HEADER METAL BINDING PROTEIN 13-DEC-12 3ZG1
TITLE NI-BOUND FORM OF M123A MUTANT OF CUPRIAVIDUS METALLIDURANS CH34 CNRXS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NICKEL AND COBALT RESISTANCE PROTEIN CNRR;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: METAL-SENSOR DOMAIN, RESIDUES 31-148;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUPRIAVIDUS METALLIDURANS;
SOURCE 3 ORGANISM_TAXID: 266264;
SOURCE 4 STRAIN: CH34;
SOURCE 5 ATCC: 43123;
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: PET30
KEYWDS METAL BINDING PROTEIN, SENSOR PROTEIN, SIGNAL TRANSDUCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.GIRARD,J.COVES
REVDAT 4 20-DEC-23 3ZG1 1 REMARK LINK
REVDAT 3 12-FEB-14 3ZG1 1 JRNL
REVDAT 2 06-NOV-13 3ZG1 1 JRNL
REVDAT 1 23-OCT-13 3ZG1 0
JRNL AUTH J.TREPREAU,C.GROSSE,J.-M.MOUESCA,G.SARRET,E.GIRARD,
JRNL AUTH 2 I.PETIT-HAERTLEIN,S.KUENNEMANN,C.DESBOURDES,E.DE ROSNY,
JRNL AUTH 3 A.P.MAILLARD,D.H.NIES,J.COVES
JRNL TITL METAL SENSING AND SIGNAL TRANSDUCTION BY CNRX FROM
JRNL TITL 2 CUPRIAVIDUS METALLIDURANS CH34: ROLE OF THE ONLY METHIONINE
JRNL TITL 3 ASSESSED BY A FUNCTIONAL, SPECTROSCOPIC, AND THEORETICAL
JRNL TITL 4 STUDY
JRNL REF METALLOMICS V. 6 263 2014
JRNL REFN ISSN 1756-5901
JRNL PMID 24154823
JRNL DOI 10.1039/C3MT00248A
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.890
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 39447
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1987
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 36.4407 - 4.4567 0.95 2746 135 0.1481 0.1994
REMARK 3 2 4.4567 - 3.5384 0.94 2658 141 0.1336 0.1757
REMARK 3 3 3.5384 - 3.0913 0.95 2721 144 0.1525 0.2068
REMARK 3 4 3.0913 - 2.8088 0.95 2697 145 0.1727 0.2235
REMARK 3 5 2.8088 - 2.6076 0.95 2684 135 0.1754 0.2271
REMARK 3 6 2.6076 - 2.4539 0.95 2649 140 0.1832 0.2637
REMARK 3 7 2.4539 - 2.3310 0.94 2708 153 0.1896 0.2544
REMARK 3 8 2.3310 - 2.2295 0.95 2662 137 0.1958 0.2358
REMARK 3 9 2.2295 - 2.1437 0.95 2655 131 0.1982 0.2241
REMARK 3 10 2.1437 - 2.0697 0.94 2678 157 0.2151 0.2735
REMARK 3 11 2.0697 - 2.0050 0.95 2648 132 0.2373 0.2376
REMARK 3 12 2.0050 - 1.9477 0.94 2665 151 0.2602 0.3245
REMARK 3 13 1.9477 - 1.8965 0.95 2667 134 0.2880 0.3244
REMARK 3 14 1.8965 - 1.8502 0.93 2623 142 0.3159 0.3398
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.800
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) : 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: 0.4000
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 3713
REMARK 3 ANGLE : 0.598 5014
REMARK 3 CHIRALITY : 0.042 544
REMARK 3 PLANARITY : 0.004 684
REMARK 3 DIHEDRAL : 12.725 1460
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 28
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 40:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5212 18.6197 7.1791
REMARK 3 T TENSOR
REMARK 3 T11: 0.2443 T22: 0.3719
REMARK 3 T33: 0.5114 T12: -0.0047
REMARK 3 T13: -0.0628 T23: -0.1039
REMARK 3 L TENSOR
REMARK 3 L11: 1.8427 L22: 6.3164
REMARK 3 L33: 7.2187 L12: -0.7786
REMARK 3 L13: -0.5992 L23: -6.1123
REMARK 3 S TENSOR
REMARK 3 S11: -0.2135 S12: 0.2240 S13: -0.9648
REMARK 3 S21: 0.1539 S22: 0.4520 S23: 0.5318
REMARK 3 S31: 0.1984 S32: -1.2539 S33: 0.5269
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 52:68)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9546 28.5172 13.2217
REMARK 3 T TENSOR
REMARK 3 T11: 0.1978 T22: 0.1668
REMARK 3 T33: 0.3183 T12: -0.0213
REMARK 3 T13: -0.0086 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.8928 L22: 3.3560
REMARK 3 L33: 3.5702 L12: -1.3345
REMARK 3 L13: -0.4715 L23: -1.4046
REMARK 3 S TENSOR
REMARK 3 S11: 0.0782 S12: -0.0263 S13: -0.2758
REMARK 3 S21: 0.2290 S22: -0.1242 S23: 0.2176
REMARK 3 S31: -0.1167 S32: 0.0503 S33: 0.0517
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 69:79)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9641 36.8352 -4.8412
REMARK 3 T TENSOR
REMARK 3 T11: 0.2200 T22: 0.1998
REMARK 3 T33: 0.2810 T12: 0.0566
REMARK 3 T13: 0.0391 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 3.5550 L22: 3.2945
REMARK 3 L33: 9.7788 L12: -0.1622
REMARK 3 L13: -0.9881 L23: -1.9660
REMARK 3 S TENSOR
REMARK 3 S11: 0.1688 S12: -0.1565 S13: 0.1701
REMARK 3 S21: -0.0576 S22: 0.0255 S23: 0.0010
REMARK 3 S31: -0.0418 S32: -0.0334 S33: -0.0955
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 80:102)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2626 40.8618 -22.7562
REMARK 3 T TENSOR
REMARK 3 T11: 0.3154 T22: 0.1892
REMARK 3 T33: 0.2922 T12: 0.0918
REMARK 3 T13: 0.0427 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 1.7171 L22: 0.7546
REMARK 3 L33: 2.0374 L12: 0.3495
REMARK 3 L13: 0.7712 L23: -0.2868
REMARK 3 S TENSOR
REMARK 3 S11: 0.1306 S12: 0.1857 S13: 0.4087
REMARK 3 S21: -0.2126 S22: -0.1251 S23: -0.0653
REMARK 3 S31: -0.2695 S32: -0.1415 S33: 0.0658
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 103:113)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9328 35.8975 -8.5809
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.1965
REMARK 3 T33: 0.2441 T12: 0.0159
REMARK 3 T13: 0.0314 T23: -0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 2.2856 L22: 3.2418
REMARK 3 L33: 9.7084 L12: 0.9609
REMARK 3 L13: -1.4222 L23: -4.0807
REMARK 3 S TENSOR
REMARK 3 S11: 0.1675 S12: -0.0343 S13: -0.0367
REMARK 3 S21: 0.1125 S22: 0.0359 S23: -0.0462
REMARK 3 S31: -0.3278 S32: -0.0564 S33: -0.2568
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 114:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2692 24.7381 13.0770
REMARK 3 T TENSOR
REMARK 3 T11: 0.2320 T22: 0.1325
REMARK 3 T33: 0.2186 T12: -0.0125
REMARK 3 T13: 0.0176 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.1516 L22: 1.5517
REMARK 3 L33: 2.8913 L12: -0.4210
REMARK 3 L13: -1.1620 L23: -1.6024
REMARK 3 S TENSOR
REMARK 3 S11: -0.1291 S12: -0.2282 S13: -0.0360
REMARK 3 S21: -0.0603 S22: -0.0372 S23: -0.1136
REMARK 3 S31: 0.1108 S32: 0.2501 S33: 0.1671
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 135:148)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0777 14.9929 5.1294
REMARK 3 T TENSOR
REMARK 3 T11: 0.2483 T22: 0.1493
REMARK 3 T33: 0.3371 T12: 0.0267
REMARK 3 T13: -0.0111 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 3.8036 L22: 3.6862
REMARK 3 L33: 7.8395 L12: -1.0665
REMARK 3 L13: -3.3147 L23: 1.4118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: -0.1234 S13: -0.5105
REMARK 3 S21: -0.0339 S22: -0.1921 S23: 0.2484
REMARK 3 S31: 0.4426 S32: 0.0045 S33: 0.1571
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 40:51)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3028 22.2687 -25.3283
REMARK 3 T TENSOR
REMARK 3 T11: 0.2325 T22: 0.2499
REMARK 3 T33: 0.3319 T12: -0.0421
REMARK 3 T13: -0.0088 T23: 0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 5.7968 L22: 5.6914
REMARK 3 L33: 3.6379 L12: 0.6453
REMARK 3 L13: 0.9337 L23: 1.2839
REMARK 3 S TENSOR
REMARK 3 S11: 0.2930 S12: -0.3563 S13: -0.3286
REMARK 3 S21: 0.2026 S22: -0.2145 S23: -0.3726
REMARK 3 S31: 0.4947 S32: -0.3583 S33: 0.2380
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 52:66)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2411 19.9300 -33.5029
REMARK 3 T TENSOR
REMARK 3 T11: 0.3200 T22: 0.1287
REMARK 3 T33: 0.3608 T12: -0.0017
REMARK 3 T13: 0.0267 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 2.4254 L22: 2.8944
REMARK 3 L33: 8.4325 L12: -0.6583
REMARK 3 L13: 1.2746 L23: 1.3437
REMARK 3 S TENSOR
REMARK 3 S11: -0.2168 S12: 0.0803 S13: -0.3715
REMARK 3 S21: -0.3421 S22: -0.0912 S23: 0.1027
REMARK 3 S31: 0.0039 S32: -0.0493 S33: 0.3846
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 67:74)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4705 20.8187 -17.2498
REMARK 3 T TENSOR
REMARK 3 T11: 0.3170 T22: 0.3256
REMARK 3 T33: 0.2585 T12: 0.0730
REMARK 3 T13: 0.0171 T23: 0.0268
REMARK 3 L TENSOR
REMARK 3 L11: 5.9684 L22: 8.1231
REMARK 3 L33: 2.0436 L12: -0.3950
REMARK 3 L13: 2.0714 L23: 1.7846
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.2198 S13: 0.1057
REMARK 3 S21: 0.1606 S22: 0.1784 S23: 0.0692
REMARK 3 S31: 0.4768 S32: 0.3072 S33: -0.0538
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 75:102)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4988 23.1503 3.0675
REMARK 3 T TENSOR
REMARK 3 T11: 0.2597 T22: 0.1404
REMARK 3 T33: 0.2429 T12: 0.0352
REMARK 3 T13: -0.0006 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.7528 L22: 2.2298
REMARK 3 L33: 3.7812 L12: -0.1848
REMARK 3 L13: 0.2349 L23: -0.6451
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: 0.0598 S13: 0.0285
REMARK 3 S21: -0.1115 S22: -0.2034 S23: -0.0255
REMARK 3 S31: 0.3950 S32: 0.2296 S33: 0.1656
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 103:113)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2342 29.7170 -8.5849
REMARK 3 T TENSOR
REMARK 3 T11: 0.2508 T22: 0.1128
REMARK 3 T33: 0.2949 T12: -0.0164
REMARK 3 T13: 0.0004 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 4.8756 L22: 1.2487
REMARK 3 L33: 4.3046 L12: 0.0294
REMARK 3 L13: 4.4597 L23: 0.1892
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: 0.3973 S13: -0.1417
REMARK 3 S21: 0.1159 S22: 0.0719 S23: -0.2416
REMARK 3 S31: -0.2323 S32: 0.4793 S33: 0.0500
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN B AND RESID 114:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2171 30.5440 -25.3851
REMARK 3 T TENSOR
REMARK 3 T11: 0.1976 T22: 0.2122
REMARK 3 T33: 0.2832 T12: 0.0054
REMARK 3 T13: 0.0169 T23: 0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 2.9588 L22: 1.2963
REMARK 3 L33: 9.0751 L12: 1.6813
REMARK 3 L13: 3.3522 L23: 1.9072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0781 S12: 0.3619 S13: 0.0944
REMARK 3 S21: 0.0567 S22: 0.2079 S23: 0.3679
REMARK 3 S31: -0.0177 S32: 0.6628 S33: -0.2543
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN B AND RESID 125:148)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8124 31.1411 -28.8844
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.2265
REMARK 3 T33: 0.2208 T12: 0.0222
REMARK 3 T13: -0.0097 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 2.1259 L22: 2.2533
REMARK 3 L33: 4.8542 L12: 0.3289
REMARK 3 L13: 0.4479 L23: -0.2116
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.2692 S13: -0.2166
REMARK 3 S21: 0.0441 S22: -0.0114 S23: 0.2069
REMARK 3 S31: 0.1850 S32: -0.3445 S33: 0.0357
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 40:50)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0631 45.3623 21.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.3126 T22: 0.2977
REMARK 3 T33: 0.6946 T12: 0.0002
REMARK 3 T13: 0.0123 T23: -0.1602
REMARK 3 L TENSOR
REMARK 3 L11: 4.0460 L22: 3.6245
REMARK 3 L33: 5.7198 L12: -2.7966
REMARK 3 L13: 1.9218 L23: -4.1715
REMARK 3 S TENSOR
REMARK 3 S11: -0.0418 S12: -0.3364 S13: 0.5434
REMARK 3 S21: 0.3203 S22: 0.1040 S23: 1.0527
REMARK 3 S31: -0.7615 S32: 0.0145 S33: -0.1629
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 51:65)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9458 37.2730 11.7510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1903 T22: 0.1292
REMARK 3 T33: 0.3263 T12: 0.0271
REMARK 3 T13: -0.0096 T23: -0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 2.3075 L22: 4.1041
REMARK 3 L33: 5.0128 L12: -0.3507
REMARK 3 L13: 2.5145 L23: -2.6883
REMARK 3 S TENSOR
REMARK 3 S11: -0.0596 S12: -0.3008 S13: 0.5529
REMARK 3 S21: -0.2585 S22: 0.0489 S23: 0.1761
REMARK 3 S31: -0.1756 S32: -0.3520 S33: -0.0256
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 66:74)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0792 29.4058 27.2104
REMARK 3 T TENSOR
REMARK 3 T11: 0.2706 T22: 0.1625
REMARK 3 T33: 0.2686 T12: -0.0305
REMARK 3 T13: 0.0110 T23: -0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 5.3748 L22: 0.2147
REMARK 3 L33: 6.2399 L12: 0.0048
REMARK 3 L13: 3.4601 L23: -0.9251
REMARK 3 S TENSOR
REMARK 3 S11: -0.1025 S12: -0.1366 S13: 0.1831
REMARK 3 S21: 0.0322 S22: -0.0119 S23: -0.4885
REMARK 3 S31: 0.5498 S32: -0.7905 S33: 0.1707
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 75:92)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8773 26.0419 46.3901
REMARK 3 T TENSOR
REMARK 3 T11: 0.2583 T22: 0.2076
REMARK 3 T33: 0.2328 T12: -0.0157
REMARK 3 T13: -0.0036 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 1.2915 L22: 1.9160
REMARK 3 L33: 8.8327 L12: 0.6335
REMARK 3 L13: -0.6558 L23: -0.1063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0926 S12: 0.0890 S13: 0.0432
REMARK 3 S21: 0.1949 S22: 0.0218 S23: -0.0999
REMARK 3 S31: 0.0289 S32: -0.5281 S33: -0.1653
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN C AND RESID 93:103)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9934 24.5593 48.4639
REMARK 3 T TENSOR
REMARK 3 T11: 0.3323 T22: 0.1118
REMARK 3 T33: 0.2893 T12: -0.0290
REMARK 3 T13: -0.0266 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 1.0032 L22: 2.0777
REMARK 3 L33: 3.7297 L12: -0.3479
REMARK 3 L13: 0.4668 L23: 0.9151
REMARK 3 S TENSOR
REMARK 3 S11: -0.1172 S12: -0.0185 S13: -0.0370
REMARK 3 S21: 0.1675 S22: 0.2667 S23: -0.0623
REMARK 3 S31: 0.1638 S32: 0.1482 S33: -0.1996
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN C AND RESID 104:116)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6638 31.0491 32.6360
REMARK 3 T TENSOR
REMARK 3 T11: 0.2961 T22: 0.0281
REMARK 3 T33: 0.3678 T12: 0.0146
REMARK 3 T13: -0.0108 T23: 0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.2045 L22: 0.3938
REMARK 3 L33: 0.7990 L12: 0.0577
REMARK 3 L13: -0.0592 L23: -0.1336
REMARK 3 S TENSOR
REMARK 3 S11: -0.0378 S12: -0.0015 S13: -0.1202
REMARK 3 S21: 0.0731 S22: -0.0013 S23: 0.0135
REMARK 3 S31: 0.1386 S32: -0.0028 S33: -0.1171
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN C AND RESID 117:148)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1776 44.9912 16.4110
REMARK 3 T TENSOR
REMARK 3 T11: 0.2727 T22: 0.0864
REMARK 3 T33: 0.3437 T12: 0.0309
REMARK 3 T13: -0.0190 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.4666 L22: 2.5233
REMARK 3 L33: 2.4233 L12: 0.1805
REMARK 3 L13: 0.3783 L23: -0.4495
REMARK 3 S TENSOR
REMARK 3 S11: -0.1779 S12: -0.1854 S13: 0.2593
REMARK 3 S21: 0.2340 S22: 0.1061 S23: -0.1331
REMARK 3 S31: -0.4185 S32: -0.2509 S33: -0.0343
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 39:45)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9925 42.4000 48.2495
REMARK 3 T TENSOR
REMARK 3 T11: 0.4990 T22: 0.2033
REMARK 3 T33: 0.6386 T12: 0.0442
REMARK 3 T13: 0.0508 T23: 0.0923
REMARK 3 L TENSOR
REMARK 3 L11: 3.0464 L22: 0.9800
REMARK 3 L33: 6.6518 L12: -0.8553
REMARK 3 L13: 1.2904 L23: -2.2784
REMARK 3 S TENSOR
REMARK 3 S11: -0.3713 S12: 0.2218 S13: 1.2399
REMARK 3 S21: -0.2797 S22: 0.1992 S23: -1.2156
REMARK 3 S31: -0.9623 S32: 0.0154 S33: 0.2634
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 46:54)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0648 46.0732 59.9045
REMARK 3 T TENSOR
REMARK 3 T11: 0.5001 T22: 0.4883
REMARK 3 T33: 0.6740 T12: 0.1221
REMARK 3 T13: 0.0830 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 6.1662 L22: 2.0602
REMARK 3 L33: 5.3786 L12: 3.1073
REMARK 3 L13: 4.9578 L23: 3.3199
REMARK 3 S TENSOR
REMARK 3 S11: -0.3065 S12: -0.3894 S13: 1.9351
REMARK 3 S21: 0.3917 S22: -0.1644 S23: 0.6683
REMARK 3 S31: -0.2674 S32: -0.1803 S33: 0.7020
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN D AND RESID 55:67)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2165 46.2520 58.1189
REMARK 3 T TENSOR
REMARK 3 T11: 0.3860 T22: 0.2633
REMARK 3 T33: 0.3280 T12: 0.0114
REMARK 3 T13: 0.0468 T23: -0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 5.2773 L22: 2.1201
REMARK 3 L33: 8.6199 L12: 0.6969
REMARK 3 L13: -4.1781 L23: -0.7148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0227 S12: -0.2971 S13: 0.7455
REMARK 3 S21: 0.1256 S22: 0.2969 S23: 0.2882
REMARK 3 S31: -0.6127 S32: 0.4763 S33: -0.1266
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN D AND RESID 68:86)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6317 44.6666 36.2664
REMARK 3 T TENSOR
REMARK 3 T11: 0.3590 T22: 0.1502
REMARK 3 T33: 0.3126 T12: -0.0623
REMARK 3 T13: 0.0097 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.2547 L22: 0.9910
REMARK 3 L33: 2.1813 L12: 0.1107
REMARK 3 L13: 0.5276 L23: -1.0747
REMARK 3 S TENSOR
REMARK 3 S11: -0.0811 S12: -0.0077 S13: 0.0680
REMARK 3 S21: 0.2892 S22: -0.2676 S23: -0.0097
REMARK 3 S31: -1.3443 S32: 0.4438 S33: 0.1185
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN D AND RESID 87:104)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1391 38.5033 20.6673
REMARK 3 T TENSOR
REMARK 3 T11: 0.1902 T22: 0.1675
REMARK 3 T33: 0.2775 T12: -0.0361
REMARK 3 T13: 0.0110 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 1.1540 L22: 1.5849
REMARK 3 L33: 3.9777 L12: -0.3783
REMARK 3 L13: -1.0053 L23: 0.2682
REMARK 3 S TENSOR
REMARK 3 S11: -0.1561 S12: 0.1196 S13: 0.2207
REMARK 3 S21: 0.0481 S22: -0.1068 S23: -0.2233
REMARK 3 S31: -0.0173 S32: 0.7410 S33: 0.2898
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN D AND RESID 105:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9009 35.7107 41.9946
REMARK 3 T TENSOR
REMARK 3 T11: 0.2350 T22: 0.0969
REMARK 3 T33: 0.2917 T12: -0.0156
REMARK 3 T13: 0.0071 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.6775 L22: 1.2279
REMARK 3 L33: 7.7031 L12: 0.7238
REMARK 3 L13: 0.5684 L23: -0.6842
REMARK 3 S TENSOR
REMARK 3 S11: -0.1032 S12: -0.0177 S13: 0.1580
REMARK 3 S21: -0.0259 S22: -0.0775 S23: 0.0399
REMARK 3 S31: -0.5301 S32: -0.3278 S33: 0.1065
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN D AND RESID 120:148)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3491 34.9196 55.9683
REMARK 3 T TENSOR
REMARK 3 T11: 0.2169 T22: 0.2686
REMARK 3 T33: 0.2580 T12: 0.0280
REMARK 3 T13: 0.0333 T23: 0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 1.5980 L22: 1.3972
REMARK 3 L33: 3.6120 L12: 0.9424
REMARK 3 L13: 1.6794 L23: 0.6724
REMARK 3 S TENSOR
REMARK 3 S11: -0.1205 S12: -0.0211 S13: 0.0609
REMARK 3 S21: -0.1545 S22: 0.0373 S23: -0.0124
REMARK 3 S31: -0.3645 S32: -0.3766 S33: 0.0916
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 3ZG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1290055087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : HORIZONTALLY DIFFRACTING SI
REMARK 200 (111) MONOCHROMATOR
REMARK 200 OPTICS : PT COATED MIRRORS IN A
REMARK 200 KIRKPATRICK-BAEZ GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39483
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 46.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.97000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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 2Y3H
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16-20% PEG2000MME, 15% GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 39.56250
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 MET A 2
REMARK 465 LYS A 3
REMARK 465 SER A 4
REMARK 465 ARG A 5
REMARK 465 THR A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 SER A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 THR A 13
REMARK 465 LEU A 14
REMARK 465 PHE A 15
REMARK 465 GLY A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 LEU A 19
REMARK 465 GLY A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 VAL A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ALA A 26
REMARK 465 TRP A 27
REMARK 465 LEU A 28
REMARK 465 TYR A 29
REMARK 465 TYR A 30
REMARK 465 SER A 31
REMARK 465 HIS A 32
REMARK 465 ARG A 33
REMARK 465 ASN A 34
REMARK 465 GLU A 35
REMARK 465 ALA A 36
REMARK 465 GLY A 37
REMARK 465 HIS A 38
REMARK 465 GLY A 39
REMARK 465 MET B 1
REMARK 465 MET B 2
REMARK 465 LYS B 3
REMARK 465 SER B 4
REMARK 465 ARG B 5
REMARK 465 THR B 6
REMARK 465 ARG B 7
REMARK 465 ARG B 8
REMARK 465 LEU B 9
REMARK 465 SER B 10
REMARK 465 LEU B 11
REMARK 465 SER B 12
REMARK 465 THR B 13
REMARK 465 LEU B 14
REMARK 465 PHE B 15
REMARK 465 GLY B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 LEU B 19
REMARK 465 GLY B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 VAL B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 ALA B 26
REMARK 465 TRP B 27
REMARK 465 LEU B 28
REMARK 465 TYR B 29
REMARK 465 TYR B 30
REMARK 465 SER B 31
REMARK 465 HIS B 32
REMARK 465 ARG B 33
REMARK 465 ASN B 34
REMARK 465 GLU B 35
REMARK 465 ALA B 36
REMARK 465 GLY B 37
REMARK 465 HIS B 38
REMARK 465 GLY B 39
REMARK 465 MET C 1
REMARK 465 MET C 2
REMARK 465 LYS C 3
REMARK 465 SER C 4
REMARK 465 ARG C 5
REMARK 465 THR C 6
REMARK 465 ARG C 7
REMARK 465 ARG C 8
REMARK 465 LEU C 9
REMARK 465 SER C 10
REMARK 465 LEU C 11
REMARK 465 SER C 12
REMARK 465 THR C 13
REMARK 465 LEU C 14
REMARK 465 PHE C 15
REMARK 465 GLY C 16
REMARK 465 ALA C 17
REMARK 465 LEU C 18
REMARK 465 LEU C 19
REMARK 465 GLY C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 VAL C 23
REMARK 465 ALA C 24
REMARK 465 ALA C 25
REMARK 465 ALA C 26
REMARK 465 TRP C 27
REMARK 465 LEU C 28
REMARK 465 TYR C 29
REMARK 465 TYR C 30
REMARK 465 SER C 31
REMARK 465 HIS C 32
REMARK 465 ARG C 33
REMARK 465 ASN C 34
REMARK 465 GLU C 35
REMARK 465 ALA C 36
REMARK 465 GLY C 37
REMARK 465 HIS C 38
REMARK 465 GLY C 39
REMARK 465 MET D 1
REMARK 465 MET D 2
REMARK 465 LYS D 3
REMARK 465 SER D 4
REMARK 465 ARG D 5
REMARK 465 THR D 6
REMARK 465 ARG D 7
REMARK 465 ARG D 8
REMARK 465 LEU D 9
REMARK 465 SER D 10
REMARK 465 LEU D 11
REMARK 465 SER D 12
REMARK 465 THR D 13
REMARK 465 LEU D 14
REMARK 465 PHE D 15
REMARK 465 GLY D 16
REMARK 465 ALA D 17
REMARK 465 LEU D 18
REMARK 465 LEU D 19
REMARK 465 GLY D 20
REMARK 465 VAL D 21
REMARK 465 SER D 22
REMARK 465 VAL D 23
REMARK 465 ALA D 24
REMARK 465 ALA D 25
REMARK 465 ALA D 26
REMARK 465 TRP D 27
REMARK 465 LEU D 28
REMARK 465 TYR D 29
REMARK 465 TYR D 30
REMARK 465 SER D 31
REMARK 465 HIS D 32
REMARK 465 ARG D 33
REMARK 465 ASN D 34
REMARK 465 GLU D 35
REMARK 465 ALA D 36
REMARK 465 GLY D 37
REMARK 465 HIS D 38
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 LEU A 41 -98.44 -62.84
REMARK 500 HIS A 42 -64.27 15.31
REMARK 500 PRO B 92 69.93 -66.37
REMARK 500 PRO C 92 66.18 -67.06
REMARK 500 PRO C 129 55.11 -68.04
REMARK 500 GLU C 130 -9.31 -167.11
REMARK 500 GLU C 130 -9.45 -167.11
REMARK 500 PRO D 92 76.34 -63.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2037 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH D2038 DISTANCE = 5.86 ANGSTROMS
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 NI A 150 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 42 NE2
REMARK 620 2 GLU A 63 OE2 122.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 150 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 42 NE2
REMARK 620 2 HIS B 46 NE2 92.5
REMARK 620 3 GLU B 63 OE1 100.6 92.8
REMARK 620 4 GLU B 63 OE2 162.5 84.7 62.4
REMARK 620 5 HIS B 119 NE2 94.0 172.9 89.1 90.1
REMARK 620 6 HOH B2003 O 97.7 86.6 161.8 99.4 89.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 150 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 42 NE2
REMARK 620 2 GLU C 63 OE1 94.0
REMARK 620 3 HIS C 119 NE2 108.0 77.7
REMARK 620 4 HOH C2037 O 150.9 93.8 101.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D 150 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 42 NE2
REMARK 620 2 HIS D 46 NE2 79.9
REMARK 620 3 GLU D 63 OE2 145.4 87.4
REMARK 620 4 GLU D 63 OE1 92.2 82.2 54.0
REMARK 620 5 HIS D 119 NE2 85.5 163.3 109.3 106.5
REMARK 620 6 HOH D2002 O 132.5 91.6 79.4 133.1 92.4
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 NI A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1152
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE C 1153
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1150
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Y39 RELATED DB: PDB
REMARK 900 NI-BOUND FORM OF CUPRIAVIDUS METALLIDURANS CH34 CNRXS
REMARK 900 RELATED ID: 2Y3B RELATED DB: PDB
REMARK 900 CO-BOUND FORM OF CUPRIAVIDUS METALLIDURANS CH34 CNRXS
REMARK 900 RELATED ID: 2Y3D RELATED DB: PDB
REMARK 900 ZN-BOUND FORM OF CUPRIAVIDUS METALLIDURANS CH34 CNRXS
REMARK 900 RELATED ID: 2Y3G RELATED DB: PDB
REMARK 900 SE-MET FORM OF CUPRIAVIDUS METALLIDURANS CH34 CNRXS
REMARK 900 RELATED ID: 2Y3H RELATED DB: PDB
REMARK 900 E63Q MUTANT OF CUPRIAVIDUS METALLIDURANS CH34 CNRXS
DBREF 3ZG1 A 1 148 UNP P37975 CNRR_RALME 1 148
DBREF 3ZG1 B 1 148 UNP P37975 CNRR_RALME 1 148
DBREF 3ZG1 C 1 148 UNP P37975 CNRR_RALME 1 148
DBREF 3ZG1 D 1 148 UNP P37975 CNRR_RALME 1 148
SEQADV 3ZG1 ALA A 123 UNP P37975 MET 123 ENGINEERED MUTATION
SEQADV 3ZG1 ALA B 123 UNP P37975 MET 123 ENGINEERED MUTATION
SEQADV 3ZG1 ALA C 123 UNP P37975 MET 123 ENGINEERED MUTATION
SEQADV 3ZG1 ALA D 123 UNP P37975 MET 123 ENGINEERED MUTATION
SEQRES 1 A 148 MET MET LYS SER ARG THR ARG ARG LEU SER LEU SER THR
SEQRES 2 A 148 LEU PHE GLY ALA LEU LEU GLY VAL SER VAL ALA ALA ALA
SEQRES 3 A 148 TRP LEU TYR TYR SER HIS ARG ASN GLU ALA GLY HIS GLY
SEQRES 4 A 148 ASP LEU HIS GLU ILE LEU HIS GLU ALA VAL PRO LEU ASP
SEQRES 5 A 148 ALA ASN GLU ARG GLU ILE LEU GLU LEU LYS GLU ASP ALA
SEQRES 6 A 148 PHE ALA GLN ARG ARG ARG GLU ILE GLU THR ARG LEU ARG
SEQRES 7 A 148 ALA ALA ASN GLY LYS LEU ALA ASP ALA ILE ALA LYS ASN
SEQRES 8 A 148 PRO ALA TRP SER PRO GLU VAL GLU ALA ALA THR GLN GLU
SEQRES 9 A 148 VAL GLU ARG ALA ALA GLY ASP LEU GLN ARG ALA THR LEU
SEQRES 10 A 148 VAL HIS VAL PHE GLU ALA ARG ALA GLY LEU LYS PRO GLU
SEQRES 11 A 148 HIS ARG PRO ALA TYR ASP ARG VAL LEU ILE ASP ALA LEU
SEQRES 12 A 148 ARG ARG GLY SER GLN
SEQRES 1 B 148 MET MET LYS SER ARG THR ARG ARG LEU SER LEU SER THR
SEQRES 2 B 148 LEU PHE GLY ALA LEU LEU GLY VAL SER VAL ALA ALA ALA
SEQRES 3 B 148 TRP LEU TYR TYR SER HIS ARG ASN GLU ALA GLY HIS GLY
SEQRES 4 B 148 ASP LEU HIS GLU ILE LEU HIS GLU ALA VAL PRO LEU ASP
SEQRES 5 B 148 ALA ASN GLU ARG GLU ILE LEU GLU LEU LYS GLU ASP ALA
SEQRES 6 B 148 PHE ALA GLN ARG ARG ARG GLU ILE GLU THR ARG LEU ARG
SEQRES 7 B 148 ALA ALA ASN GLY LYS LEU ALA ASP ALA ILE ALA LYS ASN
SEQRES 8 B 148 PRO ALA TRP SER PRO GLU VAL GLU ALA ALA THR GLN GLU
SEQRES 9 B 148 VAL GLU ARG ALA ALA GLY ASP LEU GLN ARG ALA THR LEU
SEQRES 10 B 148 VAL HIS VAL PHE GLU ALA ARG ALA GLY LEU LYS PRO GLU
SEQRES 11 B 148 HIS ARG PRO ALA TYR ASP ARG VAL LEU ILE ASP ALA LEU
SEQRES 12 B 148 ARG ARG GLY SER GLN
SEQRES 1 C 148 MET MET LYS SER ARG THR ARG ARG LEU SER LEU SER THR
SEQRES 2 C 148 LEU PHE GLY ALA LEU LEU GLY VAL SER VAL ALA ALA ALA
SEQRES 3 C 148 TRP LEU TYR TYR SER HIS ARG ASN GLU ALA GLY HIS GLY
SEQRES 4 C 148 ASP LEU HIS GLU ILE LEU HIS GLU ALA VAL PRO LEU ASP
SEQRES 5 C 148 ALA ASN GLU ARG GLU ILE LEU GLU LEU LYS GLU ASP ALA
SEQRES 6 C 148 PHE ALA GLN ARG ARG ARG GLU ILE GLU THR ARG LEU ARG
SEQRES 7 C 148 ALA ALA ASN GLY LYS LEU ALA ASP ALA ILE ALA LYS ASN
SEQRES 8 C 148 PRO ALA TRP SER PRO GLU VAL GLU ALA ALA THR GLN GLU
SEQRES 9 C 148 VAL GLU ARG ALA ALA GLY ASP LEU GLN ARG ALA THR LEU
SEQRES 10 C 148 VAL HIS VAL PHE GLU ALA ARG ALA GLY LEU LYS PRO GLU
SEQRES 11 C 148 HIS ARG PRO ALA TYR ASP ARG VAL LEU ILE ASP ALA LEU
SEQRES 12 C 148 ARG ARG GLY SER GLN
SEQRES 1 D 148 MET MET LYS SER ARG THR ARG ARG LEU SER LEU SER THR
SEQRES 2 D 148 LEU PHE GLY ALA LEU LEU GLY VAL SER VAL ALA ALA ALA
SEQRES 3 D 148 TRP LEU TYR TYR SER HIS ARG ASN GLU ALA GLY HIS GLY
SEQRES 4 D 148 ASP LEU HIS GLU ILE LEU HIS GLU ALA VAL PRO LEU ASP
SEQRES 5 D 148 ALA ASN GLU ARG GLU ILE LEU GLU LEU LYS GLU ASP ALA
SEQRES 6 D 148 PHE ALA GLN ARG ARG ARG GLU ILE GLU THR ARG LEU ARG
SEQRES 7 D 148 ALA ALA ASN GLY LYS LEU ALA ASP ALA ILE ALA LYS ASN
SEQRES 8 D 148 PRO ALA TRP SER PRO GLU VAL GLU ALA ALA THR GLN GLU
SEQRES 9 D 148 VAL GLU ARG ALA ALA GLY ASP LEU GLN ARG ALA THR LEU
SEQRES 10 D 148 VAL HIS VAL PHE GLU ALA ARG ALA GLY LEU LYS PRO GLU
SEQRES 11 D 148 HIS ARG PRO ALA TYR ASP ARG VAL LEU ILE ASP ALA LEU
SEQRES 12 D 148 ARG ARG GLY SER GLN
HET PEG A1149 7
HET NI A 150 1
HET PEG A1150 7
HET PEG A1151 7
HET CL B1149 1
HET CL B1150 1
HET NI B 150 1
HET GOL C1149 6
HET NI C 150 1
HET GOL C1150 6
HET GOL C1151 12
HET PEG C1152 7
HET PGE C1153 10
HET NI D 150 1
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NI NICKEL (II) ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 PEG 4(C4 H10 O3)
FORMUL 6 NI 4(NI 2+)
FORMUL 9 CL 2(CL 1-)
FORMUL 12 GOL 3(C3 H8 O3)
FORMUL 17 PGE C6 H14 O4
FORMUL 19 HOH *186(H2 O)
HELIX 1 1 ASP A 52 ASN A 91 1 40
HELIX 2 2 SER A 95 GLY A 126 1 32
HELIX 3 3 LYS A 128 GLU A 130 5 3
HELIX 4 4 HIS A 131 GLY A 146 1 16
HELIX 5 5 ASP B 40 VAL B 49 1 10
HELIX 6 6 ASP B 52 LEU B 59 1 8
HELIX 7 7 LEU B 59 ASN B 91 1 33
HELIX 8 8 SER B 95 GLY B 126 1 32
HELIX 9 9 HIS B 131 GLY B 146 1 16
HELIX 10 10 ASP C 40 HIS C 46 1 7
HELIX 11 11 ASP C 52 ASN C 91 1 40
HELIX 12 12 SER C 95 GLY C 126 1 32
HELIX 13 13 HIS C 131 ARG C 145 1 15
HELIX 14 14 ASP D 40 VAL D 49 1 10
HELIX 15 15 ASP D 52 ASN D 91 1 40
HELIX 16 16 SER D 95 GLY D 126 1 32
HELIX 17 17 HIS D 131 ARG D 145 1 15
HELIX 18 18 GLY D 146 GLN D 148 5 3
LINK NE2 HIS A 42 NI NI A 150 1555 1555 2.35
LINK OE2 GLU A 63 NI NI A 150 1555 1555 1.79
LINK NE2 HIS B 42 NI NI B 150 1555 1555 2.01
LINK NE2 HIS B 46 NI NI B 150 1555 1555 2.20
LINK OE1 GLU B 63 NI NI B 150 1555 1555 2.28
LINK OE2 GLU B 63 NI NI B 150 1555 1555 1.92
LINK NE2 HIS B 119 NI NI B 150 1555 1555 2.12
LINK NI NI B 150 O HOH B2003 1555 1555 2.20
LINK NE2 HIS C 42 NI NI C 150 1555 1555 2.05
LINK OE1 GLU C 63 NI NI C 150 1555 1555 2.31
LINK NE2 HIS C 119 NI NI C 150 1555 1555 2.39
LINK NI NI C 150 O HOH C2037 1555 1555 2.77
LINK NE2 HIS D 42 NI NI D 150 1555 1555 2.53
LINK NE2 HIS D 46 NI NI D 150 1555 1555 1.98
LINK OE2 GLU D 63 NI NI D 150 1555 1555 2.18
LINK OE1 GLU D 63 NI NI D 150 1555 1555 2.59
LINK NE2 HIS D 119 NI NI D 150 1555 1555 1.95
LINK NI NI D 150 O HOH D2002 1555 1555 2.52
SITE 1 AC1 3 HIS A 42 GLU A 63 HIS A 119
SITE 1 AC2 5 HIS B 42 HIS B 46 GLU B 63 HIS B 119
SITE 2 AC2 5 HOH B2003
SITE 1 AC3 4 HIS C 42 GLU C 63 HIS C 119 HOH C2037
SITE 1 AC4 5 HIS D 42 HIS D 46 GLU D 63 HIS D 119
SITE 2 AC4 5 HOH D2002
SITE 1 AC5 7 ARG A 71 ASN C 54 ALA C 125 GLY C 126
SITE 2 AC5 7 LEU C 127 LYS C 128 HOH C2004
SITE 1 AC6 6 GLU A 57 PHE C 66 GLU C 122 HOH C2009
SITE 2 AC6 6 HOH C2011 HOH C2025
SITE 1 AC7 7 GLU A 60 HOH A2014 ASN B 91 TRP B 94
SITE 2 AC7 7 SER B 95 LYS C 62 GLU C 122
SITE 1 AC8 8 LEU A 61 LYS A 62 ALA A 65 HOH A2017
SITE 2 AC8 8 PGE C1153 ASN D 91 ALA D 93 TRP D 94
SITE 1 AC9 7 GLU A 106 ARG A 107 GLY A 110 ASP A 111
SITE 2 AC9 7 HOH A2062 GLU B 106 ARG B 107
SITE 1 BC1 3 ARG C 76 GLU C 104 ARG C 107
SITE 1 BC2 9 HIS A 46 GLU A 47 GLU A 60 GLU A 63
SITE 2 BC2 9 HOH A2005 HOH A2006 LYS B 90 SER B 95
SITE 3 BC2 9 GLU B 97
SITE 1 BC3 7 PHE A 66 ARG A 69 ALA A 115 GLU A 122
SITE 2 BC3 7 PEG A1149 GLU C 57 HOH C2006
SITE 1 BC4 1 GLN B 113
SITE 1 BC5 3 ARG B 137 HOH B2022 ARG D 124
CRYST1 31.846 79.125 93.475 90.00 90.10 90.00 P 1 21 1 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 0.031401 0.000000 0.000055 0.00000
SCALE2 0.000000 0.012638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010698 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
