HEADER OXIDOREDUCTASE 27-NOV-15 5EZW
TITLE THIOSULFATE BOUND RAT CYSTEINE DIOXYGENASE Y157H VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE DIOXYGENASE TYPE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYSTEINE DIOXYGENASE TYPE I,CDO-I;
COMPND 5 EC: 1.13.11.20;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CDO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPR-IBA1/RATCDO/Y155H_VARIANT
KEYWDS THIOETHER BOND, POST-TRANSLATIONAL MODIFICATION, POST TRANSLATIONAL,
KEYWDS 2 POSTTRANSLATIONAL, CYSTEINE DIOXYGENASE, NON-HEME MONO-IRON, CUPIN,
KEYWDS 3 TYROSINE TO HISTIDINE SUBSTITUTION, BETA BARREL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER,E.P.TCHESNOKOV,G.N.L.JAMESON,S.M.WILBANKS
REVDAT 1 09-NOV-16 5EZW 0
JRNL AUTH M.FELLNER,S.M.WILBANKS
JRNL TITL THIOSULFATE BOUND RAT CYSTEINE DIOXYGENASE Y157H VARIANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10-2155
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 24543
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2293
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 26.1183 - 4.1527 1.00 2849 129 0.1455 0.1454
REMARK 3 2 4.1527 - 3.2982 1.00 2837 131 0.1452 0.1312
REMARK 3 3 3.2982 - 2.8819 1.00 2821 145 0.1611 0.1869
REMARK 3 4 2.8819 - 2.6187 1.00 2819 160 0.1767 0.2232
REMARK 3 5 2.6187 - 2.4311 1.00 2798 180 0.1785 0.2239
REMARK 3 6 2.4311 - 2.2879 1.00 2809 162 0.1805 0.1994
REMARK 3 7 2.2879 - 2.1734 0.99 2808 145 0.1677 0.1784
REMARK 3 8 2.1734 - 2.0788 1.00 2803 136 0.1650 0.1879
REMARK 3 9 2.0788 - 1.9988 0.99 2780 169 0.1846 0.1987
REMARK 3 10 1.9988 - 1.9298 0.99 2799 155 0.1821 0.1845
REMARK 3 11 1.9298 - 1.8695 0.99 2786 149 0.1827 0.2224
REMARK 3 12 1.8695 - 1.8161 0.99 2792 125 0.1871 0.2528
REMARK 3 13 1.8161 - 1.7683 0.98 2777 177 0.2053 0.2317
REMARK 3 14 1.7683 - 1.7252 0.91 2573 128 0.2479 0.3151
REMARK 3 15 1.7252 - 1.6859 0.78 2213 114 0.3096 0.3355
REMARK 3 16 1.6859 - 1.6501 0.69 1924 88 0.4006 0.4675
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.18
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 1583
REMARK 3 ANGLE : 0.858 2137
REMARK 3 CHIRALITY : 0.053 229
REMARK 3 PLANARITY : 0.005 278
REMARK 3 DIHEDRAL : 13.765 580
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5425 -19.0819 9.4176
REMARK 3 T TENSOR
REMARK 3 T11: 0.1515 T22: 0.1595
REMARK 3 T33: 0.1844 T12: 0.0140
REMARK 3 T13: -0.0011 T23: -0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 6.9347 L22: 8.9195
REMARK 3 L33: 8.3031 L12: 1.8265
REMARK 3 L13: -0.2741 L23: -2.8189
REMARK 3 S TENSOR
REMARK 3 S11: -0.0159 S12: 0.3983 S13: -0.6104
REMARK 3 S21: -0.5221 S22: 0.0666 S23: 0.1579
REMARK 3 S31: 0.3635 S32: -0.3840 S33: -0.0658
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 23 THROUGH 39 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8680 -10.7960 8.1753
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.1674
REMARK 3 T33: 0.1650 T12: 0.0061
REMARK 3 T13: -0.0308 T23: -0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 6.5028 L22: 7.3644
REMARK 3 L33: 8.6532 L12: -0.2163
REMARK 3 L13: -0.5539 L23: -4.3898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0407 S12: 0.4282 S13: 0.1321
REMARK 3 S21: -0.3268 S22: 0.1373 S23: 0.4023
REMARK 3 S31: -0.0121 S32: -0.5554 S33: -0.2014
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7521 -9.7829 25.6356
REMARK 3 T TENSOR
REMARK 3 T11: 0.0759 T22: 0.1183
REMARK 3 T33: 0.0683 T12: 0.0078
REMARK 3 T13: 0.0003 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 2.9335 L22: 7.6049
REMARK 3 L33: 4.4199 L12: 0.5778
REMARK 3 L13: 1.7011 L23: 3.5644
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: -0.1156 S13: -0.0977
REMARK 3 S21: 0.1551 S22: 0.0946 S23: -0.2724
REMARK 3 S31: 0.0811 S32: 0.1132 S33: -0.1369
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 59 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0802 -2.7128 19.6328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.1254
REMARK 3 T33: 0.1324 T12: -0.0105
REMARK 3 T13: -0.0042 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 1.6035 L22: 1.8763
REMARK 3 L33: 1.6766 L12: -0.6388
REMARK 3 L13: 0.2122 L23: 0.3274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0274 S12: 0.0184 S13: -0.0204
REMARK 3 S21: -0.0663 S22: 0.0531 S23: -0.0156
REMARK 3 S31: -0.0374 S32: -0.0315 S33: -0.0245
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0311 16.5222 20.9408
REMARK 3 T TENSOR
REMARK 3 T11: 0.3725 T22: 0.2388
REMARK 3 T33: 0.3692 T12: 0.1241
REMARK 3 T13: -0.0475 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 6.8297 L22: 9.7988
REMARK 3 L33: 6.2407 L12: -1.1763
REMARK 3 L13: -1.5015 L23: 1.6396
REMARK 3 S TENSOR
REMARK 3 S11: -0.1203 S12: -0.1871 S13: 1.0884
REMARK 3 S21: 0.2231 S22: -0.0185 S23: 0.7678
REMARK 3 S31: -1.2931 S32: -0.7869 S33: 0.0610
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 133 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5692 -4.8834 23.9788
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.2303
REMARK 3 T33: 0.2705 T12: -0.0162
REMARK 3 T13: 0.0272 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 3.4880 L22: 3.3511
REMARK 3 L33: 4.5237 L12: -0.9541
REMARK 3 L13: -1.1535 L23: 0.4841
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.3188 S13: -0.2085
REMARK 3 S21: 0.2826 S22: -0.0217 S23: 0.5487
REMARK 3 S31: -0.0867 S32: -0.3615 S33: -0.0039
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 134 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3093 3.9014 19.5493
REMARK 3 T TENSOR
REMARK 3 T11: 0.1306 T22: 0.1514
REMARK 3 T33: 0.1539 T12: 0.0327
REMARK 3 T13: -0.0068 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 5.8479 L22: 7.0010
REMARK 3 L33: 2.0373 L12: -2.9425
REMARK 3 L13: 2.2105 L23: -4.9707
REMARK 3 S TENSOR
REMARK 3 S11: -0.1940 S12: -0.1282 S13: -0.0275
REMARK 3 S21: 0.0959 S22: 0.0885 S23: 0.2698
REMARK 3 S31: -0.3412 S32: -0.5443 S33: 0.2670
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 144 THROUGH 167 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7060 -0.6757 21.8139
REMARK 3 T TENSOR
REMARK 3 T11: 0.0920 T22: 0.1340
REMARK 3 T33: 0.1586 T12: 0.0052
REMARK 3 T13: 0.0013 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 1.1059 L22: 1.7988
REMARK 3 L33: 2.4744 L12: -0.5349
REMARK 3 L13: 0.5515 L23: 0.4379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0004 S13: 0.0679
REMARK 3 S21: -0.0621 S22: 0.0142 S23: 0.0297
REMARK 3 S31: -0.0560 S32: 0.0315 S33: -0.0287
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 178 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6050 15.8575 21.7870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2859 T22: 0.2333
REMARK 3 T33: 0.3415 T12: 0.0092
REMARK 3 T13: -0.0614 T23: -0.0932
REMARK 3 L TENSOR
REMARK 3 L11: 2.0937 L22: 6.9994
REMARK 3 L33: 7.5766 L12: -4.7587
REMARK 3 L13: -6.1649 L23: 2.8861
REMARK 3 S TENSOR
REMARK 3 S11: 0.1769 S12: -0.7512 S13: 1.1445
REMARK 3 S21: 0.1523 S22: 0.2847 S23: -0.7279
REMARK 3 S31: -0.8306 S32: 0.2981 S33: -0.3457
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.4931 -1.6376 18.5306
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.2009
REMARK 3 T33: 0.2801 T12: -0.0358
REMARK 3 T13: 0.0092 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 4.7131 L22: 6.4458
REMARK 3 L33: 4.6062 L12: -4.7429
REMARK 3 L13: -1.0611 L23: 0.5125
REMARK 3 S TENSOR
REMARK 3 S11: -0.0494 S12: 0.2817 S13: 0.6236
REMARK 3 S21: -0.1234 S22: 0.1474 S23: -0.0653
REMARK 3 S31: -0.2347 S32: 0.3326 S33: -0.1124
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215777.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC VARIMAX OPTICS
REMARK 200 OPTICS : OSMIC VARIMAX OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24590
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 26.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 24.10
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.3
REMARK 200 DATA REDUNDANCY IN SHELL : 11.70
REMARK 200 R MERGE FOR SHELL (I) : 0.82300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4KWJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS OF 3 MICROL OF
REMARK 280 APPROXIMATELY 25 MG/ML Y157H-CDO (20MM TRIS-HCL, PH 8.0) AND 1
REMARK 280 MICROL RESERVOIR BUFFER CONTAINING SEEDS FROM WT-CDO WERE
REMARK 280 ALLOWED TO EQUILIBRATE ABOVE THE RESERVOIR BUFFER (26% (W/V)
REMARK 280 POLYETHYLENE GLYCOL 4000, 200 MM AMMONIUM ACETATE, 100 MM SODIUM
REMARK 280 CITRATE)., PH 6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 61.21000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.87500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.87500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.81500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.87500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.87500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 30.60500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.87500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.87500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 91.81500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.87500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.87500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 30.60500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 61.21000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 A 1
REMARK 465 GLU A 2
REMARK 465 ARG A 3
REMARK 465 PHE A 191
REMARK 465 THR A 192
REMARK 465 THR A 193
REMARK 465 SER A 194
REMARK 465 GLY A 195
REMARK 465 SER A 196
REMARK 465 LEU A 197
REMARK 465 GLU A 198
REMARK 465 ASN A 199
REMARK 465 ASN A 200
REMARK 465 SER A 201
REMARK 465 ALA A 202
REMARK 465 TRP A 203
REMARK 465 SER A 204
REMARK 465 HIS A 205
REMARK 465 PRO A 206
REMARK 465 GLN A 207
REMARK 465 PHE A 208
REMARK 465 GLU A 209
REMARK 465 LYS A 210
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 OE2 GLU A 5 O HOH A 401 2.05
REMARK 500 O HOH A 557 O HOH A 598 2.08
REMARK 500 O HOH A 581 O HOH A 585 2.14
REMARK 500 OE1 GLU A 38 O HOH A 402 2.16
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 ASN A 128 -7.12 76.12
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 FE2 A 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 NE2
REMARK 620 2 HIS A 88 NE2 103.0
REMARK 620 3 HIS A 140 NE2 97.2 97.9
REMARK 620 4 THJ A 302 S2 117.5 125.3 110.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue THJ A 302
DBREF 5EZW A 1 200 UNP P21816 CDO1_RAT 1 200
SEQADV 5EZW HIS A 157 UNP P21816 TYR 157 ENGINEERED MUTATION
SEQADV 5EZW SER A 201 UNP P21816 EXPRESSION TAG
SEQADV 5EZW ALA A 202 UNP P21816 EXPRESSION TAG
SEQADV 5EZW TRP A 203 UNP P21816 EXPRESSION TAG
SEQADV 5EZW SER A 204 UNP P21816 EXPRESSION TAG
SEQADV 5EZW HIS A 205 UNP P21816 EXPRESSION TAG
SEQADV 5EZW PRO A 206 UNP P21816 EXPRESSION TAG
SEQADV 5EZW GLN A 207 UNP P21816 EXPRESSION TAG
SEQADV 5EZW PHE A 208 UNP P21816 EXPRESSION TAG
SEQADV 5EZW GLU A 209 UNP P21816 EXPRESSION TAG
SEQADV 5EZW LYS A 210 UNP P21816 EXPRESSION TAG
SEQRES 1 A 210 MET GLU ARG THR GLU LEU LEU LYS PRO ARG THR LEU ALA
SEQRES 2 A 210 ASP LEU ILE ARG ILE LEU HIS GLU LEU PHE ALA GLY ASP
SEQRES 3 A 210 GLU VAL ASN VAL GLU GLU VAL GLN ALA VAL LEU GLU ALA
SEQRES 4 A 210 TYR GLU SER ASN PRO ALA GLU TRP ALA LEU TYR ALA LYS
SEQRES 5 A 210 PHE ASP GLN TYR ARG TYR THR ARG ASN LEU VAL ASP GLN
SEQRES 6 A 210 GLY ASN GLY LYS PHE ASN LEU MET ILE LEU CYS TRP GLY
SEQRES 7 A 210 GLU GLY HIS GLY SER SER ILE HIS ASP HIS THR ASP SER
SEQRES 8 A 210 HIS CYS PHE LEU LYS LEU LEU GLN GLY ASN LEU LYS GLU
SEQRES 9 A 210 THR LEU PHE ASP TRP PRO ASP LYS LYS SER ASN GLU MET
SEQRES 10 A 210 ILE LYS LYS SER GLU ARG THR LEU ARG GLU ASN GLN CYS
SEQRES 11 A 210 ALA TYR ILE ASN ASP SER ILE GLY LEU HIS ARG VAL GLU
SEQRES 12 A 210 ASN VAL SER HIS THR GLU PRO ALA VAL SER LEU HIS LEU
SEQRES 13 A 210 HIS SER PRO PRO PHE ASP THR CYS HIS ALA PHE ASP GLN
SEQRES 14 A 210 ARG THR GLY HIS LYS ASN LYS VAL THR MET THR PHE HIS
SEQRES 15 A 210 SER LYS PHE GLY ILE ARG THR PRO PHE THR THR SER GLY
SEQRES 16 A 210 SER LEU GLU ASN ASN SER ALA TRP SER HIS PRO GLN PHE
SEQRES 17 A 210 GLU LYS
HET FE2 A 301 1
HET THJ A 302 5
HETNAM FE2 FE (II) ION
HETNAM THJ THIOSULFATE
FORMUL 2 FE2 FE 2+
FORMUL 3 THJ O3 S2 2-
FORMUL 4 HOH *243(H2 O)
HELIX 1 AA1 THR A 11 PHE A 23 1 13
HELIX 2 AA2 ASN A 29 TYR A 40 1 12
HELIX 3 AA3 ASN A 43 ALA A 48 1 6
HELIX 4 AA4 LEU A 49 ALA A 51 5 3
HELIX 5 AA5 GLN A 65 LYS A 69 5 5
SHEET 1 AA1 7 CYS A 130 ILE A 133 0
SHEET 2 AA1 7 HIS A 92 GLN A 99 -1 N LEU A 95 O ALA A 131
SHEET 3 AA1 7 ALA A 151 SER A 158 -1 O LEU A 154 N LYS A 96
SHEET 4 AA1 7 ASN A 71 TRP A 77 -1 N MET A 73 O HIS A 155
SHEET 5 AA1 7 THR A 59 ASP A 64 -1 N VAL A 63 O LEU A 72
SHEET 6 AA1 7 SER A 183 LYS A 184 1 O SER A 183 N LEU A 62
SHEET 7 AA1 7 ILE A 187 ARG A 188 -1 O ILE A 187 N LYS A 184
SHEET 1 AA2 3 ILE A 85 HIS A 86 0
SHEET 2 AA2 3 THR A 163 PHE A 167 -1 O PHE A 167 N ILE A 85
SHEET 3 AA2 3 LYS A 174 THR A 178 -1 O VAL A 177 N CYS A 164
SHEET 1 AA3 3 LYS A 119 LEU A 125 0
SHEET 2 AA3 3 LEU A 102 PHE A 107 -1 N LEU A 106 O LYS A 120
SHEET 3 AA3 3 LEU A 139 GLU A 143 -1 O GLU A 143 N LYS A 103
LINK NE2 HIS A 86 FE FE2 A 301 1555 1555 2.01
LINK NE2 HIS A 88 FE FE2 A 301 1555 1555 2.06
LINK NE2 HIS A 140 FE FE2 A 301 1555 1555 2.09
LINK FE FE2 A 301 S2 THJ A 302 1555 1555 2.25
CISPEP 1 SER A 158 PRO A 159 0 -3.96
SITE 1 AC1 4 HIS A 86 HIS A 88 HIS A 140 THJ A 302
SITE 1 AC2 9 ARG A 60 HIS A 86 HIS A 88 HIS A 140
SITE 2 AC2 9 HIS A 155 HIS A 157 FE2 A 301 HOH A 469
SITE 3 AC2 9 HOH A 500
CRYST1 57.750 57.750 122.420 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017316 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017316 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008169 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
