| content |
HEADER HYDROLASE 30-MAR-23 8S9R
TITLE SAL2, STAPHYLOCOCCUS AUREUS LIPASE 2 (GEH, LIP2), APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL GPG FROM EXPRESSION TAG;
COMPND 5 SYNONYM: GLYCEROL ESTER HYDROLASE 2;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS USA100-CA-126;
SOURCE 3 ORGANISM_TAXID: 1385546;
SOURCE 4 GENE: LIP2, GEH, SAOUHSC_00300;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: F1002
KEYWDS SAL2, STAPHYLOCOCCUS AUREUS, S. AUREUS, FLUOROPHOSPHONATE-BINDING,
KEYWDS 2 SERINE HYDROLASES, LIPASE, GEH, SAL3, LIP2, YP-042422.1,
KEYWDS 3 WP_000943814.1, SAOUHSC_00300, Q2G155, SAUSA300_0320, NWMN_0262,
KEYWDS 4 SACOL0317, SACOL0390, SA0309, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.FELLNER
REVDAT 1 10-APR-24 8S9R 0
JRNL AUTH M.FELLNER
JRNL TITL SAL2, STAPHYLOCOCCUS AUREUS LIPASE 2 (GEH, LIP2), APO FORM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 66288
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 3232
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 47.5800 - 7.3800 1.00 2995 168 0.1741 0.2069
REMARK 3 2 7.3800 - 5.8600 1.00 2835 153 0.1781 0.1959
REMARK 3 3 5.8600 - 5.1200 1.00 2817 135 0.1751 0.1994
REMARK 3 4 5.1200 - 4.6500 1.00 2778 145 0.1567 0.2090
REMARK 3 5 4.6500 - 4.3200 1.00 2751 151 0.1544 0.1551
REMARK 3 6 4.3200 - 4.0700 1.00 2741 152 0.1616 0.1845
REMARK 3 7 4.0700 - 3.8600 1.00 2777 125 0.1993 0.2224
REMARK 3 8 3.8600 - 3.7000 1.00 2710 153 0.1942 0.2151
REMARK 3 9 3.6900 - 3.5500 1.00 2741 144 0.2074 0.2193
REMARK 3 10 3.5500 - 3.4300 1.00 2736 138 0.2153 0.2488
REMARK 3 11 3.4300 - 3.3200 1.00 2703 135 0.2161 0.2371
REMARK 3 12 3.3200 - 3.2300 1.00 2719 140 0.2540 0.2961
REMARK 3 13 3.2300 - 3.1400 1.00 2693 149 0.2645 0.2551
REMARK 3 14 3.1400 - 3.0700 1.00 2744 122 0.2482 0.2768
REMARK 3 15 3.0700 - 3.0000 1.00 2712 145 0.2407 0.2537
REMARK 3 16 3.0000 - 2.9300 1.00 2718 110 0.2348 0.2917
REMARK 3 17 2.9300 - 2.8700 1.00 2703 142 0.2530 0.2728
REMARK 3 18 2.8700 - 2.8200 1.00 2701 138 0.2381 0.2890
REMARK 3 19 2.8200 - 2.7700 1.00 2712 140 0.2563 0.2801
REMARK 3 20 2.7700 - 2.7200 1.00 2694 135 0.2792 0.3160
REMARK 3 21 2.7200 - 2.6800 1.00 2662 145 0.3078 0.3561
REMARK 3 22 2.6800 - 2.6400 1.00 2711 138 0.3324 0.3989
REMARK 3 23 2.6400 - 2.6000 0.99 2703 129 0.3766 0.3548
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.860
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: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 6215
REMARK 3 ANGLE : 0.952 8427
REMARK 3 CHIRALITY : 0.053 875
REMARK 3 PLANARITY : 0.008 1097
REMARK 3 DIHEDRAL : 15.255 2236
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.7579 -44.1520 -18.8913
REMARK 3 T TENSOR
REMARK 3 T11: 0.4852 T22: 0.4438
REMARK 3 T33: 0.4693 T12: 0.0817
REMARK 3 T13: 0.0227 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 2.5357 L22: 1.5499
REMARK 3 L33: 1.9671 L12: 0.0864
REMARK 3 L13: -0.1428 L23: -0.1157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0813 S12: 0.2964 S13: -0.3408
REMARK 3 S21: -0.2734 S22: -0.0879 S23: -0.1552
REMARK 3 S31: 0.3352 S32: 0.1030 S33: 0.0091
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 110 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.8790 -38.5320 -12.2285
REMARK 3 T TENSOR
REMARK 3 T11: 0.3960 T22: 0.3368
REMARK 3 T33: 0.4149 T12: 0.0293
REMARK 3 T13: 0.0328 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 4.7648 L22: 2.2228
REMARK 3 L33: 3.0325 L12: 0.4806
REMARK 3 L13: -1.4678 L23: 0.5888
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: 0.2142 S13: 0.1944
REMARK 3 S21: -0.2579 S22: 0.0289 S23: 0.1673
REMARK 3 S31: -0.0776 S32: -0.3672 S33: -0.0163
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 152 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4669 -27.4898 -20.1902
REMARK 3 T TENSOR
REMARK 3 T11: 0.4478 T22: 0.4566
REMARK 3 T33: 0.5343 T12: 0.0766
REMARK 3 T13: 0.0495 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 0.9595 L22: 0.8047
REMARK 3 L33: 1.8761 L12: 0.0622
REMARK 3 L13: 0.0858 L23: -0.6285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: 0.0333 S13: 0.1231
REMARK 3 S21: 0.0324 S22: 0.0724 S23: 0.1551
REMARK 3 S31: -0.2720 S32: -0.2116 S33: -0.0111
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 244 THROUGH 315 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.5326 -32.6613 0.3030
REMARK 3 T TENSOR
REMARK 3 T11: 0.4254 T22: 0.5217
REMARK 3 T33: 0.4146 T12: 0.0918
REMARK 3 T13: -0.0212 T23: -0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 6.4417 L22: 4.7056
REMARK 3 L33: 1.6614 L12: 3.5541
REMARK 3 L13: -1.4525 L23: -0.6152
REMARK 3 S TENSOR
REMARK 3 S11: 0.2315 S12: -0.6338 S13: 0.0217
REMARK 3 S21: 0.2932 S22: -0.2367 S23: -0.4150
REMARK 3 S31: -0.0547 S32: 0.3347 S33: 0.0071
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 316 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.2178 -46.7393 6.0206
REMARK 3 T TENSOR
REMARK 3 T11: 0.4640 T22: 0.5304
REMARK 3 T33: 0.4660 T12: 0.0350
REMARK 3 T13: 0.0757 T23: 0.0986
REMARK 3 L TENSOR
REMARK 3 L11: 6.9842 L22: 7.7605
REMARK 3 L33: 9.1083 L12: 5.6307
REMARK 3 L13: 2.9842 L23: 0.3865
REMARK 3 S TENSOR
REMARK 3 S11: 0.2923 S12: -0.4781 S13: -0.8093
REMARK 3 S21: 0.2582 S22: -0.0911 S23: -0.3782
REMARK 3 S31: 0.8414 S32: 0.0037 S33: -0.2466
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 363 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.6267 -42.7867 -4.9712
REMARK 3 T TENSOR
REMARK 3 T11: 0.5034 T22: 0.6023
REMARK 3 T33: 0.6783 T12: 0.1526
REMARK 3 T13: -0.0118 T23: 0.0590
REMARK 3 L TENSOR
REMARK 3 L11: 0.3630 L22: 2.7403
REMARK 3 L33: 6.3879 L12: 0.8251
REMARK 3 L13: -1.2469 L23: -1.5161
REMARK 3 S TENSOR
REMARK 3 S11: -0.2471 S12: -0.5583 S13: -0.3242
REMARK 3 S21: -0.1227 S22: -0.1328 S23: -0.8262
REMARK 3 S31: 0.4320 S32: 1.4123 S33: 0.3624
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 364 THROUGH 385 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.0724 -55.7633 -4.9735
REMARK 3 T TENSOR
REMARK 3 T11: 0.5871 T22: 0.4472
REMARK 3 T33: 0.6566 T12: 0.1208
REMARK 3 T13: -0.0370 T23: 0.0733
REMARK 3 L TENSOR
REMARK 3 L11: 6.2599 L22: 3.9547
REMARK 3 L33: 4.0383 L12: 3.8836
REMARK 3 L13: -2.0530 L23: -0.5278
REMARK 3 S TENSOR
REMARK 3 S11: 0.2273 S12: -0.5242 S13: -1.0036
REMARK 3 S21: 0.3369 S22: -0.3977 S23: -0.3994
REMARK 3 S31: 0.6333 S32: 0.4787 S33: 0.1827
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7761 -20.4401 -25.7630
REMARK 3 T TENSOR
REMARK 3 T11: 0.4151 T22: 0.5877
REMARK 3 T33: 0.4404 T12: -0.0769
REMARK 3 T13: -0.0231 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 3.5956 L22: 2.7301
REMARK 3 L33: 6.3194 L12: 0.2882
REMARK 3 L13: -0.2600 L23: 1.2856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0326 S12: 0.0165 S13: 0.3753
REMARK 3 S21: -0.2949 S22: 0.0380 S23: -0.1995
REMARK 3 S31: -0.6673 S32: 0.7335 S33: -0.0148
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 89 THROUGH 131 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4947 -21.1386 -28.8912
REMARK 3 T TENSOR
REMARK 3 T11: 0.5314 T22: 0.9626
REMARK 3 T33: 0.5667 T12: -0.1726
REMARK 3 T13: 0.0240 T23: -0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 2.8091 L22: 1.8091
REMARK 3 L33: 5.4824 L12: -0.4832
REMARK 3 L13: -0.8279 L23: -1.0945
REMARK 3 S TENSOR
REMARK 3 S11: -0.0861 S12: 0.0469 S13: 0.4136
REMARK 3 S21: -0.1662 S22: -0.0344 S23: -0.5459
REMARK 3 S31: -0.5628 S32: 1.3649 S33: 0.0868
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 132 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8666 -25.7191 -41.9786
REMARK 3 T TENSOR
REMARK 3 T11: 0.6210 T22: 1.3350
REMARK 3 T33: 0.7533 T12: -0.0877
REMARK 3 T13: 0.1203 T23: -0.1087
REMARK 3 L TENSOR
REMARK 3 L11: 5.2557 L22: 3.6170
REMARK 3 L33: 3.8036 L12: 0.1743
REMARK 3 L13: -0.2814 L23: 0.9228
REMARK 3 S TENSOR
REMARK 3 S11: -0.0581 S12: 0.9443 S13: -0.4512
REMARK 3 S21: -0.5500 S22: -0.1773 S23: -0.5758
REMARK 3 S31: -0.0878 S32: 1.0789 S33: 0.2664
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 152 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2639 -32.2297 -22.9747
REMARK 3 T TENSOR
REMARK 3 T11: 0.4755 T22: 1.0461
REMARK 3 T33: 0.5984 T12: 0.0686
REMARK 3 T13: -0.0276 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.3363 L22: 1.4861
REMARK 3 L33: 2.1480 L12: -0.2971
REMARK 3 L13: -0.1619 L23: -0.3036
REMARK 3 S TENSOR
REMARK 3 S11: 0.1255 S12: -0.2562 S13: -0.2817
REMARK 3 S21: -0.1386 S22: -0.2191 S23: -0.4329
REMARK 3 S31: -0.1067 S32: 0.9765 S33: 0.0791
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 182 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7264 -30.2400 -40.9418
REMARK 3 T TENSOR
REMARK 3 T11: 0.3659 T22: 0.4441
REMARK 3 T33: 0.4633 T12: 0.0025
REMARK 3 T13: 0.0024 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 4.2916 L22: 4.3406
REMARK 3 L33: 7.2617 L12: 3.7702
REMARK 3 L13: -1.3715 L23: 1.4341
REMARK 3 S TENSOR
REMARK 3 S11: -0.1383 S12: 0.1697 S13: 0.4463
REMARK 3 S21: -0.6382 S22: 0.2672 S23: 0.1626
REMARK 3 S31: -0.3867 S32: 0.5525 S33: -0.1232
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 219 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9232 -36.6036 -42.1394
REMARK 3 T TENSOR
REMARK 3 T11: 0.5003 T22: 0.5219
REMARK 3 T33: 0.5449 T12: 0.0278
REMARK 3 T13: 0.0496 T23: -0.0832
REMARK 3 L TENSOR
REMARK 3 L11: 2.1978 L22: 2.6264
REMARK 3 L33: 9.3028 L12: 0.9131
REMARK 3 L13: 1.3628 L23: -1.0280
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: 0.3908 S13: -0.3567
REMARK 3 S21: -0.4965 S22: 0.1710 S23: -0.1670
REMARK 3 S31: 0.9072 S32: 1.0408 S33: -0.1489
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 244 THROUGH 285 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1939 -37.8168 -15.0724
REMARK 3 T TENSOR
REMARK 3 T11: 0.4410 T22: 0.9118
REMARK 3 T33: 0.5718 T12: 0.1816
REMARK 3 T13: -0.0918 T23: 0.0994
REMARK 3 L TENSOR
REMARK 3 L11: 4.0759 L22: 3.2837
REMARK 3 L33: 3.7215 L12: 1.4949
REMARK 3 L13: -0.8025 L23: 0.7070
REMARK 3 S TENSOR
REMARK 3 S11: 0.1601 S12: -0.4706 S13: -0.4233
REMARK 3 S21: 0.1105 S22: -0.2439 S23: -0.5755
REMARK 3 S31: 0.2855 S32: 1.1035 S33: 0.0867
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 286 THROUGH 315 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5925 -44.4435 -14.9452
REMARK 3 T TENSOR
REMARK 3 T11: 0.5043 T22: 0.8184
REMARK 3 T33: 0.6311 T12: 0.0992
REMARK 3 T13: -0.0386 T23: 0.1126
REMARK 3 L TENSOR
REMARK 3 L11: 5.0390 L22: 3.8618
REMARK 3 L33: 6.9504 L12: 2.1182
REMARK 3 L13: 1.4159 L23: 0.7512
REMARK 3 S TENSOR
REMARK 3 S11: 0.1104 S12: -1.0081 S13: -0.9879
REMARK 3 S21: 0.2831 S22: 0.1602 S23: -0.6364
REMARK 3 S31: 0.7338 S32: 0.3940 S33: -0.2775
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 316 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3458 -30.7612 -8.7875
REMARK 3 T TENSOR
REMARK 3 T11: 0.5454 T22: 1.4894
REMARK 3 T33: 0.8009 T12: 0.1171
REMARK 3 T13: -0.1002 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 0.4899 L22: 1.7921
REMARK 3 L33: 2.7312 L12: 0.4906
REMARK 3 L13: 1.0844 L23: 1.6881
REMARK 3 S TENSOR
REMARK 3 S11: -0.0319 S12: 0.1562 S13: 0.1050
REMARK 3 S21: 0.1027 S22: 0.4723 S23: -0.4537
REMARK 3 S31: 0.2253 S32: 1.2270 S33: -0.4314
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 338 THROUGH 385 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6212 -25.1906 -8.9313
REMARK 3 T TENSOR
REMARK 3 T11: 0.4250 T22: 0.7963
REMARK 3 T33: 0.4324 T12: -0.0017
REMARK 3 T13: 0.0036 T23: -0.0577
REMARK 3 L TENSOR
REMARK 3 L11: 1.4142 L22: 3.9230
REMARK 3 L33: 5.2324 L12: 0.1037
REMARK 3 L13: 1.4540 L23: 0.3470
REMARK 3 S TENSOR
REMARK 3 S11: -0.0493 S12: -0.8253 S13: 0.0097
REMARK 3 S21: 0.1229 S22: -0.0095 S23: -0.1842
REMARK 3 S31: -0.4621 S32: 0.4954 S33: 0.0711
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 8S9R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273281.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-AUG-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66388
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 47.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 1.64900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2UL 6.1 MG/ML SAL2 (20MM TRIS PH 8.0,
REMARK 280 300MM NACL) WERE MIXED WITH 2UL OF RESERVOIR SOLUTION. SITTING
REMARK 280 DROP RESERVOIR CONTAINED 500UL OF 1M AMMONIUM PHOSPHATE AND 0.1M
REMARK 280 TRIS PH 8.6. CRYSTAL WAS FROZEN IN A SOLUTION OF ~25% ETHYLENE
REMARK 280 GLYCOL, 75% RESERVOIR., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 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,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 125.89550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.94775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 188.84325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 125.89550
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 188.84325
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 62.94775
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: TETRAMERIC
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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -62.94775
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 -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 LYS A -1
REMARK 465 ALA A 0
REMARK 465 ASN A 1
REMARK 465 GLN A 2
REMARK 465 VAL A 3
REMARK 465 SER A 386
REMARK 465 LYS A 387
REMARK 465 GLY A 388
REMARK 465 THR A 389
REMARK 465 GLN A 390
REMARK 465 LEU A 391
REMARK 465 LYS A 392
REMARK 465 ALA A 393
REMARK 465 SER A 394
REMARK 465 GLY B -4
REMARK 465 PRO B -3
REMARK 465 GLY B -2
REMARK 465 LYS B -1
REMARK 465 ALA B 0
REMARK 465 ASN B 1
REMARK 465 GLN B 2
REMARK 465 VAL B 3
REMARK 465 GLN B 4
REMARK 465 SER B 386
REMARK 465 LYS B 387
REMARK 465 GLY B 388
REMARK 465 THR B 389
REMARK 465 GLN B 390
REMARK 465 LEU B 391
REMARK 465 LYS B 392
REMARK 465 ALA B 393
REMARK 465 SER B 394
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 18 -2.55 68.99
REMARK 500 TYR A 29 140.68 -174.28
REMARK 500 SER A 116 -132.00 55.12
REMARK 500 PHE A 178 -68.46 -152.47
REMARK 500 ALA A 332 55.54 -107.78
REMARK 500 LEU B 18 -1.36 72.26
REMARK 500 TYR B 29 142.44 -175.57
REMARK 500 SER B 116 -119.81 58.32
REMARK 500 PHE B 178 -63.35 -138.65
REMARK 500 ALA B 332 56.55 -96.28
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD1
REMARK 620 2 ASP A 64 OD2 59.7
REMARK 620 3 HIS A 84 NE2 97.6 157.1
REMARK 620 4 HIS A 90 NE2 118.3 90.8 104.3
REMARK 620 5 ASP A 236 OD2 129.5 97.2 95.4 105.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 283 O
REMARK 620 2 ASP A 348 OD2 82.3
REMARK 620 3 ASP A 351 OD1 174.2 103.4
REMARK 620 4 ASP A 351 OD2 132.6 85.7 49.4
REMARK 620 5 ASP A 356 OD2 82.8 96.3 96.0 144.3
REMARK 620 6 ASP A 359 OD2 72.4 150.9 102.1 100.6 94.7
REMARK 620 7 HOH A 517 O 75.0 87.8 105.4 58.7 156.7 72.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 64 OD1
REMARK 620 2 ASP B 64 OD2 61.6
REMARK 620 3 HIS B 84 NE2 98.3 154.2
REMARK 620 4 HIS B 90 NE2 123.1 94.1 111.1
REMARK 620 5 ASP B 236 OD2 125.5 93.0 86.1 104.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 283 O
REMARK 620 2 ASP B 348 OD2 83.1
REMARK 620 3 ASP B 351 OD1 165.1 102.4
REMARK 620 4 ASP B 351 OD2 144.9 85.2 50.0
REMARK 620 5 ASP B 356 OD2 80.0 80.3 87.3 130.2
REMARK 620 6 ASP B 359 OD2 78.9 158.3 98.0 102.6 108.3
REMARK 620 7 HOH B 524 O 72.6 82.3 121.5 73.0 149.0 80.7
REMARK 620 N 1 2 3 4 5 6
DBREF 8S9R A -1 394 UNP Q2G155 LIP2_STAA8 295 690
DBREF 8S9R B -1 394 UNP Q2G155 LIP2_STAA8 295 690
SEQADV 8S9R GLY A -4 UNP Q2G155 EXPRESSION TAG
SEQADV 8S9R PRO A -3 UNP Q2G155 EXPRESSION TAG
SEQADV 8S9R GLY A -2 UNP Q2G155 EXPRESSION TAG
SEQADV 8S9R GLY B -4 UNP Q2G155 EXPRESSION TAG
SEQADV 8S9R PRO B -3 UNP Q2G155 EXPRESSION TAG
SEQADV 8S9R GLY B -2 UNP Q2G155 EXPRESSION TAG
SEQRES 1 A 399 GLY PRO GLY LYS ALA ASN GLN VAL GLN PRO LEU ASN LYS
SEQRES 2 A 399 TYR PRO VAL VAL PHE VAL HIS GLY PHE LEU GLY LEU VAL
SEQRES 3 A 399 GLY ASP ASN ALA PRO ALA LEU TYR PRO ASN TYR TRP GLY
SEQRES 4 A 399 GLY ASN LYS PHE LYS VAL ILE GLU GLU LEU ARG LYS GLN
SEQRES 5 A 399 GLY TYR ASN VAL HIS GLN ALA SER VAL SER ALA PHE GLY
SEQRES 6 A 399 SER ASN TYR ASP ARG ALA VAL GLU LEU TYR TYR TYR ILE
SEQRES 7 A 399 LYS GLY GLY ARG VAL ASP TYR GLY ALA ALA HIS ALA ALA
SEQRES 8 A 399 LYS TYR GLY HIS GLU ARG TYR GLY LYS THR TYR LYS GLY
SEQRES 9 A 399 ILE MET PRO ASN TRP GLU PRO GLY LYS LYS VAL HIS LEU
SEQRES 10 A 399 VAL GLY HIS SER MET GLY GLY GLN THR ILE ARG LEU MET
SEQRES 11 A 399 GLU GLU PHE LEU ARG ASN GLY ASN LYS GLU GLU ILE ALA
SEQRES 12 A 399 TYR HIS LYS ALA HIS GLY GLY GLU ILE SER PRO LEU PHE
SEQRES 13 A 399 THR GLY GLY HIS ASN ASN MET VAL ALA SER ILE THR THR
SEQRES 14 A 399 LEU ALA THR PRO HIS ASN GLY SER GLN ALA ALA ASP LYS
SEQRES 15 A 399 PHE GLY ASN THR GLU ALA VAL ARG LYS ILE MET PHE ALA
SEQRES 16 A 399 LEU ASN ARG PHE MET GLY ASN LYS TYR SER ASN ILE ASP
SEQRES 17 A 399 LEU GLY LEU THR GLN TRP GLY PHE LYS GLN LEU PRO ASN
SEQRES 18 A 399 GLU SER TYR ILE ASP TYR ILE LYS ARG VAL SER LYS SER
SEQRES 19 A 399 LYS ILE TRP THR SER ASP ASP ASN ALA ALA TYR ASP LEU
SEQRES 20 A 399 THR LEU ASP GLY SER ALA LYS LEU ASN ASN MET THR SER
SEQRES 21 A 399 MET ASN PRO ASN ILE THR TYR THR THR TYR THR GLY VAL
SEQRES 22 A 399 SER SER HIS THR GLY PRO LEU GLY TYR GLU ASN PRO ASP
SEQRES 23 A 399 LEU GLY THR PHE PHE LEU MET ALA THR THR SER ARG ILE
SEQRES 24 A 399 ILE GLY HIS ASP ALA ARG GLU GLU TRP ARG LYS ASN ASP
SEQRES 25 A 399 GLY VAL VAL PRO VAL ILE SER SER LEU HIS PRO SER ASN
SEQRES 26 A 399 GLN PRO PHE VAL ASN VAL THR ASN ASP GLU PRO ALA THR
SEQRES 27 A 399 ARG ARG GLY ILE TRP GLN VAL LYS PRO ILE ILE GLN GLY
SEQRES 28 A 399 TRP ASP HIS VAL ASP PHE ILE GLY VAL ASP PHE LEU ASP
SEQRES 29 A 399 PHE LYS ARG LYS GLY ALA GLU LEU ALA ASN PHE TYR THR
SEQRES 30 A 399 GLY ILE ILE ASN ASP LEU LEU ARG VAL GLU ALA THR GLU
SEQRES 31 A 399 SER LYS GLY THR GLN LEU LYS ALA SER
SEQRES 1 B 399 GLY PRO GLY LYS ALA ASN GLN VAL GLN PRO LEU ASN LYS
SEQRES 2 B 399 TYR PRO VAL VAL PHE VAL HIS GLY PHE LEU GLY LEU VAL
SEQRES 3 B 399 GLY ASP ASN ALA PRO ALA LEU TYR PRO ASN TYR TRP GLY
SEQRES 4 B 399 GLY ASN LYS PHE LYS VAL ILE GLU GLU LEU ARG LYS GLN
SEQRES 5 B 399 GLY TYR ASN VAL HIS GLN ALA SER VAL SER ALA PHE GLY
SEQRES 6 B 399 SER ASN TYR ASP ARG ALA VAL GLU LEU TYR TYR TYR ILE
SEQRES 7 B 399 LYS GLY GLY ARG VAL ASP TYR GLY ALA ALA HIS ALA ALA
SEQRES 8 B 399 LYS TYR GLY HIS GLU ARG TYR GLY LYS THR TYR LYS GLY
SEQRES 9 B 399 ILE MET PRO ASN TRP GLU PRO GLY LYS LYS VAL HIS LEU
SEQRES 10 B 399 VAL GLY HIS SER MET GLY GLY GLN THR ILE ARG LEU MET
SEQRES 11 B 399 GLU GLU PHE LEU ARG ASN GLY ASN LYS GLU GLU ILE ALA
SEQRES 12 B 399 TYR HIS LYS ALA HIS GLY GLY GLU ILE SER PRO LEU PHE
SEQRES 13 B 399 THR GLY GLY HIS ASN ASN MET VAL ALA SER ILE THR THR
SEQRES 14 B 399 LEU ALA THR PRO HIS ASN GLY SER GLN ALA ALA ASP LYS
SEQRES 15 B 399 PHE GLY ASN THR GLU ALA VAL ARG LYS ILE MET PHE ALA
SEQRES 16 B 399 LEU ASN ARG PHE MET GLY ASN LYS TYR SER ASN ILE ASP
SEQRES 17 B 399 LEU GLY LEU THR GLN TRP GLY PHE LYS GLN LEU PRO ASN
SEQRES 18 B 399 GLU SER TYR ILE ASP TYR ILE LYS ARG VAL SER LYS SER
SEQRES 19 B 399 LYS ILE TRP THR SER ASP ASP ASN ALA ALA TYR ASP LEU
SEQRES 20 B 399 THR LEU ASP GLY SER ALA LYS LEU ASN ASN MET THR SER
SEQRES 21 B 399 MET ASN PRO ASN ILE THR TYR THR THR TYR THR GLY VAL
SEQRES 22 B 399 SER SER HIS THR GLY PRO LEU GLY TYR GLU ASN PRO ASP
SEQRES 23 B 399 LEU GLY THR PHE PHE LEU MET ALA THR THR SER ARG ILE
SEQRES 24 B 399 ILE GLY HIS ASP ALA ARG GLU GLU TRP ARG LYS ASN ASP
SEQRES 25 B 399 GLY VAL VAL PRO VAL ILE SER SER LEU HIS PRO SER ASN
SEQRES 26 B 399 GLN PRO PHE VAL ASN VAL THR ASN ASP GLU PRO ALA THR
SEQRES 27 B 399 ARG ARG GLY ILE TRP GLN VAL LYS PRO ILE ILE GLN GLY
SEQRES 28 B 399 TRP ASP HIS VAL ASP PHE ILE GLY VAL ASP PHE LEU ASP
SEQRES 29 B 399 PHE LYS ARG LYS GLY ALA GLU LEU ALA ASN PHE TYR THR
SEQRES 30 B 399 GLY ILE ILE ASN ASP LEU LEU ARG VAL GLU ALA THR GLU
SEQRES 31 B 399 SER LYS GLY THR GLN LEU LYS ALA SER
HET ZN A 401 1
HET PO4 A 402 5
HET CA A 403 1
HET ZN B 401 1
HET PO4 B 402 5
HET PO4 B 403 5
HET CA B 404 1
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 PO4 3(O4 P 3-)
FORMUL 5 CA 2(CA 2+)
FORMUL 10 HOH *107(H2 O)
HELIX 1 AA1 VAL A 21 ALA A 25 5 5
HELIX 2 AA2 LYS A 39 GLN A 47 1 9
HELIX 3 AA3 SER A 61 GLY A 75 1 15
HELIX 4 AA4 GLY A 81 GLY A 89 1 9
HELIX 5 AA5 SER A 116 GLY A 132 1 17
HELIX 6 AA6 ASN A 133 GLY A 144 1 12
HELIX 7 AA7 SER A 148 THR A 152 5 5
HELIX 8 AA8 SER A 172 LYS A 177 1 6
HELIX 9 AA9 THR A 181 MET A 195 1 15
HELIX 10 AB1 LEU A 206 GLY A 210 5 5
HELIX 11 AB2 SER A 218 SER A 227 1 10
HELIX 12 AB3 LYS A 228 SER A 234 5 7
HELIX 13 AB4 ASN A 237 LEU A 242 1 6
HELIX 14 AB5 THR A 243 ASN A 252 1 10
HELIX 15 AB6 PHE A 285 LEU A 287 5 3
HELIX 16 AB7 MET A 288 HIS A 297 1 10
HELIX 17 AB8 ARG A 300 ARG A 304 5 5
HELIX 18 AB9 PRO A 311 LEU A 316 1 6
HELIX 19 AC1 VAL A 350 GLY A 354 5 5
HELIX 20 AC2 LYS A 363 THR A 384 1 22
HELIX 21 AC3 VAL B 21 ALA B 25 5 5
HELIX 22 AC4 LYS B 39 GLN B 47 1 9
HELIX 23 AC5 SER B 61 GLY B 75 1 15
HELIX 24 AC6 GLY B 81 GLY B 89 1 9
HELIX 25 AC7 SER B 116 GLY B 132 1 17
HELIX 26 AC8 ASN B 133 GLY B 144 1 12
HELIX 27 AC9 SER B 148 THR B 152 5 5
HELIX 28 AD1 SER B 172 LYS B 177 1 6
HELIX 29 AD2 THR B 181 GLY B 196 1 16
HELIX 30 AD3 LEU B 206 GLY B 210 5 5
HELIX 31 AD4 SER B 218 SER B 227 1 10
HELIX 32 AD5 LYS B 228 SER B 234 5 7
HELIX 33 AD6 ASN B 237 LEU B 242 1 6
HELIX 34 AD7 THR B 243 ASN B 252 1 10
HELIX 35 AD8 PHE B 285 LEU B 287 5 3
HELIX 36 AD9 MET B 288 HIS B 297 1 10
HELIX 37 AE1 ARG B 300 ARG B 304 5 5
HELIX 38 AE2 PRO B 311 LEU B 316 1 6
HELIX 39 AE3 LYS B 363 THR B 384 1 22
SHEET 1 AA1 7 VAL A 51 GLN A 53 0
SHEET 2 AA1 7 VAL A 11 VAL A 14 1 N PHE A 13 O HIS A 52
SHEET 3 AA1 7 VAL A 110 HIS A 115 1 O VAL A 113 N VAL A 14
SHEET 4 AA1 7 VAL A 159 LEU A 165 1 O ALA A 160 N VAL A 110
SHEET 5 AA1 7 THR A 261 TYR A 265 1 O THR A 261 N ILE A 162
SHEET 6 AA1 7 TRP A 338 VAL A 340 1 O GLN A 339 N THR A 264
SHEET 7 AA1 7 PHE A 323 ASN A 325 1 N VAL A 324 O TRP A 338
SHEET 1 AA2 2 GLY A 76 ASP A 79 0
SHEET 2 AA2 2 TYR A 93 TYR A 97 -1 O LYS A 95 N VAL A 78
SHEET 1 AA3 2 GLY A 267 VAL A 268 0
SHEET 2 AA3 2 ILE A 344 GLN A 345 1 O ILE A 344 N VAL A 268
SHEET 1 AA4 2 SER A 270 THR A 272 0
SHEET 2 AA4 2 GLU A 278 PRO A 280 -1 O ASN A 279 N HIS A 271
SHEET 1 AA5 7 VAL B 51 ALA B 54 0
SHEET 2 AA5 7 VAL B 11 VAL B 14 1 N PHE B 13 O HIS B 52
SHEET 3 AA5 7 VAL B 110 HIS B 115 1 O VAL B 113 N VAL B 14
SHEET 4 AA5 7 VAL B 159 LEU B 165 1 O ALA B 160 N VAL B 110
SHEET 5 AA5 7 THR B 261 TYR B 265 1 O THR B 261 N ILE B 162
SHEET 6 AA5 7 TRP B 338 VAL B 340 1 O GLN B 339 N THR B 264
SHEET 7 AA5 7 PHE B 323 ASN B 325 1 N VAL B 324 O TRP B 338
SHEET 1 AA6 2 GLY B 76 ASP B 79 0
SHEET 2 AA6 2 TYR B 93 TYR B 97 -1 O LYS B 95 N VAL B 78
SHEET 1 AA7 2 GLY B 267 VAL B 268 0
SHEET 2 AA7 2 ILE B 344 GLN B 345 1 O ILE B 344 N VAL B 268
SHEET 1 AA8 2 SER B 270 THR B 272 0
SHEET 2 AA8 2 GLU B 278 PRO B 280 -1 O ASN B 279 N HIS B 271
LINK OD1 ASP A 64 ZN ZN A 401 1555 1555 2.02
LINK OD2 ASP A 64 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 84 ZN ZN A 401 1555 1555 2.07
LINK NE2 HIS A 90 ZN ZN A 401 1555 1555 2.06
LINK OD2 ASP A 236 ZN ZN A 401 1555 1555 1.94
LINK O GLY A 283 CA CA A 403 1555 1555 2.94
LINK OD2 ASP A 348 CA CA A 403 1555 1555 2.42
LINK OD1 ASP A 351 CA CA A 403 1555 1555 2.53
LINK OD2 ASP A 351 CA CA A 403 1555 1555 2.69
LINK OD2 ASP A 356 CA CA A 403 1555 1555 2.75
LINK OD2 ASP A 359 CA CA A 403 1555 1555 2.61
LINK CA CA A 403 O HOH A 517 1555 1555 2.66
LINK OD1 ASP B 64 ZN ZN B 401 1555 1555 1.98
LINK OD2 ASP B 64 ZN ZN B 401 1555 1555 2.26
LINK NE2 HIS B 84 ZN ZN B 401 1555 1555 2.11
LINK NE2 HIS B 90 ZN ZN B 401 1555 1555 2.06
LINK OD2 ASP B 236 ZN ZN B 401 1555 1555 1.94
LINK O GLY B 283 CA CA B 404 1555 1555 2.44
LINK OD2 ASP B 348 CA CA B 404 1555 1555 2.40
LINK OD1 ASP B 351 CA CA B 404 1555 1555 2.64
LINK OD2 ASP B 351 CA CA B 404 1555 1555 2.51
LINK OD2 ASP B 356 CA CA B 404 1555 1555 2.40
LINK OD2 ASP B 359 CA CA B 404 1555 1555 2.27
LINK CA CA B 404 O HOH B 524 1555 1555 2.36
CRYST1 129.146 129.146 251.791 90.00 90.00 90.00 P 41 2 2 16
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 0.007743 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007743 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003972 0.00000
TER 3025 GLU A 385
TER 6041 GLU B 385
MASTER 604 0 7 39 26 0 0 6 6165 2 47 62
END |