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HEADER TRANSFERASE 27-APR-20 6YUV
TITLE CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS SEROGROUP A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SACC;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP A;
SOURCE 3 ORGANISM_TAXID: 65699;
SOURCE 4 GENE: SACC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS O-ACETYLTRANSFERASE, A/B HYDROLASE FOLD, SERINE TRANSFERASE,
KEYWDS 2 CATALYTIC TRIAD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.CRAMER,T.FIEBIG,R.FEDOROV,M.MUEHLENHOFF
REVDAT 1 19-AUG-20 6YUV 0
JRNL AUTH T.FIEBIG,J.T.CRAMER,A.BETHE,P.BARUCH,U.CURTH,J.I.FUEHRING,
JRNL AUTH 2 F.F.R.BUETTNER,U.VOGEL,M.SCHUBERT,R.FEDOROV,M.MUEHLENHOFF
JRNL TITL CAPSULE O-ACETYLTRANSFERASE OF NEISSERIA MENINGITIDIS
JRNL TITL 2 SEROGROUP A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 46709
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2334
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 49.4000 - 5.1400 1.00 2831 148 0.1617 0.1997
REMARK 3 2 5.1400 - 4.0800 1.00 2672 140 0.1410 0.1528
REMARK 3 3 4.0800 - 3.5700 1.00 2660 141 0.1631 0.1494
REMARK 3 4 3.5700 - 3.2400 1.00 2618 138 0.1944 0.2381
REMARK 3 5 3.2400 - 3.0100 1.00 2629 137 0.2068 0.2602
REMARK 3 6 3.0100 - 2.8300 1.00 2601 137 0.2032 0.2360
REMARK 3 7 2.8300 - 2.6900 1.00 2617 138 0.1944 0.2254
REMARK 3 8 2.6900 - 2.5700 1.00 2595 136 0.2040 0.2436
REMARK 3 9 2.5700 - 2.4700 1.00 2586 136 0.1992 0.2110
REMARK 3 10 2.4700 - 2.3900 1.00 2564 135 0.1991 0.2636
REMARK 3 11 2.3900 - 2.3100 1.00 2594 137 0.2013 0.2600
REMARK 3 12 2.3100 - 2.2500 1.00 2575 136 0.2030 0.2754
REMARK 3 13 2.2500 - 2.1900 1.00 2572 135 0.2131 0.2286
REMARK 3 14 2.1900 - 2.1300 1.00 2568 136 0.2198 0.2586
REMARK 3 15 2.1300 - 2.0900 1.00 2569 134 0.2262 0.2890
REMARK 3 16 2.0900 - 2.0400 1.00 2555 134 0.2295 0.2995
REMARK 3 17 2.0400 - 2.0000 1.00 2569 136 0.2525 0.2922
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.213
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.281
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.41
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 4006
REMARK 3 ANGLE : 0.805 5425
REMARK 3 CHIRALITY : 0.055 615
REMARK 3 PLANARITY : 0.004 683
REMARK 3 DIHEDRAL : 15.628 1452
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 1 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0768 29.6347 -24.6153
REMARK 3 T TENSOR
REMARK 3 T11: 0.4510 T22: 0.9896
REMARK 3 T33: 0.7499 T12: 0.1156
REMARK 3 T13: 0.0187 T23: -0.2933
REMARK 3 L TENSOR
REMARK 3 L11: 4.0945 L22: 5.6865
REMARK 3 L33: 8.4000 L12: 0.7660
REMARK 3 L13: -4.6264 L23: -0.7865
REMARK 3 S TENSOR
REMARK 3 S11: -0.3190 S12: 0.5401 S13: -1.0744
REMARK 3 S21: -0.3677 S22: 0.1939 S23: -1.0080
REMARK 3 S31: 0.9700 S32: 2.1420 S33: 0.0005
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1268 35.2280 -29.3077
REMARK 3 T TENSOR
REMARK 3 T11: 0.3716 T22: 0.6387
REMARK 3 T33: 0.4220 T12: -0.0004
REMARK 3 T13: 0.0430 T23: -0.1973
REMARK 3 L TENSOR
REMARK 3 L11: 3.1555 L22: 2.5000
REMARK 3 L33: 3.0625 L12: -0.5460
REMARK 3 L13: 0.4718 L23: 0.2971
REMARK 3 S TENSOR
REMARK 3 S11: -0.0393 S12: 0.6363 S13: -0.3665
REMARK 3 S21: -0.3718 S22: 0.2604 S23: -0.2602
REMARK 3 S31: 0.1199 S32: 0.6162 S33: -0.2625
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 87 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0898 34.1080 -28.2500
REMARK 3 T TENSOR
REMARK 3 T11: 0.3812 T22: 0.5471
REMARK 3 T33: 0.3111 T12: 0.0344
REMARK 3 T13: 0.0028 T23: -0.1471
REMARK 3 L TENSOR
REMARK 3 L11: 6.8050 L22: 4.9131
REMARK 3 L33: 5.0713 L12: 0.3811
REMARK 3 L13: -0.2373 L23: 1.0470
REMARK 3 S TENSOR
REMARK 3 S11: -0.0498 S12: 0.6064 S13: -0.6760
REMARK 3 S21: -0.1592 S22: 0.2770 S23: -0.5022
REMARK 3 S31: 0.1547 S32: 0.9279 S33: -0.1839
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.3688 42.6293 -26.4321
REMARK 3 T TENSOR
REMARK 3 T11: 0.3786 T22: 0.3837
REMARK 3 T33: 0.2930 T12: -0.0496
REMARK 3 T13: 0.0260 T23: -0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 3.8107 L22: 2.1595
REMARK 3 L33: 4.5187 L12: 0.2261
REMARK 3 L13: 1.1164 L23: -0.2838
REMARK 3 S TENSOR
REMARK 3 S11: -0.2202 S12: 0.3915 S13: -0.0033
REMARK 3 S21: -0.1943 S22: 0.3101 S23: -0.1284
REMARK 3 S31: -0.2978 S32: 0.5701 S33: -0.0753
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.3849 28.0445 -26.2208
REMARK 3 T TENSOR
REMARK 3 T11: 0.4712 T22: 0.3724
REMARK 3 T33: 0.4415 T12: -0.0888
REMARK 3 T13: -0.0470 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 8.5823 L22: 4.2731
REMARK 3 L33: 5.1889 L12: 0.3011
REMARK 3 L13: -1.9148 L23: -0.1665
REMARK 3 S TENSOR
REMARK 3 S11: -0.0757 S12: 0.1100 S13: -1.1608
REMARK 3 S21: 0.1326 S22: 0.0708 S23: 0.1641
REMARK 3 S31: 0.5621 S32: -0.5112 S33: 0.0100
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2812 49.1608 -31.4666
REMARK 3 T TENSOR
REMARK 3 T11: 0.4742 T22: 0.3344
REMARK 3 T33: 0.3316 T12: -0.1090
REMARK 3 T13: -0.0859 T23: 0.0721
REMARK 3 L TENSOR
REMARK 3 L11: 3.1093 L22: 3.2174
REMARK 3 L33: 3.1806 L12: -0.7456
REMARK 3 L13: 0.2345 L23: 0.8459
REMARK 3 S TENSOR
REMARK 3 S11: -0.2640 S12: 0.5465 S13: 0.1701
REMARK 3 S21: -0.4912 S22: 0.1491 S23: 0.2460
REMARK 3 S31: -0.4603 S32: -0.0022 S33: 0.1037
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0895 50.5580 -40.0559
REMARK 3 T TENSOR
REMARK 3 T11: 0.6282 T22: 0.7650
REMARK 3 T33: 0.4410 T12: -0.2240
REMARK 3 T13: -0.0635 T23: 0.0869
REMARK 3 L TENSOR
REMARK 3 L11: 2.8409 L22: 3.2652
REMARK 3 L33: 5.8225 L12: -0.5149
REMARK 3 L13: -2.0661 L23: 0.8134
REMARK 3 S TENSOR
REMARK 3 S11: 0.1052 S12: 0.7879 S13: 0.1638
REMARK 3 S21: -0.9896 S22: 0.2569 S23: -0.1046
REMARK 3 S31: -0.8199 S32: 0.2041 S33: -0.3109
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2300 48.5904 -40.6853
REMARK 3 T TENSOR
REMARK 3 T11: 0.6281 T22: 0.9263
REMARK 3 T33: 0.3961 T12: -0.2251
REMARK 3 T13: 0.1340 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 6.2104 L22: 6.9259
REMARK 3 L33: 6.9595 L12: -0.1206
REMARK 3 L13: 0.4472 L23: 0.4210
REMARK 3 S TENSOR
REMARK 3 S11: -0.2537 S12: 0.7953 S13: 0.3417
REMARK 3 S21: -1.1972 S22: 0.5458 S23: -0.6657
REMARK 3 S31: -0.4618 S32: 1.5170 S33: -0.2377
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 27 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5954 46.8008 -4.3503
REMARK 3 T TENSOR
REMARK 3 T11: 0.2470 T22: 0.3764
REMARK 3 T33: 0.4085 T12: 0.0905
REMARK 3 T13: -0.0575 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 0.8632 L22: 3.7801
REMARK 3 L33: 9.4071 L12: 1.5334
REMARK 3 L13: -1.7055 L23: -0.1901
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: -0.0150 S13: 0.0668
REMARK 3 S21: 0.0375 S22: 0.0480 S23: 0.1425
REMARK 3 S31: -0.3176 S32: -0.0049 S33: -0.0846
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 28 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5819 38.0859 4.4058
REMARK 3 T TENSOR
REMARK 3 T11: 0.3019 T22: 0.3331
REMARK 3 T33: 0.3754 T12: 0.0502
REMARK 3 T13: -0.0903 T23: -0.0825
REMARK 3 L TENSOR
REMARK 3 L11: 3.1281 L22: 2.5147
REMARK 3 L33: 5.2560 L12: 2.0267
REMARK 3 L13: -2.3871 L23: -1.2954
REMARK 3 S TENSOR
REMARK 3 S11: 0.2407 S12: -0.3564 S13: -0.1863
REMARK 3 S21: 0.0499 S22: -0.2534 S23: -0.2272
REMARK 3 S31: -0.0079 S32: 0.4434 S33: -0.0083
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.7065 37.4612 -0.6611
REMARK 3 T TENSOR
REMARK 3 T11: 0.2975 T22: 0.2640
REMARK 3 T33: 0.3454 T12: 0.0606
REMARK 3 T13: -0.0410 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 4.7388 L22: 4.4894
REMARK 3 L33: 6.5647 L12: 0.4704
REMARK 3 L13: -3.8049 L23: 0.8367
REMARK 3 S TENSOR
REMARK 3 S11: 0.1470 S12: 0.0730 S13: -0.0709
REMARK 3 S21: 0.1305 S22: -0.1128 S23: -0.0112
REMARK 3 S31: 0.0171 S32: 0.1057 S33: 0.0077
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6766 28.8256 -1.9141
REMARK 3 T TENSOR
REMARK 3 T11: 0.4285 T22: 0.5813
REMARK 3 T33: 0.6675 T12: 0.1828
REMARK 3 T13: -0.0286 T23: -0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 2.5330 L22: 2.1267
REMARK 3 L33: 2.7176 L12: 1.5593
REMARK 3 L13: 0.3426 L23: -1.5896
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: 0.1878 S13: -0.7400
REMARK 3 S21: -0.3996 S22: -0.2387 S23: -0.3768
REMARK 3 S31: 0.7240 S32: 0.8698 S33: 0.2079
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 115 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0946 29.8483 4.5940
REMARK 3 T TENSOR
REMARK 3 T11: 0.3943 T22: 0.3368
REMARK 3 T33: 0.3797 T12: -0.0024
REMARK 3 T13: -0.0058 T23: -0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 4.7049 L22: 2.5068
REMARK 3 L33: 3.7642 L12: 1.3796
REMARK 3 L13: 1.0487 L23: -1.2894
REMARK 3 S TENSOR
REMARK 3 S11: 0.0409 S12: -0.0940 S13: -0.1643
REMARK 3 S21: 0.1564 S22: -0.0746 S23: 0.1111
REMARK 3 S31: 0.3480 S32: -0.1316 S33: 0.0482
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 161 THROUGH 198 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.2882 22.7368 2.9473
REMARK 3 T TENSOR
REMARK 3 T11: 0.5573 T22: 0.3413
REMARK 3 T33: 0.4750 T12: -0.0506
REMARK 3 T13: 0.0147 T23: -0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 5.9588 L22: 1.7140
REMARK 3 L33: 3.0792 L12: -1.5362
REMARK 3 L13: 1.7758 L23: -1.2531
REMARK 3 S TENSOR
REMARK 3 S11: 0.0860 S12: 0.1541 S13: -0.8132
REMARK 3 S21: 0.0066 S22: -0.0453 S23: 0.2165
REMARK 3 S31: 0.7507 S32: -0.1226 S33: -0.0367
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 199 THROUGH 229 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2730 18.5949 11.7926
REMARK 3 T TENSOR
REMARK 3 T11: 0.5676 T22: 0.3990
REMARK 3 T33: 0.5315 T12: 0.0040
REMARK 3 T13: 0.0099 T23: 0.0849
REMARK 3 L TENSOR
REMARK 3 L11: 4.6555 L22: 5.3591
REMARK 3 L33: 7.0628 L12: -0.2802
REMARK 3 L13: -0.9063 L23: 0.5625
REMARK 3 S TENSOR
REMARK 3 S11: 0.0243 S12: -0.4259 S13: -0.9775
REMARK 3 S21: 0.3610 S22: -0.0753 S23: 0.1169
REMARK 3 S31: 1.3372 S32: 0.0708 S33: 0.0816
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 230 THROUGH 245 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4513 29.1959 13.7111
REMARK 3 T TENSOR
REMARK 3 T11: 0.5589 T22: 0.7261
REMARK 3 T33: 0.5358 T12: 0.1597
REMARK 3 T13: -0.1518 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 6.8055 L22: 4.0418
REMARK 3 L33: 2.0849 L12: 1.5295
REMARK 3 L13: -6.9218 L23: -0.4780
REMARK 3 S TENSOR
REMARK 3 S11: -0.1627 S12: -1.0206 S13: -0.2537
REMARK 3 S21: 0.2684 S22: 0.0186 S23: -0.6363
REMARK 3 S31: 0.3885 S32: 1.9110 S33: 0.2353
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 246 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0103 23.1816 7.2283
REMARK 3 T TENSOR
REMARK 3 T11: 0.9453 T22: 1.3706
REMARK 3 T33: 1.5508 T12: 0.5913
REMARK 3 T13: -0.1312 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 2.0001 L22: 2.0001
REMARK 3 L33: 2.0000 L12: 1.9997
REMARK 3 L13: 1.9998 L23: 0.8008
REMARK 3 S TENSOR
REMARK 3 S11: 2.2267 S12: 4.4135 S13: 2.9183
REMARK 3 S21: -3.2720 S22: -2.6394 S23: 3.3552
REMARK 3 S31: -2.0068 S32: -1.2292 S33: 0.4157
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 6YUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1292108332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-16
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 : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999996
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46740
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.80
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 36.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 22.90
REMARK 200 R MERGE FOR SHELL (I) : 0.69400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
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: 6YUO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE WILD TYPE CSAC CRYSTALLIZED IN
REMARK 280 SITTING DROP SETUPS AT CONCENTRATIONS OF 18 MG/ML. FINE SCREENS
REMARK 280 AROUND INITIAL SCREENING CONDITIONS RESULTED IN MANY ISOMORPHOUS
REMARK 280 CRYSTALS. MOTHER LIQUOR CONTAINED 50 MM HEPES PH 7.0, 100 MM
REMARK 280 HEPES PH 7.6, 100 MM NACL, 5 MM MGCL2, 1 MM EDTA, AND 31-42%
REMARK 280 PEG200., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.28000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 69.16000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 69.16000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.64000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 69.16000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 69.16000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.92000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 69.16000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.16000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 17.64000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 69.16000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.16000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.92000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 35.28000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 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 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 -35.28000
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 ILE A 247
REMARK 465 LEU A 248
REMARK 465 GLU A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
REMARK 465 HIS A 255
REMARK 465 ILE B 247
REMARK 465 LEU B 248
REMARK 465 GLU B 249
REMARK 465 HIS B 250
REMARK 465 HIS B 251
REMARK 465 HIS B 252
REMARK 465 HIS B 253
REMARK 465 HIS B 254
REMARK 465 HIS B 255
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 106 CD OE1 OE2
REMARK 470 LYS A 161 CG CD CE NZ
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 220 CG CD CE NZ
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 ASN A 246 CG OD1 ND2
REMARK 470 LYS B 53 CG CD CE NZ
REMARK 470 LEU B 56 CG CD1 CD2
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 LYS B 187 CD CE NZ
REMARK 470 LYS B 196 CE NZ
REMARK 470 LYS B 220 CG CD CE NZ
REMARK 470 GLU B 238 CD OE1 OE2
REMARK 470 LYS B 241 CD CE NZ
REMARK 470 GLN B 245 CD OE1 NE2
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 GLU A 31 -44.25 77.28
REMARK 500 ASP A 74 75.15 -156.42
REMARK 500 SER A 114 -121.97 59.68
REMARK 500 ALA A 136 59.97 38.08
REMARK 500 SER A 149 109.40 -160.99
REMARK 500 GLU B 31 -54.90 77.60
REMARK 500 ASP B 74 73.35 -162.71
REMARK 500 SER B 114 -121.31 63.47
REMARK 500 SER B 149 111.68 -163.48
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 A 477 DISTANCE = 6.08 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
DBREF 6YUV A 1 247 UNP O68216 O68216_NEIMD 1 247
DBREF 6YUV B 1 247 UNP O68216 O68216_NEIMD 1 247
SEQADV 6YUV LEU A 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUV GLU A 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS A 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS A 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS A 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS A 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS A 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS A 255 UNP O68216 EXPRESSION TAG
SEQADV 6YUV LEU B 248 UNP O68216 EXPRESSION TAG
SEQADV 6YUV GLU B 249 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS B 250 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS B 251 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS B 252 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS B 253 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS B 254 UNP O68216 EXPRESSION TAG
SEQADV 6YUV HIS B 255 UNP O68216 EXPRESSION TAG
SEQRES 1 A 255 MET LEU SER ASN LEU LYS THR GLY ASN ASN ILE LEU GLY
SEQRES 2 A 255 LEU PRO GLU PHE GLU LEU ASN GLY CYS ARG PHE LEU TYR
SEQRES 3 A 255 LYS LYS GLY ILE GLU LYS THR ILE ILE THR PHE SER ALA
SEQRES 4 A 255 PHE PRO PRO LYS ASP ILE ALA GLN LYS TYR ASN TYR ILE
SEQRES 5 A 255 LYS ASP PHE LEU SER SER ASN TYR THR PHE LEU ALA PHE
SEQRES 6 A 255 LEU ASP THR LYS TYR PRO GLU ASP ASP ALA ARG GLY THR
SEQRES 7 A 255 TYR TYR ILE THR ASN GLU LEU ASP ASN GLY TYR LEU GLN
SEQRES 8 A 255 THR ILE HIS CYS ILE ILE GLN LEU LEU SER ASN THR ASN
SEQRES 9 A 255 GLN GLU ASP THR TYR LEU LEU GLY SER SER LYS GLY GLY
SEQRES 10 A 255 VAL GLY ALA LEU LEU LEU GLY LEU THR TYR ASN TYR PRO
SEQRES 11 A 255 ASN ILE ILE ILE ASN ALA PRO GLN ALA LYS LEU ALA ASP
SEQRES 12 A 255 TYR ILE LYS THR ARG SER LYS THR ILE LEU SER TYR MET
SEQRES 13 A 255 LEU GLY THR SER LYS ARG PHE GLN ASP ILE ASN TYR ASP
SEQRES 14 A 255 TYR ILE ASN ASP PHE LEU LEU SER LYS ILE LYS THR CYS
SEQRES 15 A 255 ASP SER SER LEU LYS TRP ASN ILE HIS ILE THR CYS GLY
SEQRES 16 A 255 LYS ASP ASP SER TYR HIS LEU ASN GLU LEU GLU ILE LEU
SEQRES 17 A 255 LYS ASN GLU PHE ASN ILE LYS ALA ILE THR ILE LYS THR
SEQRES 18 A 255 LYS LEU ILE SER GLY GLY HIS ASP ASN GLU ALA ILE ALA
SEQRES 19 A 255 HIS TYR ARG GLU TYR PHE LYS THR ILE ILE GLN ASN ILE
SEQRES 20 A 255 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 255 MET LEU SER ASN LEU LYS THR GLY ASN ASN ILE LEU GLY
SEQRES 2 B 255 LEU PRO GLU PHE GLU LEU ASN GLY CYS ARG PHE LEU TYR
SEQRES 3 B 255 LYS LYS GLY ILE GLU LYS THR ILE ILE THR PHE SER ALA
SEQRES 4 B 255 PHE PRO PRO LYS ASP ILE ALA GLN LYS TYR ASN TYR ILE
SEQRES 5 B 255 LYS ASP PHE LEU SER SER ASN TYR THR PHE LEU ALA PHE
SEQRES 6 B 255 LEU ASP THR LYS TYR PRO GLU ASP ASP ALA ARG GLY THR
SEQRES 7 B 255 TYR TYR ILE THR ASN GLU LEU ASP ASN GLY TYR LEU GLN
SEQRES 8 B 255 THR ILE HIS CYS ILE ILE GLN LEU LEU SER ASN THR ASN
SEQRES 9 B 255 GLN GLU ASP THR TYR LEU LEU GLY SER SER LYS GLY GLY
SEQRES 10 B 255 VAL GLY ALA LEU LEU LEU GLY LEU THR TYR ASN TYR PRO
SEQRES 11 B 255 ASN ILE ILE ILE ASN ALA PRO GLN ALA LYS LEU ALA ASP
SEQRES 12 B 255 TYR ILE LYS THR ARG SER LYS THR ILE LEU SER TYR MET
SEQRES 13 B 255 LEU GLY THR SER LYS ARG PHE GLN ASP ILE ASN TYR ASP
SEQRES 14 B 255 TYR ILE ASN ASP PHE LEU LEU SER LYS ILE LYS THR CYS
SEQRES 15 B 255 ASP SER SER LEU LYS TRP ASN ILE HIS ILE THR CYS GLY
SEQRES 16 B 255 LYS ASP ASP SER TYR HIS LEU ASN GLU LEU GLU ILE LEU
SEQRES 17 B 255 LYS ASN GLU PHE ASN ILE LYS ALA ILE THR ILE LYS THR
SEQRES 18 B 255 LYS LEU ILE SER GLY GLY HIS ASP ASN GLU ALA ILE ALA
SEQRES 19 B 255 HIS TYR ARG GLU TYR PHE LYS THR ILE ILE GLN ASN ILE
SEQRES 20 B 255 LEU GLU HIS HIS HIS HIS HIS HIS
HET CL A 301 1
HET PGE B 301 10
HET CL B 302 1
HETNAM CL CHLORIDE ION
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 3 CL 2(CL 1-)
FORMUL 4 PGE C6 H14 O4
FORMUL 6 HOH *165(H2 O)
HELIX 1 AA1 MET A 1 ASN A 4 5 4
HELIX 2 AA2 ILE A 52 LEU A 56 5 5
HELIX 3 AA3 PRO A 71 ALA A 75 5 5
HELIX 4 AA4 ASN A 87 SER A 101 1 15
HELIX 5 AA5 ASN A 104 GLU A 106 5 3
HELIX 6 AA6 SER A 114 ASN A 128 1 15
HELIX 7 AA7 LYS A 140 SER A 149 1 10
HELIX 8 AA8 SER A 149 GLY A 158 1 10
HELIX 9 AA9 SER A 160 ARG A 162 5 3
HELIX 10 AB1 PHE A 163 ASP A 173 1 11
HELIX 11 AB2 ASP A 173 THR A 181 1 9
HELIX 12 AB3 ASP A 198 LYS A 215 1 18
HELIX 13 AB4 ASP A 229 GLN A 245 1 17
HELIX 14 AB5 MET B 1 ASN B 4 5 4
HELIX 15 AB6 ILE B 52 LEU B 56 5 5
HELIX 16 AB7 PRO B 71 ALA B 75 5 5
HELIX 17 AB8 ASN B 87 SER B 101 1 15
HELIX 18 AB9 ASN B 104 GLU B 106 5 3
HELIX 19 AC1 SER B 114 ASN B 128 1 15
HELIX 20 AC2 LYS B 140 SER B 149 1 10
HELIX 21 AC3 SER B 149 GLY B 158 1 10
HELIX 22 AC4 SER B 160 ARG B 162 5 3
HELIX 23 AC5 PHE B 163 ASP B 173 1 11
HELIX 24 AC6 ASP B 173 THR B 181 1 9
HELIX 25 AC7 ASP B 198 LYS B 215 1 18
HELIX 26 AC8 ASP B 229 ASN B 246 1 18
SHEET 1 AA1 9 LYS A 6 ILE A 11 0
SHEET 2 AA1 9 LEU A 14 LEU A 19 -1 O LEU A 14 N ILE A 11
SHEET 3 AA1 9 CYS A 22 LYS A 27 -1 O PHE A 24 N PHE A 17
SHEET 4 AA1 9 THR A 61 PHE A 65 -1 O ALA A 64 N LEU A 25
SHEET 5 AA1 9 THR A 33 PHE A 37 1 N ILE A 34 O THR A 61
SHEET 6 AA1 9 THR A 108 SER A 113 1 O TYR A 109 N ILE A 35
SHEET 7 AA1 9 ASN A 131 ASN A 135 1 O ILE A 133 N LEU A 110
SHEET 8 AA1 9 ASN A 189 GLY A 195 1 O HIS A 191 N ILE A 132
SHEET 9 AA1 9 LYS A 220 ILE A 224 1 O LYS A 220 N ILE A 190
SHEET 1 AA2 9 LYS B 6 ILE B 11 0
SHEET 2 AA2 9 LEU B 14 LEU B 19 -1 O LEU B 14 N ILE B 11
SHEET 3 AA2 9 CYS B 22 LYS B 27 -1 O PHE B 24 N PHE B 17
SHEET 4 AA2 9 THR B 61 PHE B 65 -1 O PHE B 62 N LYS B 27
SHEET 5 AA2 9 THR B 33 PHE B 37 1 N ILE B 34 O THR B 61
SHEET 6 AA2 9 THR B 108 SER B 113 1 O TYR B 109 N ILE B 35
SHEET 7 AA2 9 ASN B 131 ASN B 135 1 O ILE B 133 N LEU B 110
SHEET 8 AA2 9 ASN B 189 GLY B 195 1 O HIS B 191 N ILE B 132
SHEET 9 AA2 9 LYS B 220 ILE B 224 1 O LYS B 220 N ILE B 190
CISPEP 1 TYR A 70 PRO A 71 0 -1.05
CISPEP 2 TYR B 70 PRO B 71 0 3.06
SITE 1 AC1 4 PHE A 40 SER A 114 LYS A 115 ARG A 148
SITE 1 AC2 4 ASN B 83 LEU B 85 TYR B 155 MET B 156
SITE 1 AC3 3 PHE B 40 SER B 114 LYS B 115
CRYST1 138.320 138.320 70.560 90.00 90.00 90.00 P 41 21 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 0.007230 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007230 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014172 0.00000
TER 1962 ASN A 246
TER 3917 ASN B 246
MASTER 586 0 3 26 18 0 3 6 4092 2 10 40
END |