CYANIDE ION
HETNAM 10M DECYL 4-O-ALPHA-D-GLUCOPYRANOSYL-1-THIO-BETA-D-
HETNAM 2 10M GLUCOPYRANOSIDE
HETNAM CA CALCIUM ION
HETNAM HEC HEME C
HETSYN HEM HEME
HETSYN 10M (2R,3R,4S,5S,6R)-2-((2R,3S,4R,5R,6S)-6-DECYLSULFANYL-4,
HETSYN 2 10M 5-DIHYDROXY-2-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3-YLOXY)-
HETSYN 3 10M 6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL, N-DECYL-
HETSYN 4 10M BETA-D-THIOMALTOSIDE
FORMUL 5 HEM 2(C34 H32 FE N4 O4)
FORMUL 7 FE FE 3+
FORMUL 8 CYN 2(C N 1-)
FORMUL 10 10M 2(C22 H42 O10 S)
FORMUL 12 CA CA 2+
FORMUL 13 HEC C34 H34 FE N4 O4
FORMUL 14 HOH *242(H2 O)
HELIX 1 1 GLU L 79 PHE L 83 5 5
HELIX 2 2 SER L 121 SER L 127 1 7
HELIX 3 3 LYS L 183 ARG L 188 1 6
HELIX 4 4 SER H 28 TYR H 32 5 5
HELIX 5 5 GLN H 62 LYS H 65 5 4
HELIX 6 6 THR H 87 SER H 91 5 5
HELIX 7 7 SER H 167 SER H 169 5 3
HELIX 8 8 PRO H 211 SER H 214 5 4
HELIX 9 9 PHE B 10 ALA B 14 5 5
HELIX 10 10 VAL B 15 TYR B 41 1 27
HELIX 11 11 PRO B 52 ASP B 85 1 34
HELIX 12 12 SER B 90 VAL B 115 1 26
HELIX 13 13 PRO B 116 THR B 124 1 9
HELIX 14 14 PRO B 140 ARG B 164 1 25
HELIX 15 15 THR B 168 LEU B 186 1 19
HELIX 16 16 PHE B 187 TYR B 190 5 4
HELIX 17 17 ASN B 194 GLU B 211 1 18
HELIX 18 18 GLY B 212 GLY B 231 1 20
HELIX 19 19 ASP B 233 THR B 256 1 24
HELIX 20 20 GLY B 257 TYR B 260 5 4
HELIX 21 21 GLY B 267 ALA B 278 1 12
HELIX 22 22 GLU B 280 ARG B 297 1 18
HELIX 23 23 ASN B 304 ALA B 322 1 19
HELIX 24 24 GLY B 323 HIS B 329 1 7
HELIX 25 25 LEU B 331 HIS B 339 1 9
HELIX 26 26 THR B 341 MET B 368 1 28
HELIX 27 27 ASP B 379 ARG B 416 1 38
HELIX 28 28 THR B 425 LEU B 433 1 9
HELIX 29 29 LEU B 433 LEU B 456 1 24
HELIX 30 30 THR C 6 THR C 40 1 35
HELIX 31 31 ASN C 41 MET C 45 5 5
HELIX 32 32 SER C 46 ASN C 59 1 14
HELIX 33 33 ASN C 60 CYS C 64 5 5
HELIX 34 34 ASN C 80 ARG C 84 5 5
HELIX 35 35 GLY C 86 GLN C 102 1 17
HELIX 36 36 SER C 118 LYS C 134 1 17
SHEET 1 A 4 MET L 4 SER L 7 0
SHEET 2 A 4 ILE L 19 ALA L 25 -1 O ASN L 22 N SER L 7
SHEET 3 A 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 B 6 TYR L 10 ALA L 13 0
SHEET 2 B 6 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11
SHEET 3 B 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104
SHEET 4 B 6 LEU L 33 GLU L 38 -1 N ALA L 34 O GLN L 89
SHEET 5 B 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35
SHEET 6 B 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49
SHEET 1 C 4 TYR L 10 ALA L 13 0
SHEET 2 C 4 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11
SHEET 3 C 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104
SHEET 4 C 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 D 4 THR L 114 PHE L 118 0
SHEET 2 D 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114
SHEET 3 D 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 130
SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178
SHEET 1 E 4 SER L 153 ARG L 155 0
SHEET 2 E 4 ASN L 145 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 E 4 SER L 191 HIS L 198 -1 O GLU L 195 N LYS L 147
SHEET 4 E 4 SER L 201 ASN L 210 -1 O LYS L 207 N CYS L 194
SHEET 1 F 4 GLN H 3 GLN H 6 0
SHEET 2 F 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5
SHEET 3 F 4 THR H 78 LEU H 83 -1 O LEU H 83 N VAL H 18
SHEET 4 F 4 ALA H 68 VAL H 73 -1 N THR H 71 O TYR H 80
SHEET 1 G 6 VAL H 10 ALA H 12 0
SHEET 2 G 6 THR H 118 VAL H 122 1 O THR H 121 N VAL H 10
SHEET 3 G 6 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 120
SHEET 4 G 6 MET H 34 GLN H 39 -1 N HIS H 35 O SER H 97
SHEET 5 G 6 GLU H 46 VAL H 51 -1 O GLU H 46 N LYS H 38
SHEET 6 G 6 THR H 58 TYR H 60 -1 O SER H 59 N ALA H 50
SHEET 1 H 4 VAL H 10 ALA H 12 0
SHEET 2 H 4 THR H 118 VAL H 122 1 O THR H 121 N VAL H 10
SHEET 3 H 4 ALA H 92 SER H 99 -1 N ALA H 92 O VAL H 120
SHEET 4 H 4 PHE H 111 TRP H 114 -1 O VAL H 113 N ARG H 98
SHEET 1 I 4 SER H 131 LEU H 135 0
SHEET 2 I 4 SER H 146 TYR H 156 -1 O GLY H 150 N LEU H 135
SHEET 3 I 4 LEU H 185 THR H 195 -1 O TYR H 186 N TYR H 156
SHEET 4 I 4 VAL H 174 THR H 176 -1 N HIS H 175 O SER H 191
SHEET 1 J 4 SER H 131 LEU H 135 0
SHEET 2 J 4 SER H 146 TYR H 156 -1 O GLY H 150 N LEU H 135
SHEET 3 J 4 LEU H 185 THR H 195 -1 O TYR H 186 N TYR H 156
SHEET 4 J 4 VAL H 180 GLN H 182 -1 N GLN H 182 O LEU H 185
SHEET 1 K 3 THR H 162 TRP H 165 0
SHEET 2 K 3 THR H 205 HIS H 210 -1 O ASN H 207 N THR H 164
SHEET 3 K 3 THR H 215 LYS H 220 -1 O THR H 215 N HIS H 210
SHEET 1 L 2 THR C 66 LEU C 67 0
SHEET 2 L 2 GLU C 70 GLY C 71 -1 O GLU C 70 N LEU C 67
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.10
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.02
SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.10
SSBOND 4 CYS H 151 CYS H 206 1555 1555 2.03
LINK SG CYS C 61 CAB HEC C 201 1555 1555 1.82
LINK SG CYS C 64 CAC HEC C 201 1555 1555 1.88
LINK NE2 HIS B 60 FE HEM B 801 1555 1555 1.99
LINK OE1 GLU B 135 CA CA B 808 1555 1555 2.35
LINK OE2 GLU B 135 CA CA B 808 1555 1555 2.67
LINK ND1 HIS B 207 FE FE B 803 1555 1555 2.22
LINK OE1 GLU B 211 FE FE B 803 1555 1555 2.07
LINK OE2 GLU B 211 FE FE B 803 1555 1555 2.19
LINK NE2 HIS B 258 FE FE B 803 1555 1555 2.14
LINK NE2 HIS B 259 FE FE B 803 1555 1555 2.18
LINK NE2 HIS B 347 FE HEM B 802 1555 1555 2.09
LINK NE2 HIS B 349 FE HEM B 801 1555 1555 2.01
LINK O2D HEM B 801 CA CA B 808 1555 1555 2.43
LINK FE HEM B 802 C CYN B 804 1555 1555 2.07
LINK O2A HEM B 802 CA CA B 808 1555 1555 2.40
LINK FE FE B 803 N CYN B 805 1555 1555 2.29
LINK FE FE B 803 C CYN B 805 1555 1555 1.98
LINK CA CA B 808 O HOH B 905 1555 1555 2.54
LINK CA CA B 808 O GLY C 71 1555 1555 2.51
LINK CA CA B 808 OH TYR C 73 1555 1555 2.74
LINK NE2 HIS C 65 FE HEC C 201 1555 1555 1.99
LINK SD MET C 112 FE HEC C 201 1555 1555 2.32
CISPEP 1 SER L 7 PRO L 8 0 -6.53
CISPEP 2 TYR L 94 PRO L 95 0 -12.67
CISPEP 3 TYR L 140 PRO L 141 0 2.36
CISPEP 4 PHE H 157 PRO H 158 0 -5.82
CISPEP 5 GLU H 159 PRO H 160 0 5.38
CISPEP 6 ARG H 199 PRO H 200 0 13.95
CISPEP 7 PHE B 48 PRO B 49 0 3.47
CISPEP 8 GLN C 102 PRO C 103 0 -4.18
CISPEP 9 TRP C 140 PRO C 141 0 -0.06
SITE 1 AC1 20 GLN B 30 GLY B 34 MET B 37 TYR B 41
SITE 2 AC1 20 PHE B 53 ARG B 57 HIS B 60 THR B 61
SITE 3 AC1 20 GLU B 135 HIS B 349 PHE B 352 TYR B 353
SITE 4 AC1 20 MET B 397 ARG B 440 GLY B 444 HEM B 802
SITE 5 AC1 20 CA B 808 ALA C 72 TYR C 73 PHE C 74
SITE 1 AC2 28 GLU B 135 PHE B 136 TRP B 203 VAL B 210
SITE 2 AC2 28 GLU B 211 HIS B 258 SER B 277 GLU B 280
SITE 3 AC2 28 PHE B 284 ALA B 322 GLY B 326 PHE B 327
SITE 4 AC2 28 HIS B 329 THR B 330 ASN B 335 HIS B 339
SITE 5 AC2 28 GLY B 340 THR B 344 HIS B 347 ALA B 351
SITE 6 AC2 28 PHE B 352 TYR B 356 HEM B 801 CYN B 804
SITE 7 AC2 28 CYN B 805 CA B 808 HOH B 905 HOH B 926
SITE 1 AC3 6 HIS B 207 GLU B 211 HIS B 258 HIS B 259
SITE 2 AC3 6 CYN B 804 CYN B 805
SITE 1 AC4 4 GLU B 211 HEM B 802 FE B 803 CYN B 805
SITE 1 AC5 6 GLU B 211 HIS B 258 HIS B 259 HEM B 802
SITE 2 AC5 6 FE B 803 CYN B 804
SITE 1 AC6 4 TYR B 337 MET B 417 10M B 807 HOH B 937
SITE 1 AC7 9 LEU B 270 TRP B 271 SER B 274 TYR B 336
SITE 2 AC7 9 TYR B 337 10M B 806 ASN C 138 GLN C 139
SITE 3 AC7 9 PRO C 142
SITE 1 AC8 7 ARG B 57 GLU B 135 HEM B 801 HEM B 802
SITE 2 AC8 7 HOH B 905 GLY C 71 TYR C 73
SITE 1 AC9 17 MET B 427 CYS C 61 CYS C 64 HIS C 65
SITE 2 AC9 17 ALA C 75 PRO C 76 LEU C 78 ARG C 84
SITE 3 AC9 17 ARG C 85 TRP C 98 ARG C 109 ARG C 110
SITE 4 AC9 17 MET C 112 PRO C 113 LEU C 125 HOH C 311
SITE 5 AC9 17 HOH C 313
CRYST1 90.688 107.381 195.288 90.00 90.00 90.00 P 21 21 21 4
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 0.011027 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005121 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
