HEADER METAL BINDING PROTEIN 12-JAN-11 3QB9
TITLE MYCOBACTERIUM TUBERCULOSIS BACTERIOFERRITIN, BFRA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIOFERRITIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: BFR;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: BFR, BFRA, MT1925, MTCY180.42C, RV1876;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B+
KEYWDS CYTOSOL, STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 2 TBSGC, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.MCMATH,C.W.GOULDING,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 2 21-FEB-24 3QB9 1 REMARK SEQADV LINK
REVDAT 1 08-FEB-12 3QB9 0
JRNL AUTH L.M.MCMATH,C.W.GOULDING
JRNL TITL MYCOBACTERIUM TUBERCULOSIS BACTERIOFERRITIN, BFRA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 75688
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.090
REMARK 3 FREE R VALUE TEST SET COUNT : 7640
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 39.3275 - 6.5414 0.98 2258 284 0.1664 0.1944
REMARK 3 2 6.5414 - 5.1959 1.00 2312 266 0.1705 0.2301
REMARK 3 3 5.1959 - 4.5402 1.00 2305 267 0.1253 0.1903
REMARK 3 4 4.5402 - 4.1256 1.00 2275 255 0.1138 0.1598
REMARK 3 5 4.1256 - 3.8302 1.00 2281 279 0.1264 0.1846
REMARK 3 6 3.8302 - 3.6045 1.00 2290 242 0.1316 0.1797
REMARK 3 7 3.6045 - 3.4241 1.00 2303 232 0.1361 0.1991
REMARK 3 8 3.4241 - 3.2751 1.00 2272 250 0.1483 0.2368
REMARK 3 9 3.2751 - 3.1491 0.99 2308 254 0.1571 0.2416
REMARK 3 10 3.1491 - 3.0405 1.00 2255 241 0.1711 0.2249
REMARK 3 11 3.0405 - 2.9454 1.00 2279 264 0.1839 0.2578
REMARK 3 12 2.9454 - 2.8613 1.00 2286 256 0.1840 0.2586
REMARK 3 13 2.8613 - 2.7860 1.00 2286 247 0.2017 0.2706
REMARK 3 14 2.7860 - 2.7180 1.00 2306 240 0.1950 0.2520
REMARK 3 15 2.7180 - 2.6562 1.00 2279 251 0.2033 0.2667
REMARK 3 16 2.6562 - 2.5997 0.99 2290 251 0.2163 0.2869
REMARK 3 17 2.5997 - 2.5477 1.00 2259 250 0.2100 0.2843
REMARK 3 18 2.5477 - 2.4997 1.00 2295 261 0.2083 0.2808
REMARK 3 19 2.4997 - 2.4550 1.00 2248 274 0.2170 0.2762
REMARK 3 20 2.4550 - 2.4134 1.00 2235 293 0.2057 0.2792
REMARK 3 21 2.4134 - 2.3745 1.00 2271 243 0.2214 0.3330
REMARK 3 22 2.3745 - 2.3380 1.00 2241 261 0.2290 0.2862
REMARK 3 23 2.3380 - 2.3036 1.00 2285 264 0.2293 0.3017
REMARK 3 24 2.3036 - 2.2711 1.00 2311 234 0.2578 0.3385
REMARK 3 25 2.2711 - 2.2404 0.99 2268 247 0.2888 0.3202
REMARK 3 26 2.2404 - 2.2114 0.99 2249 247 0.2824 0.3272
REMARK 3 27 2.2114 - 2.1837 1.00 2298 263 0.2900 0.3096
REMARK 3 28 2.1837 - 2.1574 1.00 2282 232 0.3137 0.3452
REMARK 3 29 2.1574 - 2.1323 1.00 2237 263 0.3379 0.3853
REMARK 3 30 2.1323 - 2.1084 0.88 1984 229 0.3655 0.3874
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 39.94
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.620
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.620
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) : 3.37300
REMARK 3 B22 (A**2) : 3.37300
REMARK 3 B33 (A**2) : -6.74610
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7974
REMARK 3 ANGLE : 0.982 10824
REMARK 3 CHIRALITY : 0.060 1200
REMARK 3 PLANARITY : 0.004 1416
REMARK 3 DIHEDRAL : 14.740 3030
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -34.3994 -40.8286 -1.1453
REMARK 3 T TENSOR
REMARK 3 T11: 0.1849 T22: 0.2193
REMARK 3 T33: 0.2488 T12: -0.0530
REMARK 3 T13: 0.0114 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.1540 L22: 0.1486
REMARK 3 L33: 0.2993 L12: -0.0299
REMARK 3 L13: -0.0853 L23: -0.0362
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: 0.0142 S13: 0.1038
REMARK 3 S21: -0.0282 S22: -0.0103 S23: -0.1007
REMARK 3 S31: -0.0715 S32: 0.0829 S33: 0.0020
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:159 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 1:159 )
REMARK 3 ATOM PAIRS NUMBER : 1285
REMARK 3 RMSD : 0.038
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:159 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 1:159 )
REMARK 3 ATOM PAIRS NUMBER : 1285
REMARK 3 RMSD : 0.037
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:159 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 1:159 )
REMARK 3 ATOM PAIRS NUMBER : 1285
REMARK 3 RMSD : 0.038
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:159 )
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 1:159 )
REMARK 3 ATOM PAIRS NUMBER : 1285
REMARK 3 RMSD : 0.038
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:159 )
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 1:159 )
REMARK 3 ATOM PAIRS NUMBER : 1285
REMARK 3 RMSD : 0.036
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QB9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063426.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0972109
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL; ASYMMETRIC CUT
REMARK 200 4.9650 DEG
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75962
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110
REMARK 200 RESOLUTION RANGE LOW (A) : 39.321
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3030
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M NACL, 100 MM TRIS-HCL (PH 8.0),
REMARK 280 25 MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 62.17150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.17150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 87.48800
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 62.17150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.17150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 87.48800
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 62.17150
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 62.17150
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 87.48800
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 62.17150
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 62.17150
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 87.48800
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: 24-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 92330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 123070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -527.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 -124.34300
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -124.34300
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -124.34300
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -124.34300
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 464 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 483 LIES ON A SPECIAL POSITION.
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 -1
REMARK 465 GLY A 0
REMARK 465 LYS A 160
REMARK 465 LEU A 161
REMARK 465 ALA A 162
REMARK 465 ALA A 163
REMARK 465 ALA A 164
REMARK 465 LEU A 165
REMARK 465 GLU A 166
REMARK 465 HIS A 167
REMARK 465 HIS A 168
REMARK 465 HIS A 169
REMARK 465 HIS A 170
REMARK 465 HIS A 171
REMARK 465 HIS A 172
REMARK 465 MET B -1
REMARK 465 GLY B 0
REMARK 465 LYS B 160
REMARK 465 LEU B 161
REMARK 465 ALA B 162
REMARK 465 ALA B 163
REMARK 465 ALA B 164
REMARK 465 LEU B 165
REMARK 465 GLU B 166
REMARK 465 HIS B 167
REMARK 465 HIS B 168
REMARK 465 HIS B 169
REMARK 465 HIS B 170
REMARK 465 HIS B 171
REMARK 465 HIS B 172
REMARK 465 MET C -1
REMARK 465 GLY C 0
REMARK 465 LYS C 160
REMARK 465 LEU C 161
REMARK 465 ALA C 162
REMARK 465 ALA C 163
REMARK 465 ALA C 164
REMARK 465 LEU C 165
REMARK 465 GLU C 166
REMARK 465 HIS C 167
REMARK 465 HIS C 168
REMARK 465 HIS C 169
REMARK 465 HIS C 170
REMARK 465 HIS C 171
REMARK 465 HIS C 172
REMARK 465 MET D -1
REMARK 465 GLY D 0
REMARK 465 LYS D 160
REMARK 465 LEU D 161
REMARK 465 ALA D 162
REMARK 465 ALA D 163
REMARK 465 ALA D 164
REMARK 465 LEU D 165
REMARK 465 GLU D 166
REMARK 465 HIS D 167
REMARK 465 HIS D 168
REMARK 465 HIS D 169
REMARK 465 HIS D 170
REMARK 465 HIS D 171
REMARK 465 HIS D 172
REMARK 465 MET E -1
REMARK 465 GLY E 0
REMARK 465 LYS E 160
REMARK 465 LEU E 161
REMARK 465 ALA E 162
REMARK 465 ALA E 163
REMARK 465 ALA E 164
REMARK 465 LEU E 165
REMARK 465 GLU E 166
REMARK 465 HIS E 167
REMARK 465 HIS E 168
REMARK 465 HIS E 169
REMARK 465 HIS E 170
REMARK 465 HIS E 171
REMARK 465 HIS E 172
REMARK 465 MET F -1
REMARK 465 GLY F 0
REMARK 465 LYS F 160
REMARK 465 LEU F 161
REMARK 465 ALA F 162
REMARK 465 ALA F 163
REMARK 465 ALA F 164
REMARK 465 LEU F 165
REMARK 465 GLU F 166
REMARK 465 HIS F 167
REMARK 465 HIS F 168
REMARK 465 HIS F 169
REMARK 465 HIS F 170
REMARK 465 HIS F 171
REMARK 465 HIS F 172
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 ASP C 113 79.54 -109.69
REMARK 500 ASP F 113 79.75 -107.05
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 FE A 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 18 OE1
REMARK 620 2 GLU A 51 OE1 55.7
REMARK 620 3 HIS A 54 ND1 98.6 120.2
REMARK 620 4 GLU A 127 OE2 151.9 114.3 108.0
REMARK 620 5 HOH A 509 O 78.8 100.5 128.8 77.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 51 OE2
REMARK 620 2 GLU A 94 OE2 124.4
REMARK 620 3 GLU A 127 OE2 89.1 86.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 52 SD
REMARK 620 2 HEM B 301 NA 97.0
REMARK 620 3 HEM B 301 NB 110.7 86.8
REMARK 620 4 HEM B 301 NC 83.4 178.2 91.4
REMARK 620 5 HEM B 301 ND 74.4 92.5 174.9 89.3
REMARK 620 6 MET B 52 SD 156.6 75.3 91.2 105.0 83.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 18 OE1
REMARK 620 2 GLU B 51 OE1 60.5
REMARK 620 3 HIS B 54 ND1 106.0 108.8
REMARK 620 4 GLU B 127 OE2 149.8 121.1 101.6
REMARK 620 5 HOH B 521 O 79.9 74.5 174.1 72.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 51 OE2
REMARK 620 2 GLU B 127 OE2 95.9
REMARK 620 3 GLU B 127 OE1 124.6 48.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 18 OE1
REMARK 620 2 GLU C 51 OE1 66.7
REMARK 620 3 GLU C 51 OE2 102.2 51.6
REMARK 620 4 HIS C 54 ND1 112.1 147.8 100.5
REMARK 620 5 GLU C 127 OE2 142.3 91.0 84.3 102.9
REMARK 620 6 HOH C 520 O 83.6 59.6 99.0 151.5 58.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 51 OE2
REMARK 620 2 GLU C 94 OE2 149.3
REMARK 620 3 GLU C 127 OE2 79.4 103.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET C 52 SD
REMARK 620 2 HEM C 301 NA 73.5
REMARK 620 3 HEM C 301 NB 90.7 86.9
REMARK 620 4 HEM C 301 NC 108.4 177.4 91.3
REMARK 620 5 HEM C 301 ND 83.2 93.2 173.6 88.8
REMARK 620 6 MET D 52 SD 148.5 88.7 114.5 90.4 71.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 18 OE1
REMARK 620 2 GLU D 51 OE1 63.7
REMARK 620 3 HIS D 54 ND1 99.8 124.3
REMARK 620 4 GLU D 127 OE2 127.4 106.3 122.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 51 OE2
REMARK 620 2 GLU D 127 OE1 96.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE E 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 18 OE1
REMARK 620 2 GLU E 18 OE2 51.6
REMARK 620 3 GLU E 51 OE1 57.9 108.1
REMARK 620 4 GLU E 127 OE2 162.8 134.1 117.4
REMARK 620 5 HOH E 507 O 99.5 117.4 84.6 63.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE E 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 51 OE2
REMARK 620 2 GLU E 94 OE2 105.7
REMARK 620 3 GLU E 127 OE2 86.8 102.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET E 52 SD
REMARK 620 2 HEM E 301 NA 89.6
REMARK 620 3 HEM E 301 NB 89.6 89.2
REMARK 620 4 HEM E 301 NC 85.7 175.1 89.3
REMARK 620 5 HEM E 301 ND 79.5 91.1 169.0 89.5
REMARK 620 6 MET F 52 SD 147.7 118.9 104.6 66.0 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE F 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 18 OE1
REMARK 620 2 GLU F 51 OE1 60.6
REMARK 620 3 HIS F 54 ND1 103.2 107.7
REMARK 620 4 GLU F 127 OE2 139.0 126.7 109.9
REMARK 620 5 HOH F 516 O 80.5 115.8 130.9 59.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE F 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 51 OE2
REMARK 620 2 GLU F 94 OE2 95.1
REMARK 620 3 GLU F 127 OE1 116.3 64.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1876 RELATED DB: TARGETDB
DBREF 3QB9 A 1 159 UNP P63697 BFR_MYCTU 1 159
DBREF 3QB9 B 1 159 UNP P63697 BFR_MYCTU 1 159
DBREF 3QB9 C 1 159 UNP P63697 BFR_MYCTU 1 159
DBREF 3QB9 D 1 159 UNP P63697 BFR_MYCTU 1 159
DBREF 3QB9 E 1 159 UNP P63697 BFR_MYCTU 1 159
DBREF 3QB9 F 1 159 UNP P63697 BFR_MYCTU 1 159
SEQADV 3QB9 MET A -1 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLY A 0 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LYS A 160 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU A 161 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA A 162 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA A 163 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA A 164 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU A 165 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLU A 166 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS A 167 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS A 168 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS A 169 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS A 170 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS A 171 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS A 172 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 MET B -1 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLY B 0 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LYS B 160 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU B 161 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA B 162 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA B 163 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA B 164 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU B 165 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLU B 166 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS B 167 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS B 168 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS B 169 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS B 170 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS B 171 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS B 172 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 MET C -1 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLY C 0 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LYS C 160 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU C 161 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA C 162 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA C 163 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA C 164 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU C 165 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLU C 166 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS C 167 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS C 168 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS C 169 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS C 170 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS C 171 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS C 172 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 MET D -1 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLY D 0 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LYS D 160 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU D 161 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA D 162 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA D 163 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA D 164 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU D 165 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLU D 166 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS D 167 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS D 168 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS D 169 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS D 170 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS D 171 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS D 172 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 MET E -1 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLY E 0 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LYS E 160 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU E 161 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA E 162 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA E 163 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA E 164 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU E 165 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLU E 166 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS E 167 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS E 168 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS E 169 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS E 170 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS E 171 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS E 172 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 MET F -1 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLY F 0 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LYS F 160 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU F 161 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA F 162 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA F 163 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 ALA F 164 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 LEU F 165 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 GLU F 166 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS F 167 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS F 168 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS F 169 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS F 170 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS F 171 UNP P63697 EXPRESSION TAG
SEQADV 3QB9 HIS F 172 UNP P63697 EXPRESSION TAG
SEQRES 1 A 174 MET GLY MET GLN GLY ASP PRO ASP VAL LEU ARG LEU LEU
SEQRES 2 A 174 ASN GLU GLN LEU THR SER GLU LEU THR ALA ILE ASN GLN
SEQRES 3 A 174 TYR PHE LEU HIS SER LYS MET GLN ASP ASN TRP GLY PHE
SEQRES 4 A 174 THR GLU LEU ALA ALA HIS THR ARG ALA GLU SER PHE ASP
SEQRES 5 A 174 GLU MET ARG HIS ALA GLU GLU ILE THR ASP ARG ILE LEU
SEQRES 6 A 174 LEU LEU ASP GLY LEU PRO ASN TYR GLN ARG ILE GLY SER
SEQRES 7 A 174 LEU ARG ILE GLY GLN THR LEU ARG GLU GLN PHE GLU ALA
SEQRES 8 A 174 ASP LEU ALA ILE GLU TYR ASP VAL LEU ASN ARG LEU LYS
SEQRES 9 A 174 PRO GLY ILE VAL MET CYS ARG GLU LYS GLN ASP THR THR
SEQRES 10 A 174 SER ALA VAL LEU LEU GLU LYS ILE VAL ALA ASP GLU GLU
SEQRES 11 A 174 GLU HIS ILE ASP TYR LEU GLU THR GLN LEU GLU LEU MET
SEQRES 12 A 174 ASP LYS LEU GLY GLU GLU LEU TYR SER ALA GLN CYS VAL
SEQRES 13 A 174 SER ARG PRO PRO THR LYS LEU ALA ALA ALA LEU GLU HIS
SEQRES 14 A 174 HIS HIS HIS HIS HIS
SEQRES 1 B 174 MET GLY MET GLN GLY ASP PRO ASP VAL LEU ARG LEU LEU
SEQRES 2 B 174 ASN GLU GLN LEU THR SER GLU LEU THR ALA ILE ASN GLN
SEQRES 3 B 174 TYR PHE LEU HIS SER LYS MET GLN ASP ASN TRP GLY PHE
SEQRES 4 B 174 THR GLU LEU ALA ALA HIS THR ARG ALA GLU SER PHE ASP
SEQRES 5 B 174 GLU MET ARG HIS ALA GLU GLU ILE THR ASP ARG ILE LEU
SEQRES 6 B 174 LEU LEU ASP GLY LEU PRO ASN TYR GLN ARG ILE GLY SER
SEQRES 7 B 174 LEU ARG ILE GLY GLN THR LEU ARG GLU GLN PHE GLU ALA
SEQRES 8 B 174 ASP LEU ALA ILE GLU TYR ASP VAL LEU ASN ARG LEU LYS
SEQRES 9 B 174 PRO GLY ILE VAL MET CYS ARG GLU LYS GLN ASP THR THR
SEQRES 10 B 174 SER ALA VAL LEU LEU GLU LYS ILE VAL ALA ASP GLU GLU
SEQRES 11 B 174 GLU HIS ILE ASP TYR LEU GLU THR GLN LEU GLU LEU MET
SEQRES 12 B 174 ASP LYS LEU GLY GLU GLU LEU TYR SER ALA GLN CYS VAL
SEQRES 13 B 174 SER ARG PRO PRO THR LYS LEU ALA ALA ALA LEU GLU HIS
SEQRES 14 B 174 HIS HIS HIS HIS HIS
SEQRES 1 C 174 MET GLY MET GLN GLY ASP PRO ASP VAL LEU ARG LEU LEU
SEQRES 2 C 174 ASN GLU GLN LEU THR SER GLU LEU THR ALA ILE ASN GLN
SEQRES 3 C 174 TYR PHE LEU HIS SER LYS MET GLN ASP ASN TRP GLY PHE
SEQRES 4 C 174 THR GLU LEU ALA ALA HIS THR ARG ALA GLU SER PHE ASP
SEQRES 5 C 174 GLU MET ARG HIS ALA GLU GLU ILE THR ASP ARG ILE LEU
SEQRES 6 C 174 LEU LEU ASP GLY LEU PRO ASN TYR GLN ARG ILE GLY SER
SEQRES 7 C 174 LEU ARG ILE GLY GLN THR LEU ARG GLU GLN PHE GLU ALA
SEQRES 8 C 174 ASP LEU ALA ILE GLU TYR ASP VAL LEU ASN ARG LEU LYS
SEQRES 9 C 174 PRO GLY ILE VAL MET CYS ARG GLU LYS GLN ASP THR THR
SEQRES 10 C 174 SER ALA VAL LEU LEU GLU LYS ILE VAL ALA ASP GLU GLU
SEQRES 11 C 174 GLU HIS ILE ASP TYR LEU GLU THR GLN LEU GLU LEU MET
SEQRES 12 C 174 ASP LYS LEU GLY GLU GLU LEU TYR SER ALA GLN CYS VAL
SEQRES 13 C 174 SER ARG PRO PRO THR LYS LEU ALA ALA ALA LEU GLU HIS
SEQRES 14 C 174 HIS HIS HIS HIS HIS
SEQRES 1 D 174 MET GLY MET GLN GLY ASP PRO ASP VAL LEU ARG LEU LEU
SEQRES 2 D 174 ASN GLU GLN LEU THR SER GLU LEU THR ALA ILE ASN GLN
SEQRES 3 D 174 TYR PHE LEU HIS SER LYS MET GLN ASP ASN TRP GLY PHE
SEQRES 4 D 174 THR GLU LEU ALA ALA HIS THR ARG ALA GLU SER PHE ASP
SEQRES 5 D 174 GLU MET ARG HIS ALA GLU GLU ILE THR ASP ARG ILE LEU
SEQRES 6 D 174 LEU LEU ASP GLY LEU PRO ASN TYR GLN ARG ILE GLY SER
SEQRES 7 D 174 LEU ARG ILE GLY GLN THR LEU ARG GLU GLN PHE GLU ALA
SEQRES 8 D 174 ASP LEU ALA ILE GLU TYR ASP VAL LEU ASN ARG LEU LYS
SEQRES 9 D 174 PRO GLY ILE VAL MET CYS ARG GLU LYS GLN ASP THR THR
SEQRES 10 D 174 SER ALA VAL LEU LEU GLU LYS ILE VAL ALA ASP GLU GLU
SEQRES 11 D 174 GLU HIS ILE ASP TYR LEU GLU THR GLN LEU GLU LEU MET
SEQRES 12 D 174 ASP LYS LEU GLY GLU GLU LEU TYR SER ALA GLN CYS VAL
SEQRES 13 D 174 SER ARG PRO PRO THR LYS LEU ALA ALA ALA LEU GLU HIS
SEQRES 14 D 174 HIS HIS HIS HIS HIS
SEQRES 1 E 174 MET GLY MET GLN GLY ASP PRO ASP VAL LEU ARG LEU LEU
SEQRES 2 E 174 ASN GLU GLN LEU THR SER GLU LEU THR ALA ILE ASN GLN
SEQRES 3 E 174 TYR PHE LEU HIS SER LYS MET GLN ASP ASN TRP GLY PHE
SEQRES 4 E 174 THR GLU LEU ALA ALA HIS THR ARG ALA GLU SER PHE ASP
SEQRES 5 E 174 GLU MET ARG HIS ALA GLU GLU ILE THR ASP ARG ILE LEU
SEQRES 6 E 174 LEU LEU ASP GLY LEU PRO ASN TYR GLN ARG ILE GLY SER
SEQRES 7 E 174 LEU ARG ILE GLY GLN THR LEU ARG GLU GLN PHE GLU ALA
SEQRES 8 E 174 ASP LEU ALA ILE GLU TYR ASP VAL LEU ASN ARG LEU LYS
SEQRES 9 E 174 PRO GLY ILE VAL MET CYS ARG GLU LYS GLN ASP THR THR
SEQRES 10 E 174 SER ALA VAL LEU LEU GLU LYS ILE VAL ALA ASP GLU GLU
SEQRES 11 E 174 GLU HIS ILE ASP TYR LEU GLU THR GLN LEU GLU LEU MET
SEQRES 12 E 174 ASP LYS LEU GLY GLU GLU LEU TYR SER ALA GLN CYS VAL
SEQRES 13 E 174 SER ARG PRO PRO THR LYS LEU ALA ALA ALA LEU GLU HIS
SEQRES 14 E 174 HIS HIS HIS HIS HIS
SEQRES 1 F 174 MET GLY MET GLN GLY ASP PRO ASP VAL LEU ARG LEU LEU
SEQRES 2 F 174 ASN GLU GLN LEU THR SER GLU LEU THR ALA ILE ASN GLN
SEQRES 3 F 174 TYR PHE LEU HIS SER LYS MET GLN ASP ASN TRP GLY PHE
SEQRES 4 F 174 THR GLU LEU ALA ALA HIS THR ARG ALA GLU SER PHE ASP
SEQRES 5 F 174 GLU MET ARG HIS ALA GLU GLU ILE THR ASP ARG ILE LEU
SEQRES 6 F 174 LEU LEU ASP GLY LEU PRO ASN TYR GLN ARG ILE GLY SER
SEQRES 7 F 174 LEU ARG ILE GLY GLN THR LEU ARG GLU GLN PHE GLU ALA
SEQRES 8 F 174 ASP LEU ALA ILE GLU TYR ASP VAL LEU ASN ARG LEU LYS
SEQRES 9 F 174 PRO GLY ILE VAL MET CYS ARG GLU LYS GLN ASP THR THR
SEQRES 10 F 174 SER ALA VAL LEU LEU GLU LYS ILE VAL ALA ASP GLU GLU
SEQRES 11 F 174 GLU HIS ILE ASP TYR LEU GLU THR GLN LEU GLU LEU MET
SEQRES 12 F 174 ASP LYS LEU GLY GLU GLU LEU TYR SER ALA GLN CYS VAL
SEQRES 13 F 174 SER ARG PRO PRO THR LYS LEU ALA ALA ALA LEU GLU HIS
SEQRES 14 F 174 HIS HIS HIS HIS HIS
HET FE A 202 1
HET FE A 201 1
HET FE B 201 1
HET FE B 202 1
HET HEM B 301 43
HET NA B 173 1
HET HEM C 301 43
HET FE C 201 1
HET FE C 202 1
HET FE D 201 1
HET FE D 202 1
HET HEM E 301 43
HET FE E 201 1
HET FE E 202 1
HET FE F 201 1
HET FE F 202 1
HETNAM FE FE (III) ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NA SODIUM ION
HETSYN HEM HEME
FORMUL 7 FE 12(FE 3+)
FORMUL 11 HEM 3(C34 H32 FE N4 O4)
FORMUL 12 NA NA 1+
FORMUL 23 HOH *509(H2 O)
HELIX 1 1 ASP A 4 TRP A 35 1 32
HELIX 2 2 PHE A 37 LEU A 65 1 29
HELIX 3 3 THR A 82 LYS A 111 1 30
HELIX 4 4 ASP A 113 GLY A 145 1 33
HELIX 5 5 GLY A 145 GLN A 152 1 8
HELIX 6 6 ASP B 4 GLY B 36 1 33
HELIX 7 7 PHE B 37 LEU B 65 1 29
HELIX 8 8 THR B 82 LYS B 111 1 30
HELIX 9 9 ASP B 113 GLY B 145 1 33
HELIX 10 10 GLY B 145 GLN B 152 1 8
HELIX 11 11 ASP C 4 GLY C 36 1 33
HELIX 12 12 PHE C 37 LEU C 65 1 29
HELIX 13 13 THR C 82 LYS C 111 1 30
HELIX 14 14 ASP C 113 GLY C 145 1 33
HELIX 15 15 GLY C 145 GLN C 152 1 8
HELIX 16 16 ASP D 4 TRP D 35 1 32
HELIX 17 17 PHE D 37 LEU D 65 1 29
HELIX 18 18 THR D 82 LYS D 111 1 30
HELIX 19 19 ASP D 113 GLY D 145 1 33
HELIX 20 20 GLY D 145 GLN D 152 1 8
HELIX 21 21 ASP E 4 GLY E 36 1 33
HELIX 22 22 PHE E 37 LEU E 65 1 29
HELIX 23 23 THR E 82 LYS E 111 1 30
HELIX 24 24 ASP E 113 GLY E 145 1 33
HELIX 25 25 GLY E 145 GLN E 152 1 8
HELIX 26 26 ASP F 4 GLY F 36 1 33
HELIX 27 27 PHE F 37 LEU F 65 1 29
HELIX 28 28 THR F 82 LYS F 111 1 30
HELIX 29 29 ASP F 113 GLY F 145 1 33
HELIX 30 30 GLY F 145 GLN F 152 1 8
LINK OE1 GLU A 18 FE FE A 201 1555 1555 2.67
LINK OE1 GLU A 51 FE FE A 201 1555 1555 2.20
LINK OE2 GLU A 51 FE FE A 202 1555 1555 2.38
LINK SD MET A 52 FE HEM B 301 1555 1555 2.42
LINK ND1 HIS A 54 FE FE A 201 1555 1555 2.50
LINK OE2 GLU A 94 FE FE A 202 1555 1555 2.55
LINK OE2 GLU A 127 FE FE A 201 1555 1555 2.73
LINK OE2 GLU A 127 FE FE A 202 1555 1555 2.58
LINK FE FE A 201 O HOH A 509 1555 1555 2.24
LINK OE1 GLU B 18 FE FE B 201 1555 1555 2.50
LINK OE1 GLU B 51 FE FE B 201 1555 1555 2.21
LINK OE2 GLU B 51 FE FE B 202 1555 1555 2.50
LINK SD MET B 52 FE HEM B 301 1555 1555 2.61
LINK ND1 HIS B 54 FE FE B 201 1555 1555 2.70
LINK OE2 GLU B 127 FE FE B 201 1555 1555 2.38
LINK OE2 GLU B 127 FE FE B 202 1555 1555 2.65
LINK OE1 GLU B 127 FE FE B 202 1555 1555 2.70
LINK FE FE B 201 O HOH B 521 1555 1555 2.53
LINK OE1 GLU C 18 FE FE C 201 1555 1555 2.44
LINK OE1 GLU C 51 FE FE C 201 1555 1555 2.50
LINK OE2 GLU C 51 FE FE C 201 1555 1555 2.55
LINK OE2 GLU C 51 FE FE C 202 1555 1555 2.74
LINK SD MET C 52 FE HEM C 301 1555 1555 2.57
LINK ND1 HIS C 54 FE FE C 201 1555 1555 2.30
LINK OE2 GLU C 94 FE FE C 202 1555 1555 2.73
LINK OE2 GLU C 127 FE FE C 201 1555 1555 2.68
LINK OE2 GLU C 127 FE FE C 202 1555 1555 2.76
LINK FE FE C 201 O HOH C 520 1555 1555 2.48
LINK FE HEM C 301 SD MET D 52 1555 1555 2.58
LINK OE1 GLU D 18 FE FE D 201 1555 1555 2.40
LINK OE1 GLU D 51 FE FE D 201 1555 1555 2.47
LINK OE2 GLU D 51 FE FE D 202 1555 1555 2.58
LINK ND1 HIS D 54 FE FE D 201 1555 1555 2.66
LINK OE2 GLU D 127 FE FE D 201 1555 1555 2.47
LINK OE1 GLU D 127 FE FE D 202 1555 1555 2.61
LINK OE1 GLU E 18 FE FE E 201 1555 1555 2.44
LINK OE2 GLU E 18 FE FE E 201 1555 1555 2.60
LINK OE1 GLU E 51 FE FE E 201 1555 1555 2.26
LINK OE2 GLU E 51 FE FE E 202 1555 1555 2.41
LINK SD MET E 52 FE HEM E 301 1555 1555 2.45
LINK OE2 GLU E 94 FE FE E 202 1555 1555 2.49
LINK OE2 GLU E 127 FE FE E 201 1555 1555 2.56
LINK OE2 GLU E 127 FE FE E 202 1555 1555 2.79
LINK FE FE E 201 O HOH E 507 1555 1555 2.76
LINK FE HEM E 301 SD MET F 52 1555 1555 2.67
LINK OE1 GLU F 18 FE FE F 201 1555 1555 2.47
LINK OE1 GLU F 51 FE FE F 201 1555 1555 2.26
LINK OE2 GLU F 51 FE FE F 202 1555 1555 2.28
LINK ND1 HIS F 54 FE FE F 201 1555 1555 2.48
LINK OE2 GLU F 94 FE FE F 202 1555 1555 2.59
LINK OE2 GLU F 127 FE FE F 201 1555 1555 2.34
LINK OE1 GLU F 127 FE FE F 202 1555 1555 2.58
LINK FE FE F 201 O HOH F 516 1555 1555 2.30
CISPEP 1 ARG A 156 PRO A 157 0 -2.29
CISPEP 2 ARG B 156 PRO B 157 0 0.03
CISPEP 3 ARG C 156 PRO C 157 0 1.79
CISPEP 4 ARG D 156 PRO D 157 0 4.21
CISPEP 5 ARG E 156 PRO E 157 0 -0.38
CISPEP 6 ARG F 156 PRO F 157 0 2.12
SITE 1 AC1 5 GLU A 47 GLU A 51 GLU A 94 GLU A 127
SITE 2 AC1 5 HIS A 130
SITE 1 AC2 5 GLU A 18 GLU A 51 HIS A 54 GLU A 127
SITE 2 AC2 5 HOH A 509
SITE 1 AC3 5 GLU B 18 GLU B 51 HIS B 54 GLU B 127
SITE 2 AC3 5 HOH B 521
SITE 1 AC4 3 GLU B 51 GLU B 94 GLU B 127
SITE 1 AC5 5 GLU C 18 GLU C 51 HIS C 54 GLU C 127
SITE 2 AC5 5 HOH C 520
SITE 1 AC6 5 GLU C 51 GLU C 94 GLU C 127 HIS C 130
SITE 2 AC6 5 HOH C 511
SITE 1 AC7 4 GLU D 18 GLU D 51 HIS D 54 GLU D 127
SITE 1 AC8 5 GLU D 47 GLU D 51 GLU D 94 GLU D 127
SITE 2 AC8 5 HIS D 130
SITE 1 AC9 5 GLU E 18 GLU E 51 HIS E 54 GLU E 127
SITE 2 AC9 5 HOH E 507
SITE 1 BC1 4 GLU E 51 GLU E 94 GLU E 127 HIS E 130
SITE 1 BC2 6 GLU F 18 GLU F 51 HIS F 54 GLU F 127
SITE 2 BC2 6 HOH F 502 HOH F 516
SITE 1 BC3 3 GLU F 51 GLU F 94 GLU F 127
SITE 1 BC4 9 LEU E 19 PHE E 26 ARG E 53 GLU E 56
SITE 2 BC4 9 TYR E 71 HOH E 182 ASN F 23 PHE F 26
SITE 3 BC4 9 PHE F 49
SITE 1 BC5 14 LEU A 19 ILE A 22 ASN A 23 PHE A 26
SITE 2 BC5 14 ARG A 45 PHE A 49 ARG A 53 GLU A 56
SITE 3 BC5 14 LEU B 19 ASN B 23 PHE B 26 PHE B 49
SITE 4 BC5 14 ARG B 53 GLU B 56
SITE 1 BC6 14 LEU C 19 ASN C 23 PHE C 26 PHE C 49
SITE 2 BC6 14 ARG C 53 GLU C 56 HOH C 178 LEU D 19
SITE 3 BC6 14 ASN D 23 PHE D 26 PHE D 49 ARG D 53
SITE 4 BC6 14 GLU D 56 TYR D 71
CRYST1 124.343 124.343 174.976 90.00 90.00 90.00 I 4 48
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 0.008042 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008042 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005715 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
