HEADER ELECTRON TRANSPORT 19-MAR-14 4PWA
TITLE CRYSTAL STRUCTURE OF THE C-TYPE CYTOCHROME SORU FROM SINORHIZOBIUM
TITLE 2 MELILOTI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE CYTOCHROME C;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 28-113;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI;
SOURCE 3 ORGANISM_COMMON: ENSIFER MELILOTI;
SOURCE 4 ORGANISM_TAXID: 266834;
SOURCE 5 STRAIN: 1021;
SOURCE 6 GENE: R02831, SMC04048;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-SMC04048TAG
KEYWDS C-TYPE CYTOCHROME, HEME, ELECTRON TRANSPORT, ELECTRON TRANSFER
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.LAMING,A.P.MCGRATH,M.J.MAHER
REVDAT 4 20-SEP-23 4PWA 1 REMARK SEQADV LINK
REVDAT 3 15-FEB-17 4PWA 1 JRNL
REVDAT 2 17-FEB-16 4PWA 1 JRNL
REVDAT 1 03-JUN-15 4PWA 0
JRNL AUTH A.P.MCGRATH,E.L.LAMING,G.P.CASAS GARCIA,M.KVANSAKUL,
JRNL AUTH 2 J.M.GUSS,J.TREWHELLA,B.CALMES,P.V.BERNHARDT,G.R.HANSON,
JRNL AUTH 3 U.KAPPLER,M.J.MAHER
JRNL TITL STRUCTURAL BASIS OF INTERPROTEIN ELECTRON TRANSFER IN
JRNL TITL 2 BACTERIAL SULFITE OXIDATION.
JRNL REF ELIFE V. 4 09066 2015
JRNL REFN ESSN 2050-084X
JRNL PMID 26687009
JRNL DOI 10.7554/ELIFE.09066
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 23314
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1201
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.24
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1431
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2528
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 172
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.09000
REMARK 3 B22 (A**2) : -1.64000
REMARK 3 B33 (A**2) : -2.45000
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): 0.220
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.151
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.012
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2780 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1724 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3831 ; 1.242 ; 2.186
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4263 ; 0.880 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 344 ; 5.739 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;41.660 ;26.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;15.129 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;12.795 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 422 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3138 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 430 ; 0.001 ; 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): 1718 ; 0.449 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 690 ; 0.099 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2750 ; 0.874 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1062 ; 1.460 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1079 ; 2.406 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : C B A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 C (A): 477 ; 0.340 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 477 ; 0.150 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 A (A): 477 ; 0.180 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 477 ; 0.340 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 C (A): 449 ; 0.570 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 449 ; 0.430 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 A (A): 449 ; 0.490 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 449 ; 0.520 ; 5.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 477 ; 0.330 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 477 ; 0.400 ; 2.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 477 ; 0.330 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 477 ; 0.340 ; 2.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 449 ; 0.360 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 449 ; 0.420 ;10.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 449 ; 0.470 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 449 ; 0.430 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 : A 29 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4713 48.9268 13.7077
REMARK 3 T TENSOR
REMARK 3 T11: 0.1225 T22: 0.0763
REMARK 3 T33: 0.0542 T12: -0.0619
REMARK 3 T13: -0.0476 T23: 0.0360
REMARK 3 L TENSOR
REMARK 3 L11: 2.2658 L22: 2.8184
REMARK 3 L33: 3.7411 L12: -1.1094
REMARK 3 L13: 0.2696 L23: -1.1876
REMARK 3 S TENSOR
REMARK 3 S11: 0.0749 S12: -0.1467 S13: -0.3082
REMARK 3 S21: -0.1152 S22: 0.0201 S23: 0.1756
REMARK 3 S31: 0.1169 S32: -0.2358 S33: -0.0950
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 : B 29 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5743 37.2837 35.9155
REMARK 3 T TENSOR
REMARK 3 T11: 0.0832 T22: 0.0494
REMARK 3 T33: 0.0230 T12: -0.0134
REMARK 3 T13: -0.0175 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 2.8699 L22: 3.6101
REMARK 3 L33: 5.4439 L12: 0.5371
REMARK 3 L13: 0.7704 L23: -0.9827
REMARK 3 S TENSOR
REMARK 3 S11: 0.0022 S12: 0.0945 S13: 0.0198
REMARK 3 S21: -0.1968 S22: 0.0551 S23: 0.1942
REMARK 3 S31: 0.3168 S32: -0.1927 S33: -0.0572
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 27 C 111
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8829 54.7293 12.9617
REMARK 3 T TENSOR
REMARK 3 T11: 0.0891 T22: 0.0474
REMARK 3 T33: 0.0494 T12: -0.0179
REMARK 3 T13: -0.0500 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 3.9559 L22: 4.6084
REMARK 3 L33: 5.2782 L12: 1.1956
REMARK 3 L13: 0.9640 L23: -0.0818
REMARK 3 S TENSOR
REMARK 3 S11: 0.3005 S12: -0.1986 S13: -0.3723
REMARK 3 S21: 0.1277 S22: -0.2048 S23: -0.2581
REMARK 3 S31: 0.3682 S32: 0.1785 S33: -0.0957
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 : D 28 D 114
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7051 51.1443 36.1340
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.0441
REMARK 3 T33: 0.0563 T12: -0.0383
REMARK 3 T13: -0.0022 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 5.0582 L22: 3.7186
REMARK 3 L33: 4.3179 L12: -0.7566
REMARK 3 L13: -0.5233 L23: -1.5179
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: 0.4102 S13: 0.4528
REMARK 3 S21: -0.2432 S22: -0.0352 S23: -0.2743
REMARK 3 S31: -0.1504 S32: 0.0549 S33: 0.0028
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4PWA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000085298.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.954
REMARK 200 MONOCHROMATOR : SI VORTEX ES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23434
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.13300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.79600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4PW9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M TRI-SODIUM CITRATE PH 5.5, 0.1M
REMARK 280 GLYCINE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 64.66350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 98.52950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 64.66350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 98.52950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 64.66350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 98.52950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 64.66350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 98.52950
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 98.52950
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 98.52950
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 98.52950
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 98.52950
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 64.66350
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 64.66350
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 64.66350
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 35.47450
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 64.66350
REMARK 290 SMTRY3 16 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 129.32700
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 8810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 35.47450
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 64.66350
REMARK 350 BIOMT3 2 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 A 27
REMARK 465 GLU A 28
REMARK 465 SER A 115
REMARK 465 SER A 116
REMARK 465 SER A 117
REMARK 465 VAL A 118
REMARK 465 ASP A 119
REMARK 465 LYS A 120
REMARK 465 LEU A 121
REMARK 465 ALA A 122
REMARK 465 ALA A 123
REMARK 465 ALA A 124
REMARK 465 LEU A 125
REMARK 465 GLU A 126
REMARK 465 HIS A 127
REMARK 465 HIS A 128
REMARK 465 HIS A 129
REMARK 465 HIS A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 MET B 27
REMARK 465 GLU B 28
REMARK 465 SER B 115
REMARK 465 SER B 116
REMARK 465 SER B 117
REMARK 465 VAL B 118
REMARK 465 ASP B 119
REMARK 465 LYS B 120
REMARK 465 LEU B 121
REMARK 465 ALA B 122
REMARK 465 ALA B 123
REMARK 465 ALA B 124
REMARK 465 LEU B 125
REMARK 465 GLU B 126
REMARK 465 HIS B 127
REMARK 465 HIS B 128
REMARK 465 HIS B 129
REMARK 465 HIS B 130
REMARK 465 HIS B 131
REMARK 465 HIS B 132
REMARK 465 ALA C 112
REMARK 465 LYS C 113
REMARK 465 ASN C 114
REMARK 465 SER C 115
REMARK 465 SER C 116
REMARK 465 SER C 117
REMARK 465 VAL C 118
REMARK 465 ASP C 119
REMARK 465 LYS C 120
REMARK 465 LEU C 121
REMARK 465 ALA C 122
REMARK 465 ALA C 123
REMARK 465 ALA C 124
REMARK 465 LEU C 125
REMARK 465 GLU C 126
REMARK 465 HIS C 127
REMARK 465 HIS C 128
REMARK 465 HIS C 129
REMARK 465 HIS C 130
REMARK 465 HIS C 131
REMARK 465 HIS C 132
REMARK 465 MET D 27
REMARK 465 SER D 115
REMARK 465 SER D 116
REMARK 465 SER D 117
REMARK 465 VAL D 118
REMARK 465 ASP D 119
REMARK 465 LYS D 120
REMARK 465 LEU D 121
REMARK 465 ALA D 122
REMARK 465 ALA D 123
REMARK 465 ALA D 124
REMARK 465 LEU D 125
REMARK 465 GLU D 126
REMARK 465 HIS D 127
REMARK 465 HIS D 128
REMARK 465 HIS D 129
REMARK 465 HIS D 130
REMARK 465 HIS D 131
REMARK 465 HIS D 132
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 29 CG CD OE1 OE2
REMARK 470 ASP A 30 CG OD1 OD2
REMARK 470 LYS A 31 CG CD CE NZ
REMARK 470 ASN B 114 CG OD1 ND2
REMARK 470 ARG D 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 91 CG CD OE1 OE2
REMARK 470 GLU D 96 CG CD OE1 OE2
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 GLU A 41 -51.17 -125.11
REMARK 500 GLU A 41 -52.32 -124.57
REMARK 500 GLU B 41 -49.22 -139.89
REMARK 500 GLU C 41 -47.87 -135.14
REMARK 500 GLU D 41 -45.34 -148.03
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 HEC A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 51 NE2
REMARK 620 2 HEC A 201 NA 90.1
REMARK 620 3 HEC A 201 NB 88.3 90.8
REMARK 620 4 HEC A 201 NC 87.1 177.2 89.3
REMARK 620 5 HEC A 201 ND 88.7 89.7 177.0 90.1
REMARK 620 6 MET A 87 SD 170.1 83.6 99.4 99.1 83.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 51 NE2
REMARK 620 2 HEC B 201 NA 87.2
REMARK 620 3 HEC B 201 NB 86.8 88.6
REMARK 620 4 HEC B 201 NC 90.9 178.1 91.2
REMARK 620 5 HEC B 201 ND 91.4 91.2 178.2 89.0
REMARK 620 6 MET B 87 SD 169.5 82.3 93.7 99.5 88.0
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 51 NE2
REMARK 620 2 HEC C 201 NA 88.0
REMARK 620 3 HEC C 201 NB 89.1 89.6
REMARK 620 4 HEC C 201 NC 90.7 178.5 91.2
REMARK 620 5 HEC C 201 ND 90.1 91.1 178.9 88.1
REMARK 620 6 MET C 87 SD 170.4 83.1 94.5 98.2 86.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 51 NE2
REMARK 620 2 HEC D 201 NA 90.6
REMARK 620 3 HEC D 201 NB 91.0 90.0
REMARK 620 4 HEC D 201 NC 87.9 178.5 89.5
REMARK 620 5 HEC D 201 ND 88.5 91.4 178.5 89.1
REMARK 620 6 MET D 87 SD 172.4 83.5 93.8 98.0 86.9
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 HEC A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PW9 RELATED DB: PDB
REMARK 900 RELATED ID: 4PW3 RELATED DB: PDB
DBREF 4PWA A 28 113 UNP Q92M25 Q92M25_RHIME 28 113
DBREF 4PWA B 28 113 UNP Q92M25 Q92M25_RHIME 28 113
DBREF 4PWA C 28 113 UNP Q92M25 Q92M25_RHIME 28 113
DBREF 4PWA D 28 113 UNP Q92M25 Q92M25_RHIME 28 113
SEQADV 4PWA MET A 27 UNP Q92M25 INITIATING METHIONINE
SEQADV 4PWA ASN A 114 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER A 115 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER A 116 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER A 117 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA VAL A 118 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ASP A 119 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LYS A 120 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU A 121 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA A 122 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA A 123 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA A 124 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU A 125 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA GLU A 126 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS A 127 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS A 128 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS A 129 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS A 130 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS A 131 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS A 132 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA MET B 27 UNP Q92M25 INITIATING METHIONINE
SEQADV 4PWA ASN B 114 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER B 115 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER B 116 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER B 117 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA VAL B 118 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ASP B 119 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LYS B 120 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU B 121 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA B 122 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA B 123 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA B 124 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU B 125 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA GLU B 126 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS B 127 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS B 128 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS B 129 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS B 130 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS B 131 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS B 132 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA MET C 27 UNP Q92M25 INITIATING METHIONINE
SEQADV 4PWA ASN C 114 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER C 115 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER C 116 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER C 117 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA VAL C 118 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ASP C 119 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LYS C 120 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU C 121 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA C 122 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA C 123 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA C 124 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU C 125 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA GLU C 126 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS C 127 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS C 128 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS C 129 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS C 130 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS C 131 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS C 132 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA MET D 27 UNP Q92M25 INITIATING METHIONINE
SEQADV 4PWA ASN D 114 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER D 115 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER D 116 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA SER D 117 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA VAL D 118 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ASP D 119 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LYS D 120 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU D 121 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA D 122 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA D 123 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA ALA D 124 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA LEU D 125 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA GLU D 126 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS D 127 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS D 128 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS D 129 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS D 130 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS D 131 UNP Q92M25 EXPRESSION TAG
SEQADV 4PWA HIS D 132 UNP Q92M25 EXPRESSION TAG
SEQRES 1 A 106 MET GLU GLU ASP LYS LEU ALA LEU GLY ARG GLU ILE PHE
SEQRES 2 A 106 LEU GLU ARG SER GLU PRO GLN CYS ALA LEU CYS HIS THR
SEQRES 3 A 106 LEU ALA ASP ALA GLU ALA VAL GLY GLU VAL GLY PRO ASN
SEQRES 4 A 106 LEU ASP GLU LEU LYS PRO ASP ALA GLU ARG VAL ASN THR
SEQRES 5 A 106 ALA VAL THR ASN GLY ILE GLY PRO MET PRO ALA ASN GLU
SEQRES 6 A 106 ILE LEU THR ASP GLU GLU ILE GLU ALA VAL ALA LEU TYR
SEQRES 7 A 106 VAL SER THR VAL ALA GLY LYS ALA LYS ASN SER SER SER
SEQRES 8 A 106 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 9 A 106 HIS HIS
SEQRES 1 B 106 MET GLU GLU ASP LYS LEU ALA LEU GLY ARG GLU ILE PHE
SEQRES 2 B 106 LEU GLU ARG SER GLU PRO GLN CYS ALA LEU CYS HIS THR
SEQRES 3 B 106 LEU ALA ASP ALA GLU ALA VAL GLY GLU VAL GLY PRO ASN
SEQRES 4 B 106 LEU ASP GLU LEU LYS PRO ASP ALA GLU ARG VAL ASN THR
SEQRES 5 B 106 ALA VAL THR ASN GLY ILE GLY PRO MET PRO ALA ASN GLU
SEQRES 6 B 106 ILE LEU THR ASP GLU GLU ILE GLU ALA VAL ALA LEU TYR
SEQRES 7 B 106 VAL SER THR VAL ALA GLY LYS ALA LYS ASN SER SER SER
SEQRES 8 B 106 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 9 B 106 HIS HIS
SEQRES 1 C 106 MET GLU GLU ASP LYS LEU ALA LEU GLY ARG GLU ILE PHE
SEQRES 2 C 106 LEU GLU ARG SER GLU PRO GLN CYS ALA LEU CYS HIS THR
SEQRES 3 C 106 LEU ALA ASP ALA GLU ALA VAL GLY GLU VAL GLY PRO ASN
SEQRES 4 C 106 LEU ASP GLU LEU LYS PRO ASP ALA GLU ARG VAL ASN THR
SEQRES 5 C 106 ALA VAL THR ASN GLY ILE GLY PRO MET PRO ALA ASN GLU
SEQRES 6 C 106 ILE LEU THR ASP GLU GLU ILE GLU ALA VAL ALA LEU TYR
SEQRES 7 C 106 VAL SER THR VAL ALA GLY LYS ALA LYS ASN SER SER SER
SEQRES 8 C 106 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 9 C 106 HIS HIS
SEQRES 1 D 106 MET GLU GLU ASP LYS LEU ALA LEU GLY ARG GLU ILE PHE
SEQRES 2 D 106 LEU GLU ARG SER GLU PRO GLN CYS ALA LEU CYS HIS THR
SEQRES 3 D 106 LEU ALA ASP ALA GLU ALA VAL GLY GLU VAL GLY PRO ASN
SEQRES 4 D 106 LEU ASP GLU LEU LYS PRO ASP ALA GLU ARG VAL ASN THR
SEQRES 5 D 106 ALA VAL THR ASN GLY ILE GLY PRO MET PRO ALA ASN GLU
SEQRES 6 D 106 ILE LEU THR ASP GLU GLU ILE GLU ALA VAL ALA LEU TYR
SEQRES 7 D 106 VAL SER THR VAL ALA GLY LYS ALA LYS ASN SER SER SER
SEQRES 8 D 106 VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS
SEQRES 9 D 106 HIS HIS
HET HEC A 201 43
HET HEC B 201 43
HET HEC C 201 43
HET HEC D 201 43
HETNAM HEC HEME C
FORMUL 5 HEC 4(C34 H34 FE N4 O4)
FORMUL 9 HOH *227(H2 O)
HELIX 1 1 GLU A 29 GLU A 41 1 13
HELIX 2 2 GLN A 46 HIS A 51 1 6
HELIX 3 3 ALA A 54 GLU A 57 5 4
HELIX 4 4 ASN A 65 LYS A 70 1 6
HELIX 5 5 ASP A 72 GLY A 83 1 12
HELIX 6 6 THR A 94 ALA A 109 1 16
HELIX 7 7 ASP B 30 GLU B 41 1 12
HELIX 8 8 GLN B 46 HIS B 51 1 6
HELIX 9 9 ALA B 54 GLU B 57 5 4
HELIX 10 10 ASN B 65 LYS B 70 1 6
HELIX 11 11 ASP B 72 GLY B 83 1 12
HELIX 12 12 THR B 94 ALA B 109 1 16
HELIX 13 13 GLU C 28 GLU C 41 1 14
HELIX 14 14 GLN C 46 HIS C 51 1 6
HELIX 15 15 ALA C 54 GLU C 57 5 4
HELIX 16 16 ASN C 65 LYS C 70 1 6
HELIX 17 17 ASP C 72 GLY C 83 1 12
HELIX 18 18 THR C 94 ALA C 109 1 16
HELIX 19 19 GLU D 29 GLU D 41 1 13
HELIX 20 20 GLN D 46 HIS D 51 1 6
HELIX 21 21 ALA D 54 GLU D 57 5 4
HELIX 22 22 ASN D 65 LYS D 70 1 6
HELIX 23 23 ASP D 72 GLY D 83 1 12
HELIX 24 24 THR D 94 ALA D 109 1 16
SHEET 1 A 2 THR A 52 LEU A 53 0
SHEET 2 A 2 ALA A 58 VAL A 59 -1 O ALA A 58 N LEU A 53
SHEET 1 B 2 THR B 52 LEU B 53 0
SHEET 2 B 2 ALA B 58 VAL B 59 -1 O ALA B 58 N LEU B 53
SHEET 1 C 2 THR C 52 LEU C 53 0
SHEET 2 C 2 ALA C 58 VAL C 59 -1 O ALA C 58 N LEU C 53
SHEET 1 D 2 THR D 52 LEU D 53 0
SHEET 2 D 2 ALA D 58 VAL D 59 -1 O ALA D 58 N LEU D 53
LINK SG CYS A 47 CAB HEC A 201 1555 1555 1.79
LINK SG CYS A 50 CAC HEC A 201 1555 1555 1.87
LINK SG CYS B 47 CAB HEC B 201 1555 1555 1.81
LINK SG CYS B 50 CAC HEC B 201 1555 1555 1.86
LINK SG CYS C 47 CAB HEC C 201 1555 1555 1.80
LINK SG CYS C 50 CAC HEC C 201 1555 1555 1.86
LINK SG CYS D 47 CAB HEC D 201 1555 1555 1.80
LINK SG CYS D 50 CAC HEC D 201 1555 1555 1.88
LINK NE2 HIS A 51 FE HEC A 201 1555 1555 2.02
LINK SD MET A 87 FE HEC A 201 1555 1555 2.40
LINK NE2 HIS B 51 FE HEC B 201 1555 1555 2.01
LINK SD MET B 87 FE HEC B 201 1555 1555 2.39
LINK NE2 HIS C 51 FE HEC C 201 1555 1555 1.93
LINK SD MET C 87 FE HEC C 201 1555 1555 2.29
LINK NE2 HIS D 51 FE HEC D 201 1555 1555 2.00
LINK SD MET D 87 FE HEC D 201 1555 1555 2.30
CISPEP 1 GLU A 44 PRO A 45 0 -9.19
CISPEP 2 GLU B 44 PRO B 45 0 -10.12
CISPEP 3 GLU C 44 PRO C 45 0 -6.54
CISPEP 4 GLU D 44 PRO D 45 0 -7.47
SITE 1 AC1 16 PRO A 45 CYS A 47 CYS A 50 HIS A 51
SITE 2 AC1 16 PRO A 64 LEU A 69 ARG A 75 VAL A 80
SITE 3 AC1 16 ILE A 84 GLY A 85 PRO A 86 MET A 87
SITE 4 AC1 16 HOH A 307 HOH A 313 HOH A 366 HOH C 318
SITE 1 AC2 18 GLN B 46 CYS B 47 CYS B 50 HIS B 51
SITE 2 AC2 18 GLY B 63 PRO B 64 LEU B 69 ARG B 75
SITE 3 AC2 18 VAL B 76 VAL B 80 ILE B 84 PRO B 86
SITE 4 AC2 18 MET B 87 HOH B 305 HOH B 309 HOH B 327
SITE 5 AC2 18 HEC D 201 HOH D 328
SITE 1 AC3 18 HOH A 310 PRO C 45 GLN C 46 CYS C 47
SITE 2 AC3 18 CYS C 50 HIS C 51 PRO C 64 LEU C 69
SITE 3 AC3 18 ARG C 75 VAL C 80 ILE C 84 GLY C 85
SITE 4 AC3 18 PRO C 86 MET C 87 HOH C 309 HOH C 313
SITE 5 AC3 18 HOH C 322 HOH C 351
SITE 1 AC4 21 HEC B 201 PRO D 45 CYS D 47 CYS D 50
SITE 2 AC4 21 HIS D 51 GLY D 63 PRO D 64 GLU D 68
SITE 3 AC4 21 LEU D 69 ARG D 75 VAL D 76 VAL D 80
SITE 4 AC4 21 ILE D 84 GLY D 85 PRO D 86 MET D 87
SITE 5 AC4 21 HOH D 305 HOH D 307 HOH D 308 HOH D 321
SITE 6 AC4 21 HOH D 343
CRYST1 70.949 129.327 197.059 90.00 90.00 90.00 F 2 2 2 64
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 0.014095 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007732 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005075 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
