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HEADER HYDROLASE 31-JUL-25 9S6B
TITLE AEROPYRUM PERNIX ACYLAMINOACYL PEPTIDASE CO-CRYSTALLIZED WITH
TITLE 2 MEROPENEM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AARE,ACYL-PEPTIDE HYDROLASE,APH,ACYLAMINOACYL-PEPTIDASE;
COMPND 5 EC: 3.4.19.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: D524A ACTIVE SITE MUTANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX K1;
SOURCE 3 ORGANISM_TAXID: 272557;
SOURCE 4 GENE: APE_1547.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE PROTEASE, HBPG, LIGAND BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.HARMAT,L.TAKACS,A.KISS-SZEMAN,Z.BANOCZI,I.JAKLI,N.HOSOGI,
AUTHOR 2 D.A.K.TRAORE,A.PERCZEL,D.K.MENYHARD
REVDAT 1 22-OCT-25 9S6B 0
JRNL AUTH A.J.KISS-SZEMAN,L.TAKACS,I.JAKLI,Z.BANOCZI,N.HOSOGI,
JRNL AUTH 2 D.A.K.TRAORE,V.HARMAT,A.PERCZEL,D.K.MENYHARD
JRNL TITL LIGAND BINDING PRO-MISCUITY OF ACYLPEPTIDE HYDROLASE,
JRNL TITL 2 STRUCTURAL ANALYSIS OF A DETOXIFYING SERINE HYDROLASE.
JRNL REF PROTEIN SCI. V. 34 70320 2025
JRNL REFN ESSN 1469-896X
JRNL PMID 41074793
JRNL DOI 10.1002/PRO.70320
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.950
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 105790
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2101
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 39.2200 - 5.6700 0.99 6976 136 0.1637 0.1672
REMARK 3 2 5.6700 - 4.5000 0.99 6969 132 0.1470 0.1841
REMARK 3 3 4.5000 - 3.9300 0.99 6991 123 0.1555 0.1526
REMARK 3 4 3.9300 - 3.5700 0.99 7004 126 0.1863 0.2205
REMARK 3 5 3.5700 - 3.3200 0.99 7029 130 0.1995 0.2410
REMARK 3 6 3.3200 - 3.1200 0.99 7007 131 0.2248 0.3032
REMARK 3 7 3.1200 - 2.9700 1.00 6965 156 0.2360 0.2998
REMARK 3 8 2.9700 - 2.8400 1.00 7024 158 0.2389 0.2610
REMARK 3 9 2.8400 - 2.7300 1.00 6999 151 0.2433 0.3183
REMARK 3 10 2.7300 - 2.6300 1.00 6993 158 0.2584 0.2975
REMARK 3 11 2.6300 - 2.5500 1.00 7063 148 0.2805 0.2954
REMARK 3 12 2.5500 - 2.4800 0.96 6777 136 0.2969 0.3593
REMARK 3 13 2.4800 - 2.4100 0.94 6629 136 0.3164 0.3358
REMARK 3 14 2.4100 - 2.3500 0.94 6579 151 0.3440 0.3465
REMARK 3 15 2.3500 - 2.3000 0.95 6684 129 0.3744 0.3678
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) : 0.374
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.92
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 : 0.003 17100
REMARK 3 ANGLE : 0.562 23285
REMARK 3 CHIRALITY : 0.044 2659
REMARK 3 PLANARITY : 0.004 3048
REMARK 3 DIHEDRAL : 11.685 6006
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 27
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8065 -20.1394 12.8768
REMARK 3 T TENSOR
REMARK 3 T11: 0.6951 T22: 0.4938
REMARK 3 T33: 0.5865 T12: -0.0417
REMARK 3 T13: -0.0757 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.0911 L22: 0.4099
REMARK 3 L33: 0.5965 L12: 0.2760
REMARK 3 L13: -0.0377 L23: -0.3693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0375 S12: -0.1390 S13: 0.1161
REMARK 3 S21: 0.8896 S22: -0.1742 S23: -0.3432
REMARK 3 S31: 0.1551 S32: -0.1495 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 43 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3093 -32.4070 -3.8594
REMARK 3 T TENSOR
REMARK 3 T11: 0.5794 T22: 0.5009
REMARK 3 T33: 0.5255 T12: -0.0686
REMARK 3 T13: 0.0173 T23: 0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 1.7703 L22: 1.6176
REMARK 3 L33: 1.8365 L12: -0.2866
REMARK 3 L13: 0.4387 L23: 0.5508
REMARK 3 S TENSOR
REMARK 3 S11: -0.1883 S12: 0.0851 S13: 0.2879
REMARK 3 S21: -0.1763 S22: -0.0419 S23: -0.0929
REMARK 3 S31: -0.1001 S32: 0.3349 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 143 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4762 -35.7396 -12.5844
REMARK 3 T TENSOR
REMARK 3 T11: 0.6371 T22: 0.5200
REMARK 3 T33: 0.5431 T12: -0.0084
REMARK 3 T13: -0.1028 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.5487 L22: 0.3655
REMARK 3 L33: 1.3752 L12: 0.2307
REMARK 3 L13: -0.4022 L23: 0.8478
REMARK 3 S TENSOR
REMARK 3 S11: -0.3254 S12: 0.1842 S13: 0.0295
REMARK 3 S21: -0.4440 S22: 0.0274 S23: 0.3454
REMARK 3 S31: -0.1237 S32: -0.2728 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 224 THROUGH 353 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8086 -29.2776 8.3375
REMARK 3 T TENSOR
REMARK 3 T11: 0.5200 T22: 0.5762
REMARK 3 T33: 0.5683 T12: 0.0317
REMARK 3 T13: -0.0396 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 0.7692 L22: 0.5758
REMARK 3 L33: 0.7368 L12: 0.2194
REMARK 3 L13: 0.2500 L23: -0.1774
REMARK 3 S TENSOR
REMARK 3 S11: -0.0878 S12: -0.1730 S13: 0.0963
REMARK 3 S21: 0.1141 S22: -0.1123 S23: 0.3006
REMARK 3 S31: -0.0267 S32: -0.4458 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 354 THROUGH 521 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6054 -6.8175 -3.3322
REMARK 3 T TENSOR
REMARK 3 T11: 0.7106 T22: 0.6435
REMARK 3 T33: 0.7152 T12: 0.1519
REMARK 3 T13: -0.2083 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 0.8574 L22: 2.8494
REMARK 3 L33: 0.1174 L12: 1.1853
REMARK 3 L13: 0.5251 L23: -0.0583
REMARK 3 S TENSOR
REMARK 3 S11: -0.2353 S12: 0.2824 S13: 0.1997
REMARK 3 S21: -0.3291 S22: 0.0929 S23: 0.3102
REMARK 3 S31: -0.2021 S32: -0.1067 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 522 THROUGH 581 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9925 -2.3003 -1.3621
REMARK 3 T TENSOR
REMARK 3 T11: 0.8198 T22: 0.6588
REMARK 3 T33: 0.7013 T12: 0.0869
REMARK 3 T13: -0.2305 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 1.1447 L22: 0.9296
REMARK 3 L33: 1.0737 L12: 1.1918
REMARK 3 L13: -0.6828 L23: -0.5313
REMARK 3 S TENSOR
REMARK 3 S11: -0.1196 S12: 0.4685 S13: -0.1088
REMARK 3 S21: -0.1723 S22: 0.1383 S23: -0.0371
REMARK 3 S31: 0.0392 S32: 0.2331 S33: -0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5703 14.5152 26.6259
REMARK 3 T TENSOR
REMARK 3 T11: 0.4950 T22: 0.5044
REMARK 3 T33: 0.6298 T12: -0.0084
REMARK 3 T13: -0.0232 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 0.6041 L22: 0.4632
REMARK 3 L33: 1.5322 L12: -0.5294
REMARK 3 L13: 0.0133 L23: -0.6219
REMARK 3 S TENSOR
REMARK 3 S11: 0.2486 S12: -0.0758 S13: -0.2867
REMARK 3 S21: 0.1319 S22: -0.1775 S23: 0.3830
REMARK 3 S31: 0.2520 S32: -0.1305 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4350 35.9889 23.3421
REMARK 3 T TENSOR
REMARK 3 T11: 0.4803 T22: 0.5085
REMARK 3 T33: 0.6435 T12: 0.0316
REMARK 3 T13: 0.0651 T23: -0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 1.1834 L22: 1.5608
REMARK 3 L33: 0.7254 L12: -0.5348
REMARK 3 L13: -0.3138 L23: -0.6841
REMARK 3 S TENSOR
REMARK 3 S11: 0.1102 S12: -0.0222 S13: -0.0385
REMARK 3 S21: -0.1030 S22: -0.1142 S23: 0.3938
REMARK 3 S31: -0.1735 S32: -0.2878 S33: -0.0001
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 143 THROUGH 253 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6916 40.1849 15.8908
REMARK 3 T TENSOR
REMARK 3 T11: 0.5502 T22: 0.5797
REMARK 3 T33: 0.5034 T12: 0.0023
REMARK 3 T13: 0.1032 T23: 0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 1.9446 L22: 0.8261
REMARK 3 L33: 0.9574 L12: 0.2540
REMARK 3 L13: -0.0826 L23: 0.2298
REMARK 3 S TENSOR
REMARK 3 S11: 0.1261 S12: 0.2530 S13: 0.3070
REMARK 3 S21: -0.1297 S22: -0.1845 S23: -0.0792
REMARK 3 S31: -0.2809 S32: 0.1845 S33: -0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 254 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0941 18.1971 25.9312
REMARK 3 T TENSOR
REMARK 3 T11: 0.5354 T22: 0.5369
REMARK 3 T33: 0.5052 T12: 0.0237
REMARK 3 T13: 0.0068 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 2.1440 L22: 1.2017
REMARK 3 L33: 1.5749 L12: 0.6176
REMARK 3 L13: 0.8437 L23: 0.3761
REMARK 3 S TENSOR
REMARK 3 S11: 0.2350 S12: 0.1693 S13: -0.2599
REMARK 3 S21: 0.1832 S22: -0.0443 S23: -0.1592
REMARK 3 S31: 0.2534 S32: 0.4248 S33: 0.0002
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 340 THROUGH 432 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5161 8.5539 5.9453
REMARK 3 T TENSOR
REMARK 3 T11: 0.5660 T22: 0.9574
REMARK 3 T33: 0.6986 T12: 0.2185
REMARK 3 T13: -0.0466 T23: -0.2855
REMARK 3 L TENSOR
REMARK 3 L11: 1.9019 L22: 0.6514
REMARK 3 L33: 1.2052 L12: 0.4520
REMARK 3 L13: 1.1845 L23: 0.5472
REMARK 3 S TENSOR
REMARK 3 S11: 0.3206 S12: 0.9319 S13: -0.5632
REMARK 3 S21: -0.0131 S22: 0.2866 S23: -0.3309
REMARK 3 S31: 0.2069 S32: 0.8300 S33: 0.0445
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 433 THROUGH 528 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8724 7.7115 -6.3210
REMARK 3 T TENSOR
REMARK 3 T11: 0.8040 T22: 1.2502
REMARK 3 T33: 0.6222 T12: 0.1011
REMARK 3 T13: -0.0787 T23: -0.1739
REMARK 3 L TENSOR
REMARK 3 L11: 3.7320 L22: 1.8172
REMARK 3 L33: 0.8246 L12: 1.5091
REMARK 3 L13: 0.1863 L23: 0.3535
REMARK 3 S TENSOR
REMARK 3 S11: -0.2293 S12: 1.8263 S13: -0.2020
REMARK 3 S21: -0.3421 S22: 0.3191 S23: -0.0992
REMARK 3 S31: 0.1662 S32: 0.6748 S33: 0.2316
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 529 THROUGH 580 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3696 1.9850 0.5042
REMARK 3 T TENSOR
REMARK 3 T11: 0.7419 T22: 0.7237
REMARK 3 T33: 0.7004 T12: 0.1367
REMARK 3 T13: -0.1584 T23: -0.1545
REMARK 3 L TENSOR
REMARK 3 L11: 1.8623 L22: 0.2250
REMARK 3 L33: 1.0890 L12: 0.6801
REMARK 3 L13: -0.2285 L23: -0.2968
REMARK 3 S TENSOR
REMARK 3 S11: 0.2504 S12: 0.6448 S13: -0.3105
REMARK 3 S21: -0.2869 S22: 0.2606 S23: 0.1106
REMARK 3 S31: 0.2070 S32: -0.0855 S33: -0.0002
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 42 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8134 38.5747 -49.2665
REMARK 3 T TENSOR
REMARK 3 T11: 0.5986 T22: 0.5844
REMARK 3 T33: 0.5953 T12: -0.0370
REMARK 3 T13: 0.0244 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 0.0931 L22: 0.5014
REMARK 3 L33: 0.6738 L12: -0.1201
REMARK 3 L13: 0.1602 L23: -0.9549
REMARK 3 S TENSOR
REMARK 3 S11: -0.1661 S12: 0.7072 S13: -0.0218
REMARK 3 S21: -0.2797 S22: 0.2363 S23: 0.0304
REMARK 3 S31: 0.1151 S32: -0.0867 S33: 0.0002
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 43 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6635 41.8111 -43.1315
REMARK 3 T TENSOR
REMARK 3 T11: 0.5650 T22: 0.8998
REMARK 3 T33: 0.8092 T12: 0.0552
REMARK 3 T13: -0.0822 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.6719 L22: 2.0839
REMARK 3 L33: 2.7811 L12: -0.6659
REMARK 3 L13: -0.0669 L23: -0.1720
REMARK 3 S TENSOR
REMARK 3 S11: 0.3104 S12: 0.1047 S13: -0.2466
REMARK 3 S21: 0.1535 S22: -0.1325 S23: -0.6125
REMARK 3 S31: 0.5452 S32: 0.9781 S33: -0.0001
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 224 THROUGH 323 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9471 56.4758 -39.8261
REMARK 3 T TENSOR
REMARK 3 T11: 0.5526 T22: 0.5885
REMARK 3 T33: 0.4762 T12: -0.1469
REMARK 3 T13: 0.0250 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 1.3772 L22: 1.5948
REMARK 3 L33: 1.8677 L12: -0.0328
REMARK 3 L13: 0.1160 L23: -0.3893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0582 S12: -0.0984 S13: 0.1935
REMARK 3 S21: 0.1747 S22: -0.0641 S23: -0.0999
REMARK 3 S31: -0.2274 S32: 0.3521 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 324 THROUGH 493 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4932 36.2457 -25.7678
REMARK 3 T TENSOR
REMARK 3 T11: 0.5121 T22: 0.4665
REMARK 3 T33: 0.4420 T12: -0.0165
REMARK 3 T13: 0.0106 T23: 0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 1.1515 L22: 3.5579
REMARK 3 L33: 2.3699 L12: 0.8559
REMARK 3 L13: 0.4024 L23: 0.8457
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: -0.0887 S13: -0.0888
REMARK 3 S21: 0.3183 S22: 0.1012 S23: -0.2013
REMARK 3 S31: -0.0152 S32: 0.2433 S33: 0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 494 THROUGH 581 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1622 20.6116 -29.7579
REMARK 3 T TENSOR
REMARK 3 T11: 0.4824 T22: 0.5236
REMARK 3 T33: 0.5795 T12: -0.0028
REMARK 3 T13: -0.0717 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.3047 L22: 3.9324
REMARK 3 L33: 1.5847 L12: -0.8607
REMARK 3 L13: -0.7767 L23: 0.8088
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0247 S13: -0.1446
REMARK 3 S21: 0.4329 S22: 0.2027 S23: -0.4440
REMARK 3 S31: 0.0467 S32: 0.3721 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 6 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.2295 10.8898 -47.7209
REMARK 3 T TENSOR
REMARK 3 T11: 0.5045 T22: 0.6006
REMARK 3 T33: 0.6202 T12: -0.0128
REMARK 3 T13: 0.0512 T23: -0.1450
REMARK 3 L TENSOR
REMARK 3 L11: 0.7488 L22: 0.3861
REMARK 3 L33: 1.0594 L12: 0.0730
REMARK 3 L13: -0.0544 L23: -0.4528
REMARK 3 S TENSOR
REMARK 3 S11: 0.0629 S12: -0.1215 S13: 0.4015
REMARK 3 S21: -0.0734 S22: -0.1502 S23: 0.1696
REMARK 3 S31: -0.2246 S32: -0.3363 S33: 0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 83 THROUGH 142 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.1549 0.2483 -33.3487
REMARK 3 T TENSOR
REMARK 3 T11: 0.6988 T22: 1.1822
REMARK 3 T33: 0.5935 T12: -0.1112
REMARK 3 T13: 0.1523 T23: -0.2326
REMARK 3 L TENSOR
REMARK 3 L11: 0.3130 L22: 1.0901
REMARK 3 L33: 0.5660 L12: 0.4711
REMARK 3 L13: -0.3484 L23: -0.0634
REMARK 3 S TENSOR
REMARK 3 S11: -0.1153 S12: -0.6601 S13: 0.5121
REMARK 3 S21: 0.5663 S22: -0.0501 S23: 0.1202
REMARK 3 S31: 0.1404 S32: -0.6759 S33: -0.0030
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 143 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.2290 -16.4183 -41.4083
REMARK 3 T TENSOR
REMARK 3 T11: 0.7560 T22: 0.7861
REMARK 3 T33: 0.4409 T12: -0.1592
REMARK 3 T13: 0.1222 T23: 0.0902
REMARK 3 L TENSOR
REMARK 3 L11: 0.6652 L22: 1.2250
REMARK 3 L33: 0.7924 L12: -0.6498
REMARK 3 L13: -0.1703 L23: 0.2636
REMARK 3 S TENSOR
REMARK 3 S11: -0.1877 S12: -0.4795 S13: -0.1602
REMARK 3 S21: 0.3988 S22: -0.0522 S23: 0.1988
REMARK 3 S31: 0.7147 S32: -0.1213 S33: -0.0043
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 214 THROUGH 246 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.6879 -20.7712 -57.4784
REMARK 3 T TENSOR
REMARK 3 T11: 0.7464 T22: 0.5019
REMARK 3 T33: 0.6066 T12: -0.1470
REMARK 3 T13: 0.1093 T23: 0.1020
REMARK 3 L TENSOR
REMARK 3 L11: 0.5999 L22: 0.4489
REMARK 3 L33: 0.2895 L12: -0.5499
REMARK 3 L13: 0.3977 L23: -0.1385
REMARK 3 S TENSOR
REMARK 3 S11: -0.1954 S12: -0.0293 S13: -0.2341
REMARK 3 S21: -0.2554 S22: -0.0029 S23: -0.0399
REMARK 3 S31: 0.4884 S32: -0.1875 S33: 0.0000
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 247 THROUGH 299 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.3412 -5.2834 -60.0547
REMARK 3 T TENSOR
REMARK 3 T11: 0.4555 T22: 0.5029
REMARK 3 T33: 0.4852 T12: -0.0676
REMARK 3 T13: 0.0177 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 0.4504 L22: 1.6243
REMARK 3 L33: 1.6611 L12: 0.5895
REMARK 3 L13: 0.3546 L23: 0.4238
REMARK 3 S TENSOR
REMARK 3 S11: -0.1089 S12: 0.0370 S13: 0.2161
REMARK 3 S21: -0.2782 S22: -0.0032 S23: 0.1297
REMARK 3 S31: 0.2298 S32: -0.2306 S33: 0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 300 THROUGH 339 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2678 7.0806 -61.8221
REMARK 3 T TENSOR
REMARK 3 T11: 0.5997 T22: 0.5421
REMARK 3 T33: 0.5698 T12: -0.0235
REMARK 3 T13: 0.0103 T23: 0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 0.5301 L22: 0.6238
REMARK 3 L33: -0.1687 L12: 0.6559
REMARK 3 L13: 0.3076 L23: 0.5903
REMARK 3 S TENSOR
REMARK 3 S11: -0.2548 S12: 0.2608 S13: 0.3590
REMARK 3 S21: -0.3015 S22: 0.1129 S23: 0.1306
REMARK 3 S31: -0.1859 S32: -0.0594 S33: -0.0001
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 340 THROUGH 432 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.7940 -2.1714 -56.4293
REMARK 3 T TENSOR
REMARK 3 T11: 0.4996 T22: 0.4820
REMARK 3 T33: 0.5856 T12: 0.0063
REMARK 3 T13: 0.1176 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.2471 L22: 2.0434
REMARK 3 L33: 1.9881 L12: 1.6262
REMARK 3 L13: 0.5662 L23: 1.1894
REMARK 3 S TENSOR
REMARK 3 S11: -0.1929 S12: 0.0062 S13: -0.2291
REMARK 3 S21: -0.1409 S22: 0.3598 S23: -0.4536
REMARK 3 S31: 0.1002 S32: 0.2111 S33: 0.0001
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 433 THROUGH 541 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9273 -0.6078 -41.8569
REMARK 3 T TENSOR
REMARK 3 T11: 0.6138 T22: 0.5433
REMARK 3 T33: 0.7539 T12: 0.0786
REMARK 3 T13: -0.0428 T23: -0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 1.4751 L22: 2.3442
REMARK 3 L33: 2.4365 L12: 0.5833
REMARK 3 L13: 0.7413 L23: 1.5082
REMARK 3 S TENSOR
REMARK 3 S11: 0.1997 S12: -0.0923 S13: -0.4418
REMARK 3 S21: 0.4990 S22: 0.3302 S23: -0.5230
REMARK 3 S31: 0.7870 S32: 0.3987 S33: -0.0001
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 542 THROUGH 580 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7812 13.8875 -43.9286
REMARK 3 T TENSOR
REMARK 3 T11: 0.4265 T22: 0.5362
REMARK 3 T33: 0.5616 T12: -0.0384
REMARK 3 T13: 0.0678 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.5362 L22: 1.6252
REMARK 3 L33: 1.2839 L12: 0.0405
REMARK 3 L13: 0.7484 L23: 0.6420
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: -0.1365 S13: -0.0528
REMARK 3 S21: -0.0555 S22: 0.2182 S23: 0.0082
REMARK 3 S31: -0.3152 S32: 0.1596 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 5 through 7 or
REMARK 3 (resid 8 and (name N or name CA or name C
REMARK 3 or name O or name CB )) or resid 9
REMARK 3 through 10 or (resid 11 and (name N or
REMARK 3 name CA or name C or name O or name CB or
REMARK 3 name CG or name CD )) or resid 12 through
REMARK 3 31 or (resid 32 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 33 through 37 or resid 39 through 41 or
REMARK 3 (resid 42 through 43 and (name N or name
REMARK 3 CA or name C or name O or name CB )) or
REMARK 3 resid 44 through 60 or (resid 61 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB or name CG or name CD or name NE )
REMARK 3 ) or (resid 62 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 63 through 84 or (resid 89 and (name N or
REMARK 3 name CA or name C or name O )) or resid
REMARK 3 90 through 93 or (resid 94 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 95 or resid 97 through 98 or
REMARK 3 (resid 99 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 100
REMARK 3 through 103 or (resid 104 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 105 through 109 or (resid 110
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 111 through 112
REMARK 3 or (resid 113 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or (resid
REMARK 3 114 and (name N or name CA or name C or
REMARK 3 name O or name CB or name CG1 or name CG2)
REMARK 3 ) or resid 115 through 121 or resid 123
REMARK 3 through 127 or resid 132 or (resid 133
REMARK 3 through 136 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 137 through 138 or (resid 139 through 140
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or (resid 144 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 145 or (resid 146 through 150
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 151 or (resid
REMARK 3 153 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or resid 154 through
REMARK 3 158 or (resid 159 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 160 through 181 or (resid 182 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 183 through 186 or
REMARK 3 (resid 187 through 188 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 189 through 206 or (resid 207
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 208 through 215
REMARK 3 or (resid 216 through 217 and (name N or
REMARK 3 name CA or name C or name O or name CB or
REMARK 3 name CG )) or resid 218 through 278 or
REMARK 3 resid 280 through 293 or (resid 294 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 295 through 351 or
REMARK 3 resid 353 through 427 or resid 429
REMARK 3 through 477 or (resid 478 through 481 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 482 through 484 or
REMARK 3 (resid 485 through 486 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 487 or (resid 488 through 490
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 491 or (resid
REMARK 3 492 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or resid 493 through
REMARK 3 496 or (resid 497 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 (resid 498 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG )) or
REMARK 3 resid 499 through 500 or (resid 501 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 502 through 512 or
REMARK 3 (resid 513 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG )) or
REMARK 3 resid 514 through 522 or (resid 523
REMARK 3 through 524 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 525 or (resid 526 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 527 through 529 or (resid 530 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB or name CG )) or resid 531
REMARK 3 through 554 or (resid 558 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 559 through 566 or (resid 567
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB or name CG1 or name CG2)) or
REMARK 3 resid 568 through 581))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and (resid 5 through 37 or
REMARK 3 resid 39 through 95 or resid 97 through
REMARK 3 101 or (resid 102 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 103 through 121 or resid 123
REMARK 3 through 127 or resid 132 through 140 or
REMARK 3 resid 144 through 230 or (resid 231 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 232 through 237 or
REMARK 3 (resid 238 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 239
REMARK 3 through 278 or resid 280 through 323 or
REMARK 3 (resid 324 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 325
REMARK 3 through 326 or (resid 327 through 328 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 329 through 338 or
REMARK 3 (resid 339 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG )) or
REMARK 3 resid 340 through 344 or (resid 345 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 346 through 351 or
REMARK 3 resid 353 through 427 or resid 429
REMARK 3 through 430 or (resid 431 and (name N or
REMARK 3 name CA or name C or name O or name CB or
REMARK 3 name CG or name CD )) or resid 432
REMARK 3 through 478 or (resid 479 through 481 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 482 through 498 or
REMARK 3 (resid 499 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG1 or
REMARK 3 name CG2)) or resid 500 through 552 or
REMARK 3 (resid 553 and (name N or name CA or name
REMARK 3 C or name O )) or resid 554 through 581))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : ens_2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 6 through 53 or
REMARK 3 resid 55 through 60 or (resid 61 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 62 through 71 or
REMARK 3 resid 73 through 81 or (resid 82 through
REMARK 3 85 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or (resid 86 through
REMARK 3 89 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or resid 90 through
REMARK 3 98 or (resid 99 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 100 through 103 or (resid 104 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 105 through 109 or (resid 110
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 111 through 112
REMARK 3 or (resid 113 and (name N or name CA or
REMARK 3 name C or name O or name CB or name CG or
REMARK 3 name CD )) or resid 114 through 121 or
REMARK 3 (resid 122 through 123 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 124 through 130 or (resid 133
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 134 through 168
REMARK 3 or resid 170 through 187 or resid 189
REMARK 3 through 193 or (resid 194 through 195 and
REMARK 3 (name N or name CA or name C or name O ))
REMARK 3 or resid 196 through 206 or (resid 207
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB or name CG or name CD or
REMARK 3 name CE )) or resid 208 through 233 or
REMARK 3 resid 235 through 263 or resid 265
REMARK 3 through 293 or (resid 294 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 295 through 323 or (resid 324
REMARK 3 through 325 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 326 or (resid 327 and (name N or name CA
REMARK 3 or name C or name O or name CB or name CG
REMARK 3 )) or (resid 328 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 resid 329 or (resid 330 and (name N or
REMARK 3 name CA or name C or name O or name CB or
REMARK 3 name CG1 or name CG2)) or resid 331
REMARK 3 through 481 or resid 483 through 489 or
REMARK 3 (resid 490 through 499 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 500 through 509 or resid 511
REMARK 3 through 524 or (resid 525 through 526 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 527 through 580))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "D" and (resid 6 through 31 or
REMARK 3 (resid 32 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 33
REMARK 3 through 40 or (resid 41 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 42 through 71 or resid 73
REMARK 3 through 130 or resid 133 through 168 or
REMARK 3 resid 170 through 187 or resid 189
REMARK 3 through 191 or (resid 192 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 193 through 216 or (resid 217
REMARK 3 through 218 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 219 through 233 or resid 235 through 237
REMARK 3 or (resid 238 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 239 through 243 or (resid 244 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 245 through 263 or resid 265
REMARK 3 through 344 or (resid 345 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 346 through 404 or (resid 405
REMARK 3 through 406 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 407 through 409 or (resid 410 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 or name CG or name CD )) or resid 411 or
REMARK 3 (resid 412 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 413
REMARK 3 through 423 or (resid 424 through 428 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 429 through 430 or
REMARK 3 (resid 431 and (name N or name CA or name
REMARK 3 C or name O or name CB or name CG )) or
REMARK 3 resid 432 through 457 or (resid 458 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB )) or resid 459 through 475 or
REMARK 3 (resid 476 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 477 or
REMARK 3 (resid 478 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or (resid 479
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O )) or (resid 480 and (name N or name CA
REMARK 3 or name C or name O or name CB )) or
REMARK 3 (resid 481 through 483 and (name N or
REMARK 3 name CA or name C or name O )) or resid
REMARK 3 484 through 486 or (resid 487 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 )) or resid 488 or (resid 489 through 493
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or (resid 496 through 499
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 500 through 502
REMARK 3 or (resid 503 and (name N or name CA or
REMARK 3 name C or name O or name CB )) or resid
REMARK 3 504 through 505 or (resid 506 and (name N
REMARK 3 or name CA or name C or name O or name CB
REMARK 3 or name CG1 or name CG2)) or resid 507
REMARK 3 through 509 or resid 511 or (resid 512
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB or name CG1 or name CG2)) or
REMARK 3 (resid 513 and (name N or name CA or name
REMARK 3 C or name O or name CB )) or resid 514
REMARK 3 through 529 or (resid 530 and (name N or
REMARK 3 name CA or name C or name O or name CB ))
REMARK 3 or resid 531 through 538 or (resid 539
REMARK 3 and (name N or name CA or name C or name
REMARK 3 O or name CB )) or resid 540 through 541
REMARK 3 or (resid 542 and (name N or name CA or
REMARK 3 name C or name O or name CB or name CG or
REMARK 3 name CD or name NE )) or resid 543
REMARK 3 through 549 or (resid 550 through 551 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB or name CG1 or name CG2)) or
REMARK 3 resid 552 through 557 or (resid 558 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB or name CG1 or name CG2)) or
REMARK 3 resid 559 through 566 or (resid 567 and
REMARK 3 (name N or name CA or name C or name O or
REMARK 3 name CB or name CG1 or name CG2)) or
REMARK 3 resid 568 through 580))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9S6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-25.
REMARK 100 THE DEPOSITION ID IS D_1292149739.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.050
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR: 0.45MM EDTA, 33MM SODIUM
REMARK 280 ACETATE BUFFER PH=5.0, 1.2% PEG MW 4000; PROTEIN SOLUTION: 0.24
REMARK 280 MM IN 20MM TRIS PH=8.0, MEROPENEM SOLUTION: 62.5MM IN METHANOL.
REMARK 280 DROP CONTENT: RESERVOIR/PROTEIN/MEROPENEM SOLUTIONS= 1/1/0.5
REMARK 280 VOLUME RATIO. CRYSTALS WERE SOAKED IN 30%W/W HBPG SOLURION
REMARK 280 SATURATED WITH MEROPENEM., PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 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 ARG A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 ARG A 582
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ILE B 3
REMARK 465 ILE B 4
REMARK 465 MET B 5
REMARK 465 GLU B 131
REMARK 465 ASP B 132
REMARK 465 GLY B 494
REMARK 465 GLY B 495
REMARK 465 GLY B 555
REMARK 465 HIS B 556
REMARK 465 ARG B 581
REMARK 465 ARG B 582
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 ILE C 3
REMARK 465 ILE C 4
REMARK 465 LYS C 85
REMARK 465 GLY C 86
REMARK 465 ALA C 87
REMARK 465 GLU C 88
REMARK 465 GLY C 128
REMARK 465 ALA C 129
REMARK 465 GLY C 141
REMARK 465 GLY C 142
REMARK 465 GLY C 152
REMARK 465 GLY C 555
REMARK 465 HIS C 556
REMARK 465 ALA C 557
REMARK 465 ARG C 582
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 ILE D 3
REMARK 465 ILE D 4
REMARK 465 MET D 5
REMARK 465 GLY D 54
REMARK 465 ASP D 482
REMARK 465 GLY D 555
REMARK 465 HIS D 556
REMARK 465 ARG D 581
REMARK 465 ARG D 582
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 MET A 5 CG SD CE
REMARK 470 ARG A 11 CZ NH1 NH2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 LYS A 85 CG CD CE NZ
REMARK 470 ARG A 99 NE CZ NH1 NH2
REMARK 470 GLU A 102 CG CD OE1 OE2
REMARK 470 ARG A 216 NE CZ NH1 NH2
REMARK 470 GLU A 217 CD OE1 OE2
REMARK 470 ARG A 226 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 LYS A 238 CG CD CE NZ
REMARK 470 ARG A 244 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 294 CD CE NZ
REMARK 470 GLU A 324 CG CD OE1 OE2
REMARK 470 ARG A 327 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 328 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 339 CD OE1 OE2
REMARK 470 ARG A 345 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 431 NE CZ NH1 NH2
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 ILE A 499 CD1
REMARK 470 LYS A 513 CE NZ
REMARK 470 ARG A 526 CD NE CZ NH1 NH2
REMARK 470 LYS A 530 CE NZ
REMARK 470 ASP A 553 CB CG OD1 OD2
REMARK 470 HIS A 556 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 580 CG CD OE1 OE2
REMARK 470 ARG A 581 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 32 CG OD1 OD2
REMARK 470 LYS B 35 NZ
REMARK 470 PHE B 41 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 52 CG OD1 OD2
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 ARG B 61 CZ NH1 NH2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 ARG B 99 NE CZ NH1 NH2
REMARK 470 LYS B 110 NZ
REMARK 470 ARG B 113 NH1 NH2
REMARK 470 ARG B 133 NE CZ NH1 NH2
REMARK 470 ARG B 149 CD NE CZ NH1 NH2
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
REMARK 470 SER B 192 OG
REMARK 470 GLU B 194 CG CD OE1 OE2
REMARK 470 ARG B 216 NE CZ NH1 NH2
REMARK 470 GLU B 217 CG CD OE1 OE2
REMARK 470 LYS B 238 CG CD CE NZ
REMARK 470 ARG B 244 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 325 CG OD1 OD2
REMARK 470 ARG B 345 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 405 CG CD OE1 OE2
REMARK 470 GLU B 406 CG CD OE1 OE2
REMARK 470 LYS B 410 CE NZ
REMARK 470 ILE B 412 CG1 CG2 CD1
REMARK 470 SER B 424 OG
REMARK 470 ARG B 428 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 431 CD NE CZ NH1 NH2
REMARK 470 LYS B 458 CG CD CE NZ
REMARK 470 LYS B 463 NZ
REMARK 470 GLU B 475 CG CD OE1 OE2
REMARK 470 GLU B 476 CG CD OE1 OE2
REMARK 470 TYR B 478 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 479 CB CG CD OE1 OE2
REMARK 470 LEU B 480 CG CD1 CD2
REMARK 470 SER B 481 CB OG
REMARK 470 ASP B 482 CB CG OD1 OD2
REMARK 470 ALA B 483 CB
REMARK 470 ARG B 486 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 487 CG OD1 ND2
REMARK 470 ILE B 489 CG1 CG2 CD1
REMARK 470 GLU B 490 CD OE1 OE2
REMARK 470 GLN B 491 CG CD OE1 NE2
REMARK 470 LEU B 492 CG CD1 CD2
REMARK 470 THR B 493 OG1 CG2
REMARK 470 SER B 496 OG
REMARK 470 ARG B 497 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 498 CG CD OE1 OE2
REMARK 470 ILE B 499 CG1 CG2 CD1
REMARK 470 ARG B 501 CG CD NE CZ NH1 NH2
REMARK 470 SER B 502 OG
REMARK 470 ARG B 503 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 506 CD1
REMARK 470 ARG B 511 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 512 CD1
REMARK 470 LYS B 513 CG CD CE NZ
REMARK 470 ARG B 526 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 530 CG CD CE NZ
REMARK 470 LEU B 539 CG CD1 CD2
REMARK 470 ARG B 542 CZ NH1 NH2
REMARK 470 ILE B 550 CD1
REMARK 470 ILE B 551 CD1
REMARK 470 ILE B 558 CD1
REMARK 470 ILE B 567 CD1
REMARK 470 MET C 5 CG SD CE
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 ARG C 11 NE CZ NH1 NH2
REMARK 470 ASP C 32 CG OD1 OD2
REMARK 470 SER C 42 OG
REMARK 470 GLU C 43 CG CD OE1 OE2
REMARK 470 ARG C 61 CZ NH1 NH2
REMARK 470 GLU C 62 CG CD OE1 OE2
REMARK 470 GLN C 89 CB CG CD OE1 NE2
REMARK 470 LYS C 94 CG CD CE NZ
REMARK 470 ARG C 99 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 104 CG CD OE1 NE2
REMARK 470 LYS C 110 CG CD CE NZ
REMARK 470 ARG C 113 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 114 CD1
REMARK 470 THR C 130 OG1 CG2
REMARK 470 GLU C 131 CB CG CD OE1 OE2
REMARK 470 ARG C 133 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 134 CG1 CG2
REMARK 470 LEU C 136 CG CD1 CD2
REMARK 470 LEU C 139 CG CD1 CD2
REMARK 470 ASP C 140 CG OD1 OD2
REMARK 470 LEU C 144 CG CD1 CD2
REMARK 470 GLU C 146 CG CD OE1 OE2
REMARK 470 LEU C 147 CG CD1 CD2
REMARK 470 ARG C 149 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 150 CG CD1 CD2
REMARK 470 PHE C 153 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 159 CG1 CG2 CD1
REMARK 470 LEU C 182 CG CD1 CD2
REMARK 470 LEU C 187 CG CD1 CD2
REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 207 CG CD CE NZ
REMARK 470 ARG C 216 CD NE CZ NH1 NH2
REMARK 470 GLU C 217 CD OE1 OE2
REMARK 470 ARG C 226 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 244 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 294 CG CD CE NZ
REMARK 470 ARG C 327 CZ NH1 NH2
REMARK 470 TYR C 478 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 479 CD OE1 OE2
REMARK 470 LEU C 480 CG CD1 CD2
REMARK 470 SER C 481 OG
REMARK 470 PHE C 485 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 486 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 488 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE C 489 CG1 CG2 CD1
REMARK 470 GLU C 490 CG CD OE1 OE2
REMARK 470 LEU C 492 CG CD1 CD2
REMARK 470 ARG C 497 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 498 CD OE1 OE2
REMARK 470 ARG C 501 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 513 CD CE NZ
REMARK 470 ASN C 523 CG OD1 ND2
REMARK 470 ARG C 526 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 530 CD CE NZ
REMARK 470 ILE C 558 CG1 CG2 CD1
REMARK 470 ILE C 567 CD1
REMARK 470 GLU C 580 CG CD OE1 OE2
REMARK 470 ARG C 581 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 35 NZ
REMARK 470 ASP D 52 CG OD1 OD2
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 82 CG OD1 OD2
REMARK 470 VAL D 83 CG1 CG2
REMARK 470 SER D 84 OG
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 GLU D 88 CG CD OE1 OE2
REMARK 470 GLN D 89 CG CD OE1 NE2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 104 CG CD OE1 NE2
REMARK 470 LYS D 110 CG CD CE NZ
REMARK 470 ARG D 113 NE CZ NH1 NH2
REMARK 470 GLU D 122 CG CD OE1 OE2
REMARK 470 GLU D 131 CB CG CD OE1 OE2
REMARK 470 ASP D 132 CG OD1 OD2
REMARK 470 ARG D 133 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 149 CD NE CZ NH1 NH2
REMARK 470 ARG D 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 194 CB CG CD OE1 OE2
REMARK 470 LYS D 207 NZ
REMARK 470 ARG D 216 NE CZ NH1 NH2
REMARK 470 LYS D 238 NZ
REMARK 470 ARG D 244 NE CZ NH1 NH2
REMARK 470 LYS D 294 CG CD CE NZ
REMARK 470 GLU D 324 CG CD OE1 OE2
REMARK 470 ASP D 325 CG OD1 OD2
REMARK 470 ARG D 327 CD NE CZ NH1 NH2
REMARK 470 ARG D 328 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 330 CD1
REMARK 470 LYS D 463 NZ
REMARK 470 GLU D 475 CG CD OE1 OE2
REMARK 470 GLU D 479 CG CD OE1 OE2
REMARK 470 SER D 481 OG
REMARK 470 ARG D 486 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 490 CG CD OE1 OE2
REMARK 470 GLN D 491 CG CD OE1 NE2
REMARK 470 LEU D 492 CG CD1 CD2
REMARK 470 THR D 493 OG1 CG2
REMARK 470 ARG D 497 NE CZ NH1 NH2
REMARK 470 GLU D 498 CG CD OE1 OE2
REMARK 470 ARG D 501 CG CD NE CZ NH1 NH2
REMARK 470 SER D 502 OG
REMARK 470 ARG D 511 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 513 CD CE NZ
REMARK 470 SER D 525 OG
REMARK 470 ARG D 526 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 530 CE NZ
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 ASP A 32 -128.60 44.03
REMARK 500 ASP A 52 141.16 -170.96
REMARK 500 ARG A 61 -78.25 -97.57
REMARK 500 SER A 66 -179.08 -171.41
REMARK 500 THR A 130 -169.65 -101.14
REMARK 500 ALA A 148 148.47 -171.12
REMARK 500 SER A 340 -164.59 -102.42
REMARK 500 ASP A 414 52.66 -140.49
REMARK 500 SER A 445 -116.01 51.99
REMARK 500 ASP A 553 14.27 52.67
REMARK 500 ASP B 32 -133.96 41.92
REMARK 500 ASP B 52 103.72 -160.02
REMARK 500 THR B 214 -166.94 -124.89
REMARK 500 ARG B 216 -65.10 -103.21
REMARK 500 CYS B 416 56.50 39.44
REMARK 500 SER B 445 -118.80 58.01
REMARK 500 ASN B 523 55.77 -141.82
REMARK 500 ASP C 32 120.26 -37.66
REMARK 500 ASP C 52 141.51 -170.99
REMARK 500 ARG C 61 -74.84 -98.54
REMARK 500 ALA C 148 147.54 -172.58
REMARK 500 SER C 340 -165.47 -103.41
REMARK 500 ASP C 414 53.02 -140.30
REMARK 500 SER C 445 -117.22 51.82
REMARK 500 HIS C 508 27.64 -140.28
REMARK 500 ASP C 553 15.70 51.06
REMARK 500 ASP D 32 -126.08 41.73
REMARK 500 ASP D 34 69.46 -152.09
REMARK 500 ASP D 52 105.46 -160.98
REMARK 500 THR D 130 -160.20 -128.68
REMARK 500 ARG D 133 -169.43 -168.54
REMARK 500 THR D 214 -166.80 -125.35
REMARK 500 ARG D 216 -64.57 -103.93
REMARK 500 ASP D 414 59.84 -142.61
REMARK 500 SER D 445 -118.32 57.61
REMARK 500 ASN D 523 56.36 -143.61
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 673 DISTANCE = 6.38 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1AX B 601
REMARK 610 1AX C 601
REMARK 610 1AX D 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O4H RELATED DB: PDB
REMARK 900 ISOSTRUCTURAL STRUCTURE OF THE SAME MUTANT FORM OF APAAP
REMARK 900 (UNCOMPLEXED). USED AS MODEL OF MOLECULAR REPLACEMENT.
DBREF 9S6B A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 9S6B B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 9S6B C 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 9S6B D 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
SEQADV 9S6B ALA A 524 UNP Q9YBQ2 ASP 524 ENGINEERED MUTATION
SEQADV 9S6B ALA B 524 UNP Q9YBQ2 ASP 524 ENGINEERED MUTATION
SEQADV 9S6B ALA C 524 UNP Q9YBQ2 ASP 524 ENGINEERED MUTATION
SEQADV 9S6B ALA D 524 UNP Q9YBQ2 ASP 524 ENGINEERED MUTATION
SEQRES 1 A 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 A 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 A 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 A 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 A 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 A 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 A 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 A 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 A 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 A 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 A 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 A 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 A 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 A 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 A 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 A 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 A 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 A 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 A 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 A 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 A 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 A 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 A 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 A 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 A 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 A 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 A 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 A 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 A 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 A 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 A 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 A 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 A 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 A 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 A 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 A 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 A 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 A 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 A 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 A 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 A 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 A 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 A 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 A 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 A 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 B 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 B 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 B 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 B 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 B 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 B 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 B 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 B 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 B 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 B 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 B 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 B 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 B 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 B 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 B 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 B 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 B 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 B 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 B 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 B 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 B 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 B 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 B 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 B 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 B 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 B 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 B 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 B 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 B 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 B 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 B 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 B 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 B 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 B 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 B 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 B 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 B 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 B 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 B 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 B 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 B 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 B 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 B 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 B 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 B 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 C 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 C 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 C 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 C 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 C 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 C 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 C 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 C 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 C 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 C 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 C 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 C 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 C 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 C 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 C 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 C 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 C 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 C 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 C 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 C 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 C 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 C 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 C 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 C 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 C 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 C 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 C 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 C 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 C 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 C 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 C 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 C 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 C 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 C 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 C 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 C 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 C 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 C 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 C 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 C 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 C 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 C 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 C 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 C 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 C 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 D 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 D 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 D 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 D 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 D 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 D 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 D 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 D 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 D 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 D 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 D 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 D 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 D 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 D 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 D 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 D 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 D 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 D 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 D 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 D 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 D 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 D 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 D 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 D 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 D 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 D 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 D 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 D 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 D 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 D 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 D 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 D 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 D 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 D 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 D 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 D 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 D 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 D 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 D 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 D 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 D 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 D 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 D 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 D 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 D 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
HET 1AX B 601 7
HET 1AX C 601 9
HET 1AX D 601 7
HETNAM 1AX (2R,2'R)-3,3'-OXYDIPROPANE-1,2-DIOL
FORMUL 5 1AX 3(C6 H14 O5)
FORMUL 8 HOH *251(H2 O)
HELIX 1 AA1 GLU A 8 VAL A 22 1 15
HELIX 2 AA2 LYS A 238 ARG A 244 1 7
HELIX 3 AA3 PRO A 323 SER A 329 1 7
HELIX 4 AA4 ASP A 379 ALA A 388 1 10
HELIX 5 AA5 GLY A 404 LYS A 410 1 7
HELIX 6 AA6 GLY A 417 SER A 433 1 17
HELIX 7 AA7 SER A 445 LYS A 458 1 14
HELIX 8 AA8 ASP A 473 LEU A 480 1 8
HELIX 9 AA9 ASP A 482 GLY A 494 1 13
HELIX 10 AB1 SER A 496 ARG A 503 1 8
HELIX 11 AB2 SER A 504 ILE A 512 5 9
HELIX 12 AB3 PRO A 528 ARG A 542 1 15
HELIX 13 AB4 THR A 560 GLU A 580 1 21
HELIX 14 AB5 GLU B 8 VAL B 22 1 15
HELIX 15 AB6 LYS B 238 ARG B 244 1 7
HELIX 16 AB7 PRO B 323 SER B 329 1 7
HELIX 17 AB8 ASP B 379 ALA B 388 1 10
HELIX 18 AB9 GLY B 404 LYS B 410 1 7
HELIX 19 AC1 GLY B 417 SER B 433 1 17
HELIX 20 AC2 SER B 445 LYS B 458 1 14
HELIX 21 AC3 ASP B 473 SER B 481 1 9
HELIX 22 AC4 ASP B 482 THR B 493 1 12
HELIX 23 AC5 ARG B 497 SER B 504 1 8
HELIX 24 AC6 PRO B 505 ILE B 512 5 8
HELIX 25 AC7 PRO B 528 ARG B 542 1 15
HELIX 26 AC8 THR B 560 LEU B 568 1 9
HELIX 27 AC9 LEU B 568 ARG B 579 1 12
HELIX 28 AD1 GLU C 8 VAL C 22 1 15
HELIX 29 AD2 LYS C 238 ARG C 244 1 7
HELIX 30 AD3 PRO C 323 SER C 329 1 7
HELIX 31 AD4 ASP C 379 ALA C 388 1 10
HELIX 32 AD5 GLY C 404 LYS C 410 1 7
HELIX 33 AD6 GLY C 417 SER C 433 1 17
HELIX 34 AD7 SER C 445 LYS C 458 1 14
HELIX 35 AD8 ASP C 473 LEU C 480 1 8
HELIX 36 AD9 ASP C 482 GLY C 494 1 13
HELIX 37 AE1 SER C 496 ARG C 503 1 8
HELIX 38 AE2 SER C 504 ILE C 512 5 9
HELIX 39 AE3 LEU C 529 ARG C 542 1 14
HELIX 40 AE4 THR C 560 GLU C 580 1 21
HELIX 41 AE5 GLU D 8 VAL D 22 1 15
HELIX 42 AE6 LYS D 238 ARG D 244 1 7
HELIX 43 AE7 PRO D 323 SER D 329 1 7
HELIX 44 AE8 ASP D 379 ALA D 388 1 10
HELIX 45 AE9 GLY D 404 LYS D 410 1 7
HELIX 46 AF1 GLY D 417 SER D 433 1 17
HELIX 47 AF2 SER D 445 LYS D 458 1 14
HELIX 48 AF3 ASP D 473 SER D 481 1 9
HELIX 49 AF4 ALA D 484 GLY D 494 1 11
HELIX 50 AF5 SER D 496 ARG D 503 1 8
HELIX 51 AF6 SER D 504 ILE D 512 5 9
HELIX 52 AF7 LEU D 529 ARG D 542 1 14
HELIX 53 AF8 THR D 560 LEU D 568 1 9
HELIX 54 AF9 LEU D 568 ARG D 579 1 12
SHEET 1 AA1 4 LYS A 24 VAL A 31 0
SHEET 2 AA1 4 LYS A 35 SER A 42 -1 O LEU A 37 N GLY A 29
SHEET 3 AA1 4 SER A 45 ASP A 52 -1 O TYR A 49 N VAL A 38
SHEET 4 AA1 4 GLU A 55 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 AA2 4 SER A 66 VAL A 67 0
SHEET 2 AA2 4 ARG A 76 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 AA2 4 HIS A 90 ASN A 96 -1 O PHE A 93 N LEU A 79
SHEET 4 AA2 4 GLU A 103 ARG A 105 -1 O GLN A 104 N LYS A 94
SHEET 1 AA3 5 ASP A 69 PRO A 70 0
SHEET 2 AA3 5 ARG A 113 ASP A 119 1 O ASP A 119 N ASP A 69
SHEET 3 AA3 5 VAL A 124 ALA A 129 -1 O VAL A 125 N VAL A 118
SHEET 4 AA3 5 VAL A 134 ASP A 140 -1 O TYR A 137 N PHE A 126
SHEET 5 AA3 5 GLY A 143 LEU A 150 -1 O LEU A 150 N VAL A 134
SHEET 1 AA4 4 GLY A 154 ARG A 160 0
SHEET 2 AA4 4 LEU A 163 GLY A 171 -1 O ALA A 165 N ASP A 158
SHEET 3 AA4 4 ARG A 174 ASN A 181 -1 O SER A 176 N GLY A 168
SHEET 4 AA4 4 ARG A 188 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 AA5 4 SER A 196 ILE A 202 0
SHEET 2 AA5 4 VAL A 208 GLU A 213 -1 O GLY A 211 N SER A 198
SHEET 3 AA5 4 ALA A 218 VAL A 223 -1 O ARG A 219 N LEU A 212
SHEET 4 AA5 4 VAL A 230 ASP A 232 -1 O GLU A 231 N THR A 222
SHEET 1 AA6 4 ALA A 247 TYR A 253 0
SHEET 2 AA6 4 LEU A 259 ARG A 265 -1 O VAL A 262 N TRP A 250
SHEET 3 AA6 4 ARG A 268 ILE A 273 -1 O ALA A 270 N ALA A 263
SHEET 4 AA6 4 GLU A 276 VAL A 278 -1 O VAL A 278 N VAL A 271
SHEET 1 AA7 4 ASN A 284 TRP A 291 0
SHEET 2 AA7 4 LYS A 294 SER A 301 -1 O LYS A 294 N TRP A 291
SHEET 3 AA7 4 THR A 304 LEU A 311 -1 O ARG A 307 N HIS A 299
SHEET 4 AA7 4 PRO A 316 LEU A 318 -1 O LEU A 317 N ILE A 308
SHEET 1 AA816 ILE A 330 GLU A 339 0
SHEET 2 AA816 ARG A 345 SER A 353 -1 O VAL A 346 N VAL A 338
SHEET 3 AA816 HIS A 391 PRO A 395 -1 O VAL A 392 N LEU A 351
SHEET 4 AA816 GLY A 360 VAL A 366 1 N VAL A 363 O HIS A 391
SHEET 5 AA816 ALA A 436 TYR A 444 1 O TYR A 440 N VAL A 364
SHEET 6 AA816 ALA A 464 GLY A 468 1 O GLY A 468 N GLY A 443
SHEET 7 AA816 LEU A 516 PRO A 521 1 O ALA A 517 N ALA A 467
SHEET 8 AA816 PHE A 546 ILE A 551 1 O GLU A 547 N LEU A 518
SHEET 9 AA816 PHE B 546 ILE B 551 -1 O ALA B 548 N ILE A 550
SHEET 10 AA816 LEU B 516 PRO B 521 1 N LEU B 518 O GLU B 547
SHEET 11 AA816 ALA B 464 GLY B 468 1 N ALA B 467 O ALA B 517
SHEET 12 AA816 ALA B 436 TYR B 444 1 N GLY B 443 O GLY B 468
SHEET 13 AA816 GLY B 360 VAL B 366 1 N VAL B 364 O TYR B 440
SHEET 14 AA816 HIS B 391 PRO B 395 1 O HIS B 391 N VAL B 363
SHEET 15 AA816 ARG B 345 SER B 353 -1 N TYR B 349 O MET B 394
SHEET 16 AA816 ILE B 330 GLU B 339 -1 N VAL B 338 O VAL B 346
SHEET 1 AA9 4 LYS B 24 VAL B 31 0
SHEET 2 AA9 4 LYS B 35 SER B 42 -1 O LEU B 37 N GLY B 29
SHEET 3 AA9 4 SER B 45 TYR B 51 -1 O TYR B 49 N VAL B 38
SHEET 4 AA9 4 THR B 56 LYS B 58 -1 O VAL B 57 N LEU B 50
SHEET 1 AB1 4 SER B 66 VAL B 67 0
SHEET 2 AB1 4 ARG B 76 ASP B 82 -1 O VAL B 80 N SER B 66
SHEET 3 AB1 4 HIS B 90 ASN B 96 -1 O PHE B 93 N LEU B 79
SHEET 4 AB1 4 GLN B 104 ARG B 105 -1 O GLN B 104 N LYS B 94
SHEET 1 AB2 5 ASP B 69 PRO B 70 0
SHEET 2 AB2 5 ARG B 113 ASP B 119 1 O GLY B 117 N ASP B 69
SHEET 3 AB2 5 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 AB2 5 ALA B 135 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 AB2 5 GLY B 143 ARG B 149 -1 O ALA B 148 N LEU B 136
SHEET 1 AB3 4 PHE B 153 ARG B 160 0
SHEET 2 AB3 4 LEU B 163 PHE B 169 -1 O PHE B 169 N PHE B 153
SHEET 3 AB3 4 SER B 176 ASN B 181 -1 O SER B 180 N ILE B 164
SHEET 4 AB3 4 GLY B 185 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 AB4 3 SER B 196 PHE B 197 0
SHEET 2 AB4 3 VAL B 208 GLU B 213 -1 O GLU B 213 N SER B 196
SHEET 3 AB4 3 SER B 201 ILE B 202 -1 N SER B 201 O THR B 209
SHEET 1 AB5 4 SER B 196 PHE B 197 0
SHEET 2 AB5 4 VAL B 208 GLU B 213 -1 O GLU B 213 N SER B 196
SHEET 3 AB5 4 ARG B 219 VAL B 223 -1 O ARG B 219 N LEU B 212
SHEET 4 AB5 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 AB6 4 ALA B 247 TYR B 253 0
SHEET 2 AB6 4 LEU B 259 ARG B 265 -1 O ARG B 264 N ALA B 247
SHEET 3 AB6 4 ARG B 268 ILE B 273 -1 O PHE B 272 N VAL B 261
SHEET 4 AB6 4 GLU B 276 VAL B 278 -1 O GLU B 276 N ILE B 273
SHEET 1 AB7 4 ASN B 284 TRP B 291 0
SHEET 2 AB7 4 LYS B 294 SER B 301 -1 O LYS B 294 N TRP B 291
SHEET 3 AB7 4 THR B 304 LEU B 311 -1 O ARG B 307 N HIS B 299
SHEET 4 AB7 4 PRO B 316 LEU B 318 -1 O LEU B 317 N ILE B 308
SHEET 1 AB8 4 LYS C 24 VAL C 31 0
SHEET 2 AB8 4 LYS C 35 SER C 42 -1 O LEU C 37 N GLY C 29
SHEET 3 AB8 4 SER C 45 ASP C 52 -1 O TYR C 49 N VAL C 38
SHEET 4 AB8 4 GLU C 55 LYS C 58 -1 O VAL C 57 N LEU C 50
SHEET 1 AB9 4 SER C 66 VAL C 67 0
SHEET 2 AB9 4 ARG C 76 ASP C 82 -1 O VAL C 80 N SER C 66
SHEET 3 AB9 4 HIS C 90 ASN C 96 -1 O PHE C 93 N LEU C 79
SHEET 4 AB9 4 GLU C 103 ARG C 105 -1 O GLN C 104 N LYS C 94
SHEET 1 AC1 5 ASP C 69 PRO C 70 0
SHEET 2 AC1 5 GLY C 117 ASP C 119 1 O ASP C 119 N ASP C 69
SHEET 3 AC1 5 VAL C 124 PHE C 126 -1 O VAL C 125 N VAL C 118
SHEET 4 AC1 5 VAL C 134 LEU C 139 -1 O TYR C 137 N PHE C 126
SHEET 5 AC1 5 ARG C 145 LEU C 150 -1 O LEU C 150 N VAL C 134
SHEET 1 AC2 4 GLY C 154 ARG C 160 0
SHEET 2 AC2 4 LEU C 163 GLY C 171 -1 O LEU C 167 N PHE C 155
SHEET 3 AC2 4 ARG C 174 ASN C 181 -1 O SER C 176 N GLY C 168
SHEET 4 AC2 4 ARG C 188 PHE C 190 -1 O PHE C 190 N LEU C 177
SHEET 1 AC3 4 SER C 196 ILE C 202 0
SHEET 2 AC3 4 VAL C 208 GLU C 213 -1 O GLY C 211 N SER C 198
SHEET 3 AC3 4 ALA C 218 VAL C 223 -1 O ARG C 219 N LEU C 212
SHEET 4 AC3 4 VAL C 230 ASP C 232 -1 O GLU C 231 N THR C 222
SHEET 1 AC4 4 ALA C 247 TYR C 253 0
SHEET 2 AC4 4 LEU C 259 ARG C 265 -1 O VAL C 262 N TRP C 250
SHEET 3 AC4 4 ARG C 268 ILE C 273 -1 O ALA C 270 N ALA C 263
SHEET 4 AC4 4 GLU C 276 VAL C 278 -1 O GLU C 276 N ILE C 273
SHEET 1 AC5 4 ASN C 284 TRP C 291 0
SHEET 2 AC5 4 LYS C 294 SER C 301 -1 O LYS C 294 N TRP C 291
SHEET 3 AC5 4 THR C 304 LEU C 311 -1 O LEU C 311 N LEU C 295
SHEET 4 AC5 4 PRO C 316 LEU C 318 -1 O LEU C 317 N ILE C 308
SHEET 1 AC616 ILE C 330 GLU C 339 0
SHEET 2 AC616 ARG C 345 SER C 353 -1 O THR C 348 N VAL C 336
SHEET 3 AC616 HIS C 391 PRO C 395 -1 O VAL C 392 N LEU C 351
SHEET 4 AC616 GLY C 360 VAL C 366 1 N VAL C 363 O HIS C 391
SHEET 5 AC616 ALA C 436 TYR C 444 1 O TYR C 440 N VAL C 364
SHEET 6 AC616 ALA C 464 GLY C 468 1 O GLY C 468 N GLY C 443
SHEET 7 AC616 LEU C 516 PRO C 521 1 O ALA C 517 N ALA C 467
SHEET 8 AC616 PHE C 546 ILE C 551 1 O GLU C 547 N LEU C 518
SHEET 9 AC616 PHE D 546 ILE D 551 -1 O ALA D 548 N ILE C 550
SHEET 10 AC616 LEU D 516 PRO D 521 1 N LEU D 518 O GLU D 547
SHEET 11 AC616 ALA D 464 GLY D 468 1 N GLY D 465 O ALA D 517
SHEET 12 AC616 ALA D 436 TYR D 444 1 N GLY D 443 O GLY D 468
SHEET 13 AC616 GLY D 360 VAL D 366 1 N VAL D 364 O TYR D 440
SHEET 14 AC616 HIS D 391 PRO D 395 1 O HIS D 391 N VAL D 363
SHEET 15 AC616 ARG D 345 SER D 353 -1 N TYR D 349 O MET D 394
SHEET 16 AC616 ILE D 330 GLU D 339 -1 N VAL D 338 O VAL D 346
SHEET 1 AC7 4 LYS D 24 VAL D 31 0
SHEET 2 AC7 4 LYS D 35 SER D 42 -1 O LEU D 37 N GLY D 29
SHEET 3 AC7 4 SER D 45 TYR D 51 -1 O TYR D 49 N VAL D 38
SHEET 4 AC7 4 THR D 56 LYS D 58 -1 O VAL D 57 N LEU D 50
SHEET 1 AC8 4 SER D 66 VAL D 67 0
SHEET 2 AC8 4 ARG D 76 ASP D 82 -1 O VAL D 80 N SER D 66
SHEET 3 AC8 4 HIS D 90 ASN D 96 -1 O PHE D 93 N LEU D 79
SHEET 4 AC8 4 GLN D 104 ARG D 105 -1 O GLN D 104 N LYS D 94
SHEET 1 AC9 5 ASP D 69 PRO D 70 0
SHEET 2 AC9 5 ARG D 113 ASP D 119 1 O GLY D 117 N ASP D 69
SHEET 3 AC9 5 VAL D 124 ALA D 129 -1 O VAL D 125 N VAL D 118
SHEET 4 AC9 5 VAL D 134 ASP D 140 -1 O TYR D 137 N PHE D 126
SHEET 5 AC9 5 GLY D 143 LEU D 150 -1 O LEU D 150 N VAL D 134
SHEET 1 AD1 4 PHE D 153 ARG D 160 0
SHEET 2 AD1 4 LEU D 163 PHE D 169 -1 O PHE D 169 N PHE D 153
SHEET 3 AD1 4 SER D 176 ASN D 181 -1 O SER D 180 N ILE D 164
SHEET 4 AD1 4 GLY D 185 PHE D 190 -1 O PHE D 190 N LEU D 177
SHEET 1 AD2 4 SER D 196 ILE D 202 0
SHEET 2 AD2 4 VAL D 208 GLU D 213 -1 O THR D 209 N SER D 201
SHEET 3 AD2 4 ARG D 219 VAL D 223 -1 O VAL D 223 N VAL D 208
SHEET 4 AD2 4 VAL D 230 ASP D 232 -1 O GLU D 231 N THR D 222
SHEET 1 AD3 4 ALA D 247 TYR D 253 0
SHEET 2 AD3 4 LEU D 259 ARG D 265 -1 O VAL D 262 N TRP D 250
SHEET 3 AD3 4 ARG D 268 ILE D 273 -1 O ARG D 268 N ARG D 265
SHEET 4 AD3 4 GLU D 276 VAL D 278 -1 O GLU D 276 N ILE D 273
SHEET 1 AD4 4 ASN D 284 TRP D 291 0
SHEET 2 AD4 4 LYS D 294 SER D 301 -1 O LYS D 294 N TRP D 291
SHEET 3 AD4 4 THR D 304 LEU D 311 -1 O ARG D 307 N HIS D 299
SHEET 4 AD4 4 PRO D 316 LEU D 318 -1 O LEU D 317 N ILE D 308
SSBOND 1 CYS A 416 CYS A 453 1555 1555 2.03
SSBOND 2 CYS B 416 CYS B 453 1555 1555 2.02
SSBOND 3 CYS C 416 CYS C 453 1555 1555 2.03
SSBOND 4 CYS D 416 CYS D 453 1555 1555 2.03
CISPEP 1 LEU A 311 PRO A 312 0 1.47
CISPEP 2 THR A 358 PRO A 359 0 2.20
CISPEP 3 GLY A 369 PRO A 370 0 7.05
CISPEP 4 LEU B 311 PRO B 312 0 2.19
CISPEP 5 THR B 358 PRO B 359 0 3.31
CISPEP 6 GLY B 369 PRO B 370 0 3.78
CISPEP 7 LEU C 311 PRO C 312 0 1.28
CISPEP 8 THR C 358 PRO C 359 0 3.22
CISPEP 9 GLY C 369 PRO C 370 0 7.04
CISPEP 10 LEU D 311 PRO D 312 0 2.70
CISPEP 11 THR D 358 PRO D 359 0 3.03
CISPEP 12 GLY D 369 PRO D 370 0 3.17
CRYST1 71.042 98.283 98.902 105.51 103.19 100.39 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014076 0.002581 0.004363 0.00000
SCALE2 0.000000 0.010344 0.003521 0.00000
SCALE3 0.000000 0.000000 0.010970 0.00000
MTRIX1 1 0.123801 -0.624962 -0.770776 -20.11356 1
MTRIX2 1 -0.622631 -0.653741 0.430061 16.70101 1
MTRIX3 1 -0.772660 0.426667 -0.470055 -38.30861 1
MTRIX1 2 0.124305 -0.642438 -0.756189 -20.02092 1
MTRIX2 2 -0.624659 -0.642793 0.443416 16.26748 1
MTRIX3 2 -0.770940 0.417242 -0.481207 -38.04529 1
TER 4295 ARG A 581
TER 8435 GLU B 580
TER 12529 ARG C 581
TER 16720 GLU D 580
MASTER 1228 0 3 54 151 0 0 1216913 4 30 180
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