HEADER HYDROLASE 04-AUG-06 2HY1
TITLE CRYSTAL STRUCTURE OF RV0805
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RV0805;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC CORE (RESIDUES 1-278);
COMPND 5 SYNONYM: ICC PROTEIN;
COMPND 6 EC: 3.1.4.17;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV0805;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PPROEXHTC
KEYWDS METALLOPHOSPHOESTERASE, CAMP, PHOSPHODIESTERASE, BI-NUCLEAR ACTIVE
KEYWDS 2 SITE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.SHENOY,M.CAPUDER,P.DRASKOVIC,D.LAMBA,S.S.VISWESWARIAH,M.PODOBNIK
REVDAT 5 14-FEB-24 2HY1 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2HY1 1 REMARK
REVDAT 3 13-JUL-11 2HY1 1 VERSN
REVDAT 2 24-FEB-09 2HY1 1 VERSN
REVDAT 1 26-DEC-06 2HY1 0
JRNL AUTH A.R.SHENOY,M.CAPUDER,P.DRASKOVIC,D.LAMBA,S.S.VISWESWARIAH,
JRNL AUTH 2 M.PODOBNIK
JRNL TITL STRUCTURAL AND BIOCHEMICAL ANALYSIS OF THE RV0805 CYCLIC
JRNL TITL 2 NUCLEOTIDE PHOSPHODIESTERASE FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS.
JRNL REF J.MOL.BIOL. V. 365 211 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17059828
JRNL DOI 10.1016/J.JMB.2006.10.005
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.R.SHENOY,N.SREENATH,M.PODOBNIK,M.KOVACEVIC,
REMARK 1 AUTH 2 S.S.VISWESWARIAH
REMARK 1 TITL THE RV0805 GENE FROM MYCOBACTERIUM TUBERCULOSIS ENCODES A
REMARK 1 TITL 2 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE: BIOCHEMICAL AND
REMARK 1 TITL 3 MUTATIONAL ANALYSIS
REMARK 1 REF BIOCHEMISTRY V. 44 15695 2005
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 20228
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) : 0.283
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2073
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) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1116
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1727
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.40000
REMARK 3 B22 (A**2) : -1.76000
REMARK 3 B33 (A**2) : 3.16000
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): 0.169
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.452
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1768 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2414 ; 1.044 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 224 ; 5.005 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;33.853 ;23.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 274 ;14.408 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;11.787 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 285 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1334 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 752 ; 0.175 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1182 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 127 ; 0.098 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.007 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 30 ; 0.148 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.130 ; 0.200
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): 1164 ; 0.289 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1823 ; 0.477 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 667 ; 0.781 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 591 ; 1.190 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 10 A 36
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0904 11.3969 11.6279
REMARK 3 T TENSOR
REMARK 3 T11: 0.0605 T22: 0.0673
REMARK 3 T33: 0.0208 T12: -0.0028
REMARK 3 T13: -0.0687 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 8.3420 L22: 3.8965
REMARK 3 L33: 10.1813 L12: -1.7732
REMARK 3 L13: -7.5146 L23: 2.6077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0918 S12: -0.4624 S13: -0.1418
REMARK 3 S21: 0.4281 S22: 0.0487 S23: -0.2539
REMARK 3 S31: 0.0936 S32: 0.2478 S33: 0.0430
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 : A 37 A 46
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7878 13.5597 24.8820
REMARK 3 T TENSOR
REMARK 3 T11: 0.4766 T22: 0.3160
REMARK 3 T33: 0.0210 T12: -0.0510
REMARK 3 T13: -0.1075 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 38.2304 L22: 8.2815
REMARK 3 L33: 9.0401 L12: -16.2043
REMARK 3 L13: -6.4239 L23: 4.1279
REMARK 3 S TENSOR
REMARK 3 S11: -0.3846 S12: -2.1199 S13: -0.0467
REMARK 3 S21: 1.4541 S22: 0.3441 S23: -0.2504
REMARK 3 S31: 0.6912 S32: 0.3994 S33: 0.0406
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 : A 47 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1043 9.3011 17.6907
REMARK 3 T TENSOR
REMARK 3 T11: 0.2257 T22: 0.4323
REMARK 3 T33: 0.2062 T12: 0.1107
REMARK 3 T13: -0.1574 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 2.2597 L22: 8.9649
REMARK 3 L33: 38.7210 L12: -2.4003
REMARK 3 L13: -6.1160 L23: -5.4289
REMARK 3 S TENSOR
REMARK 3 S11: -0.2890 S12: -1.0261 S13: -0.0066
REMARK 3 S21: 0.9503 S22: -0.1050 S23: -0.9108
REMARK 3 S31: 0.9465 S32: 1.7650 S33: 0.3939
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 : A 56 A 72
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4450 20.5372 15.0555
REMARK 3 T TENSOR
REMARK 3 T11: 0.1417 T22: 0.0243
REMARK 3 T33: -0.0310 T12: 0.0201
REMARK 3 T13: -0.0171 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 7.3299 L22: 4.7839
REMARK 3 L33: 3.3043 L12: -1.5701
REMARK 3 L13: -0.9489 L23: 1.6438
REMARK 3 S TENSOR
REMARK 3 S11: -0.0528 S12: -0.6090 S13: -0.0019
REMARK 3 S21: 0.4289 S22: 0.0220 S23: 0.3401
REMARK 3 S31: -0.3312 S32: -0.1060 S33: 0.0308
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 73 A 77
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6831 26.7152 19.4046
REMARK 3 T TENSOR
REMARK 3 T11: 0.3540 T22: 0.1458
REMARK 3 T33: 0.1390 T12: -0.0397
REMARK 3 T13: -0.0679 T23: -0.0916
REMARK 3 L TENSOR
REMARK 3 L11: 21.0601 L22: 0.1315
REMARK 3 L33: 7.4039 L12: -1.0175
REMARK 3 L13: 1.2067 L23: -0.8356
REMARK 3 S TENSOR
REMARK 3 S11: 0.2091 S12: -0.5442 S13: 1.0351
REMARK 3 S21: 0.4940 S22: -0.1083 S23: -0.0305
REMARK 3 S31: -1.0365 S32: 0.4536 S33: -0.1008
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 78 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2506 19.6402 15.7612
REMARK 3 T TENSOR
REMARK 3 T11: 0.1995 T22: 0.2709
REMARK 3 T33: 0.1212 T12: -0.0888
REMARK 3 T13: -0.0852 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 10.5961 L22: 4.1767
REMARK 3 L33: 12.8956 L12: -4.1448
REMARK 3 L13: -8.5765 L23: 4.0653
REMARK 3 S TENSOR
REMARK 3 S11: -0.0257 S12: -1.3775 S13: 0.4169
REMARK 3 S21: 0.4965 S22: 0.3307 S23: -0.2622
REMARK 3 S31: -0.1394 S32: 1.2803 S33: -0.3050
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 91 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1342 25.8780 11.4294
REMARK 3 T TENSOR
REMARK 3 T11: 0.1043 T22: -0.0182
REMARK 3 T33: 0.0943 T12: -0.0028
REMARK 3 T13: -0.0429 T23: -0.0486
REMARK 3 L TENSOR
REMARK 3 L11: 2.4026 L22: 4.5230
REMARK 3 L33: 2.7217 L12: -2.3181
REMARK 3 L13: 0.7392 L23: -0.7101
REMARK 3 S TENSOR
REMARK 3 S11: -0.2460 S12: -0.2344 S13: 0.4113
REMARK 3 S21: 0.5758 S22: 0.1065 S23: -0.0655
REMARK 3 S31: -0.4177 S32: 0.0147 S33: 0.1394
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 109 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2275 30.7215 6.0274
REMARK 3 T TENSOR
REMARK 3 T11: 0.0755 T22: 0.0064
REMARK 3 T33: 0.2225 T12: -0.0073
REMARK 3 T13: -0.0505 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.5618 L22: 7.9177
REMARK 3 L33: 5.0316 L12: -1.7191
REMARK 3 L13: 1.1800 L23: 1.8800
REMARK 3 S TENSOR
REMARK 3 S11: -0.0904 S12: -0.0946 S13: 0.6221
REMARK 3 S21: 0.0712 S22: 0.1670 S23: -0.5537
REMARK 3 S31: -0.6494 S32: 0.3543 S33: -0.0766
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 120 A 124
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1348 20.5403 -0.1282
REMARK 3 T TENSOR
REMARK 3 T11: 0.0501 T22: 0.0522
REMARK 3 T33: 0.1155 T12: 0.0051
REMARK 3 T13: -0.0602 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 18.2201 L22: 21.0017
REMARK 3 L33: 0.0798 L12: -17.7650
REMARK 3 L13: -0.3501 L23: 0.8598
REMARK 3 S TENSOR
REMARK 3 S11: -1.1381 S12: -1.2192 S13: 0.7509
REMARK 3 S21: 1.1580 S22: 0.8870 S23: -0.3685
REMARK 3 S31: 0.0262 S32: -0.0097 S33: 0.2511
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 125 A 139
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7486 19.5829 1.9308
REMARK 3 T TENSOR
REMARK 3 T11: 0.0005 T22: -0.0336
REMARK 3 T33: 0.0197 T12: 0.0101
REMARK 3 T13: -0.0410 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 10.9088 L22: 3.5532
REMARK 3 L33: 3.0695 L12: -4.2579
REMARK 3 L13: -4.5075 L23: 1.3608
REMARK 3 S TENSOR
REMARK 3 S11: -0.1118 S12: -0.0981 S13: 0.2252
REMARK 3 S21: 0.0798 S22: 0.0814 S23: 0.0695
REMARK 3 S31: -0.0860 S32: -0.0234 S33: 0.0304
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 140 A 151
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2445 21.6727 -1.2006
REMARK 3 T TENSOR
REMARK 3 T11: 0.0285 T22: 0.0561
REMARK 3 T33: 0.1594 T12: 0.0425
REMARK 3 T13: -0.0666 T23: 0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 10.6875 L22: 5.3267
REMARK 3 L33: 13.4523 L12: 5.9386
REMARK 3 L13: -10.6358 L23: -5.8906
REMARK 3 S TENSOR
REMARK 3 S11: 0.2475 S12: 0.1925 S13: 0.5253
REMARK 3 S21: 0.1789 S22: -0.0345 S23: 0.4665
REMARK 3 S31: -0.6313 S32: -0.3696 S33: -0.2130
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 152 A 158
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4334 19.5526 -10.7746
REMARK 3 T TENSOR
REMARK 3 T11: 0.0866 T22: 0.0996
REMARK 3 T33: 0.0462 T12: -0.0459
REMARK 3 T13: -0.0214 T23: 0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 24.5850 L22: 9.4108
REMARK 3 L33: 7.3092 L12: -3.0200
REMARK 3 L13: -2.6742 L23: 0.1857
REMARK 3 S TENSOR
REMARK 3 S11: 0.1231 S12: 1.2675 S13: 1.4507
REMARK 3 S21: -0.6909 S22: -0.1317 S23: 0.0965
REMARK 3 S31: -0.4785 S32: 0.3974 S33: 0.0087
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 159 A 187
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3750 11.1547 2.9669
REMARK 3 T TENSOR
REMARK 3 T11: 0.0024 T22: -0.0428
REMARK 3 T33: 0.0830 T12: 0.0147
REMARK 3 T13: -0.0298 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 4.3528 L22: 3.5263
REMARK 3 L33: 3.9599 L12: -0.1410
REMARK 3 L13: -0.4916 L23: 0.9562
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: -0.1625 S13: 0.0225
REMARK 3 S21: 0.1467 S22: -0.0859 S23: 0.6706
REMARK 3 S31: 0.1520 S32: -0.4355 S33: 0.1314
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 188 A 193
REMARK 3 ORIGIN FOR THE GROUP (A): -10.1590 12.6831 -7.2322
REMARK 3 T TENSOR
REMARK 3 T11: 0.0625 T22: 0.1017
REMARK 3 T33: 0.1372 T12: 0.0174
REMARK 3 T13: -0.1077 T23: 0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 21.3690 L22: 2.7991
REMARK 3 L33: 12.7102 L12: 5.6596
REMARK 3 L13: -6.1553 L23: 0.5902
REMARK 3 S TENSOR
REMARK 3 S11: -0.4364 S12: 1.1505 S13: 0.4520
REMARK 3 S21: -0.3291 S22: 0.1677 S23: 0.7366
REMARK 3 S31: -0.0583 S32: -0.6143 S33: 0.2688
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 194 A 199
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3989 11.0312 -10.3092
REMARK 3 T TENSOR
REMARK 3 T11: 0.1504 T22: 0.2048
REMARK 3 T33: 0.1230 T12: -0.0308
REMARK 3 T13: -0.0657 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 30.4286 L22: 10.4246
REMARK 3 L33: 4.8818 L12: -9.5439
REMARK 3 L13: -0.9045 L23: -1.2500
REMARK 3 S TENSOR
REMARK 3 S11: 0.2884 S12: 1.9075 S13: -1.1754
REMARK 3 S21: -0.8416 S22: -0.2135 S23: 0.6873
REMARK 3 S31: 0.1236 S32: -0.5286 S33: -0.0750
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 200 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9711 9.7018 3.3332
REMARK 3 T TENSOR
REMARK 3 T11: -0.0113 T22: -0.0042
REMARK 3 T33: 0.0409 T12: -0.0017
REMARK 3 T13: -0.0165 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 3.4395 L22: 4.4843
REMARK 3 L33: 3.3185 L12: 0.4428
REMARK 3 L13: 0.3255 L23: -0.0905
REMARK 3 S TENSOR
REMARK 3 S11: -0.0632 S12: -0.0506 S13: -0.0355
REMARK 3 S21: 0.1388 S22: 0.0279 S23: 0.0902
REMARK 3 S31: 0.0643 S32: -0.1484 S33: 0.0353
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 209 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4317 4.1914 10.5014
REMARK 3 T TENSOR
REMARK 3 T11: 0.1006 T22: 0.1572
REMARK 3 T33: 0.0842 T12: 0.0021
REMARK 3 T13: 0.0296 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 2.6617 L22: 18.9045
REMARK 3 L33: 26.3356 L12: 1.2920
REMARK 3 L13: 2.4929 L23: 16.5127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0086 S12: -0.4469 S13: 0.2199
REMARK 3 S21: 1.0369 S22: -0.5233 S23: 0.8444
REMARK 3 S31: 0.0636 S32: -1.5389 S33: 0.5147
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 215 A 226
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8348 5.9618 2.1460
REMARK 3 T TENSOR
REMARK 3 T11: -0.0301 T22: -0.0590
REMARK 3 T33: -0.0552 T12: -0.0004
REMARK 3 T13: 0.0090 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 6.6369 L22: 4.3393
REMARK 3 L33: 9.8660 L12: 0.0114
REMARK 3 L13: 2.8679 L23: -0.1696
REMARK 3 S TENSOR
REMARK 3 S11: 0.1032 S12: 0.0470 S13: -0.0317
REMARK 3 S21: 0.0067 S22: 0.0371 S23: 0.2344
REMARK 3 S31: -0.1940 S32: 0.0233 S33: -0.1403
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 227 A 256
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5004 5.7513 8.4914
REMARK 3 T TENSOR
REMARK 3 T11: 0.0642 T22: 0.0467
REMARK 3 T33: 0.0987 T12: -0.0301
REMARK 3 T13: -0.0591 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 9.5726 L22: 5.1359
REMARK 3 L33: 12.9436 L12: -2.0133
REMARK 3 L13: -7.3701 L23: 2.0384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0788 S12: -0.6359 S13: 0.2885
REMARK 3 S21: 0.5770 S22: 0.2130 S23: -0.3460
REMARK 3 S31: 0.1226 S32: 0.3565 S33: -0.1342
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 257 A 265
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1254 1.9335 6.9095
REMARK 3 T TENSOR
REMARK 3 T11: 0.0413 T22: 0.0090
REMARK 3 T33: 0.0737 T12: -0.0323
REMARK 3 T13: -0.0283 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 10.0335 L22: 9.5992
REMARK 3 L33: 21.9946 L12: 0.8565
REMARK 3 L13: -8.5266 L23: -2.5535
REMARK 3 S TENSOR
REMARK 3 S11: 0.0991 S12: -0.5394 S13: -0.2309
REMARK 3 S21: 0.5291 S22: -0.0041 S23: -0.3053
REMARK 3 S31: 0.1803 S32: 0.6306 S33: -0.0950
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2HY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000038895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI)
REMARK 200 OPTICS : MONOCHROMATOR, MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 50.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.37500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, MGCL2, MES, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 27.63150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.14950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.63150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.14950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS:-X,-Y,Z
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
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 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 HIS A 9
REMARK 465 GLY A 26
REMARK 465 GLY A 27
REMARK 465 ASP A 28
REMARK 465 ARG A 29
REMARK 465 ARG A 30
REMARK 465 LEU A 31
REMARK 465 TYR A 32
REMARK 465 GLY A 33
REMARK 465 ALA A 34
REMARK 465 VAL A 35
REMARK 465 TYR A 229
REMARK 465 THR A 230
REMARK 465 GLN A 231
REMARK 465 ASP A 232
REMARK 465 LEU A 233
REMARK 465 THR A 234
REMARK 465 VAL A 235
REMARK 465 ALA A 236
REMARK 465 ALA A 237
REMARK 465 GLY A 238
REMARK 465 GLY A 239
REMARK 465 THR A 240
REMARK 465 ARG A 241
REMARK 465 GLY A 242
REMARK 465 ARG A 243
REMARK 465 ASP A 244
REMARK 465 GLY A 245
REMARK 465 ALA A 246
REMARK 465 GLN A 247
REMARK 465 LEU A 266
REMARK 465 GLY A 267
REMARK 465 GLY A 268
REMARK 465 GLY A 269
REMARK 465 GLU A 270
REMARK 465 THR A 271
REMARK 465 VAL A 272
REMARK 465 GLY A 273
REMARK 465 THR A 274
REMARK 465 PHE A 275
REMARK 465 VAL A 276
REMARK 465 SER A 277
REMARK 465 PRO A 278
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 265 C PRO A 265 O 0.201
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 THR A 61 45.40 -87.85
REMARK 500 ASP A 125 -113.40 52.95
REMARK 500 HIS A 169 -61.12 -94.34
REMARK 500 HIS A 207 -41.02 81.57
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 444 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 21 OD2
REMARK 620 2 HIS A 23 NE2 116.4
REMARK 620 3 ASP A 63 OD2 91.1 102.3
REMARK 620 4 HIS A 209 NE2 81.7 93.5 164.2
REMARK 620 5 PO4 A 666 O3 162.2 80.1 91.7 91.1
REMARK 620 6 HOH A 768 O 79.9 163.7 76.4 88.5 83.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 555 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD2
REMARK 620 2 ASN A 97 OD1 96.1
REMARK 620 3 HIS A 169 NE2 90.8 90.9
REMARK 620 4 HIS A 207 ND1 163.3 100.0 93.2
REMARK 620 5 PO4 A 666 O4 84.1 89.3 175.0 91.7
REMARK 620 6 HOH A 768 O 67.3 149.0 114.3 96.3 64.0
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 FE A 444
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 555
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 666
DBREF 2HY1 A 3 278 UNP O06629 O06629_MYCTU 3 278
SEQADV 2HY1 GLY A -1 UNP O06629 CLONING ARTIFACT
SEQADV 2HY1 ALA A 0 UNP O06629 CLONING ARTIFACT
SEQADV 2HY1 MET A 1 UNP O06629 CLONING ARTIFACT
SEQADV 2HY1 ASP A 2 UNP O06629 CLONING ARTIFACT
SEQRES 1 A 280 GLY ALA MET ASP ARG LEU ARG ALA ALA GLU HIS PRO ARG
SEQRES 2 A 280 PRO ASP TYR VAL LEU LEU HIS ILE SER ASP THR HIS LEU
SEQRES 3 A 280 ILE GLY GLY ASP ARG ARG LEU TYR GLY ALA VAL ASP ALA
SEQRES 4 A 280 ASP ASP ARG LEU GLY GLU LEU LEU GLU GLN LEU ASN GLN
SEQRES 5 A 280 SER GLY LEU ARG PRO ASP ALA ILE VAL PHE THR GLY ASP
SEQRES 6 A 280 LEU ALA ASP LYS GLY GLU PRO ALA ALA TYR ARG LYS LEU
SEQRES 7 A 280 ARG GLY LEU VAL GLU PRO PHE ALA ALA GLN LEU GLY ALA
SEQRES 8 A 280 GLU LEU VAL TRP VAL MET GLY ASN HIS ASP ASP ARG ALA
SEQRES 9 A 280 GLU LEU ARG LYS PHE LEU LEU ASP GLU ALA PRO SER MET
SEQRES 10 A 280 ALA PRO LEU ASP ARG VAL CYS MET ILE ASP GLY LEU ARG
SEQRES 11 A 280 ILE ILE VAL LEU ASP THR SER VAL PRO GLY HIS HIS HIS
SEQRES 12 A 280 GLY GLU ILE ARG ALA SER GLN LEU GLY TRP LEU ALA GLU
SEQRES 13 A 280 GLU LEU ALA THR PRO ALA PRO ASP GLY THR ILE LEU ALA
SEQRES 14 A 280 LEU HIS HIS PRO PRO ILE PRO SER VAL LEU ASP MET ALA
SEQRES 15 A 280 VAL THR VAL GLU LEU ARG ASP GLN ALA ALA LEU GLY ARG
SEQRES 16 A 280 VAL LEU ARG GLY THR ASP VAL ARG ALA ILE LEU ALA GLY
SEQRES 17 A 280 HIS LEU HIS TYR SER THR ASN ALA THR PHE VAL GLY ILE
SEQRES 18 A 280 PRO VAL SER VAL ALA SER ALA THR CYS TYR THR GLN ASP
SEQRES 19 A 280 LEU THR VAL ALA ALA GLY GLY THR ARG GLY ARG ASP GLY
SEQRES 20 A 280 ALA GLN GLY CYS ASN LEU VAL HIS VAL TYR PRO ASP THR
SEQRES 21 A 280 VAL VAL HIS SER VAL ILE PRO LEU GLY GLY GLY GLU THR
SEQRES 22 A 280 VAL GLY THR PHE VAL SER PRO
HET FE A 444 1
HET MN A 555 1
HET PO4 A 666 5
HETNAM FE FE (III) ION
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 FE FE 3+
FORMUL 3 MN MN 2+
FORMUL 4 PO4 O4 P 3-
FORMUL 5 HOH *103(H2 O)
HELIX 1 1 ASP A 36 GLY A 52 1 17
HELIX 2 2 GLU A 69 GLY A 88 1 20
HELIX 3 3 ASP A 100 LEU A 108 1 9
HELIX 4 4 ARG A 145 ALA A 157 1 13
HELIX 5 5 LEU A 177 THR A 182 1 6
HELIX 6 6 ASP A 187 ARG A 196 1 10
SHEET 1 A 5 GLU A 90 TRP A 93 0
SHEET 2 A 5 ALA A 57 PHE A 60 1 N ILE A 58 O GLU A 90
SHEET 3 A 5 TYR A 14 ILE A 19 1 N LEU A 17 O VAL A 59
SHEET 4 A 5 CYS A 249 VAL A 254 -1 O ASN A 250 N HIS A 18
SHEET 5 A 5 VAL A 259 ILE A 264 -1 O ILE A 264 N CYS A 249
SHEET 1 B 6 ARG A 120 ILE A 124 0
SHEET 2 B 6 LEU A 127 VAL A 131 -1 O LEU A 127 N ILE A 124
SHEET 3 B 6 THR A 164 ALA A 167 1 O ALA A 167 N ILE A 130
SHEET 4 B 6 VAL A 200 ALA A 205 1 O ARG A 201 N THR A 164
SHEET 5 B 6 ILE A 219 VAL A 223 1 O SER A 222 N ILE A 203
SHEET 6 B 6 THR A 212 PHE A 216 -1 N THR A 212 O VAL A 223
LINK OD2 ASP A 21 FE FE A 444 1555 1555 2.03
LINK NE2 HIS A 23 FE FE A 444 1555 1555 2.29
LINK OD2 ASP A 63 FE FE A 444 1555 1555 2.16
LINK OD2 ASP A 63 MN MN A 555 1555 1555 2.26
LINK OD1 ASN A 97 MN MN A 555 1555 1555 2.09
LINK NE2 HIS A 169 MN MN A 555 1555 1555 2.13
LINK ND1 HIS A 207 MN MN A 555 1555 1555 2.20
LINK NE2 HIS A 209 FE FE A 444 1555 1555 2.29
LINK FE FE A 444 O3 PO4 A 666 1555 1555 2.29
LINK FE FE A 444 O HOH A 768 1555 1555 1.95
LINK MN MN A 555 O4 PO4 A 666 1555 1555 2.52
LINK MN MN A 555 O HOH A 768 1555 1555 2.34
SITE 1 AC1 7 ASP A 21 HIS A 23 ASP A 63 HIS A 209
SITE 2 AC1 7 MN A 555 PO4 A 666 HOH A 768
SITE 1 AC2 7 ASP A 63 ASN A 97 HIS A 169 HIS A 207
SITE 2 AC2 7 FE A 444 PO4 A 666 HOH A 768
SITE 1 AC3 9 HIS A 23 ASP A 63 ASN A 97 HIS A 98
SITE 2 AC3 9 HIS A 207 HIS A 209 FE A 444 MN A 555
SITE 3 AC3 9 HOH A 768
CRYST1 55.263 94.299 50.916 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018095 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010605 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
