HEADER HYDROLASE/ANTIBIOTIC 23-MAR-12 4EBN
TITLE BLAC AMOXICILLIN ACYL-INTERMEDIATE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PENICILLINASE;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: BLAA, BLAC, MT2128, MTCY49.07C, RV2068C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS AMBLER CLASS A BETA-LACTAMASE, BETA-LACTAMASE, SERINE HYDROLASE,
KEYWDS 2 ESTERASE, HYDROLASE-ANTIBIOTIC COMPLEX, STRUCTURAL GENOMICS, TB
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, TBSGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.MIRE,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 2 13-SEP-23 4EBN 1 REMARK SEQADV LINK
REVDAT 1 03-APR-13 4EBN 0
JRNL AUTH J.A.MIRE,P.PAI,N.SIDDIQI,D.H.RUSSELL,E.J.RUBIN,
JRNL AUTH 2 J.C.SACCHETTINI
JRNL TITL FAROPENEM IS EFFECTIVE AGAINST MYCOBACTERIUM TUBERCULOSIS IN
JRNL TITL 2 VITRO AND IN VIVO
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 36951
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1839
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.2695 - 6.6955 1.00 2775 158 0.1939 0.2047
REMARK 3 2 6.6955 - 5.3167 1.00 2728 155 0.2293 0.2515
REMARK 3 3 5.3167 - 4.6453 1.00 2692 169 0.1766 0.1932
REMARK 3 4 4.6453 - 4.2209 1.00 2744 131 0.1701 0.2188
REMARK 3 5 4.2209 - 3.9185 1.00 2731 136 0.1811 0.2307
REMARK 3 6 3.9185 - 3.6876 1.00 2714 131 0.1997 0.2468
REMARK 3 7 3.6876 - 3.5030 1.00 2722 137 0.2071 0.2250
REMARK 3 8 3.5030 - 3.3505 0.99 2704 138 0.2229 0.2734
REMARK 3 9 3.3505 - 3.2216 0.99 2678 145 0.2533 0.2770
REMARK 3 10 3.2216 - 3.1104 0.99 2681 134 0.2735 0.3413
REMARK 3 11 3.1104 - 3.0132 0.98 2668 129 0.2925 0.3015
REMARK 3 12 3.0132 - 2.9271 0.98 2635 137 0.3156 0.3782
REMARK 3 13 2.9271 - 2.8500 0.97 2640 139 0.3469 0.3790
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 : 0.86
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 33.46
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 60.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.04800
REMARK 3 B22 (A**2) : -2.37450
REMARK 3 B33 (A**2) : 0.32640
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.28930
REMARK 3 B23 (A**2) : 0.00000
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 : 0.017 8015
REMARK 3 ANGLE : 1.662 10973
REMARK 3 CHIRALITY : 0.093 1283
REMARK 3 PLANARITY : 0.012 1441
REMARK 3 DIHEDRAL : 17.795 2813
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 29:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3076 -1.4391 -5.7599
REMARK 3 T TENSOR
REMARK 3 T11: 0.2242 T22: 0.3496
REMARK 3 T33: 0.4192 T12: -0.0363
REMARK 3 T13: -0.0920 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.4762 L22: 0.3534
REMARK 3 L33: 0.9173 L12: 0.2992
REMARK 3 L13: -0.2938 L23: 0.2038
REMARK 3 S TENSOR
REMARK 3 S11: 0.0893 S12: 0.5168 S13: -0.3346
REMARK 3 S21: -0.4857 S22: 0.0144 S23: 0.0303
REMARK 3 S31: 0.2004 S32: 0.0196 S33: 0.0024
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 58:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4178 17.8957 15.9672
REMARK 3 T TENSOR
REMARK 3 T11: 0.1302 T22: 0.3115
REMARK 3 T33: 0.1418 T12: -0.0227
REMARK 3 T13: 0.0818 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 1.0299 L22: 0.7564
REMARK 3 L33: 1.0531 L12: 0.5788
REMARK 3 L13: 0.8972 L23: -0.0692
REMARK 3 S TENSOR
REMARK 3 S11: -0.3966 S12: -0.0052 S13: 0.6770
REMARK 3 S21: 0.3557 S22: 0.0226 S23: -0.3841
REMARK 3 S31: -0.4708 S32: 0.2386 S33: -0.0162
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 145:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.8507 20.8380 2.9663
REMARK 3 T TENSOR
REMARK 3 T11: 0.3539 T22: 0.5236
REMARK 3 T33: 0.5257 T12: -0.0505
REMARK 3 T13: -0.0261 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.1032 L22: 0.1447
REMARK 3 L33: 0.2194 L12: 0.1297
REMARK 3 L13: 0.0877 L23: 0.1367
REMARK 3 S TENSOR
REMARK 3 S11: -0.2825 S12: 0.0400 S13: 0.3749
REMARK 3 S21: -0.2709 S22: 0.2599 S23: 0.0594
REMARK 3 S31: -0.2904 S32: -0.1978 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 180:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4879 3.5915 7.4452
REMARK 3 T TENSOR
REMARK 3 T11: 0.1709 T22: 0.2158
REMARK 3 T33: 0.2772 T12: -0.0116
REMARK 3 T13: 0.0283 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.0830 L22: 1.0739
REMARK 3 L33: 1.4999 L12: 0.7965
REMARK 3 L13: 0.0016 L23: 0.6682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0258 S12: -0.0483 S13: -0.0041
REMARK 3 S21: 0.0195 S22: 0.0319 S23: -0.0634
REMARK 3 S31: -0.0498 S32: -0.1146 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 29:144)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9568 7.9516 28.0649
REMARK 3 T TENSOR
REMARK 3 T11: 0.3962 T22: 0.3705
REMARK 3 T33: 0.3948 T12: 0.0065
REMARK 3 T13: 0.0248 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.8920 L22: 1.4309
REMARK 3 L33: 0.7563 L12: -0.1105
REMARK 3 L13: 0.5957 L23: -0.2485
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: -0.0246 S13: 0.1449
REMARK 3 S21: 0.0500 S22: 0.0430 S23: 0.0687
REMARK 3 S31: -0.1571 S32: -0.0811 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 145:164)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1133 16.4380 32.5286
REMARK 3 T TENSOR
REMARK 3 T11: 0.7268 T22: 0.6043
REMARK 3 T33: 0.7113 T12: 0.0861
REMARK 3 T13: 0.1614 T23: -0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 0.7101 L22: 0.0983
REMARK 3 L33: 0.7722 L12: 0.0700
REMARK 3 L13: 0.4396 L23: -0.1015
REMARK 3 S TENSOR
REMARK 3 S11: 0.1696 S12: -0.9403 S13: 0.0459
REMARK 3 S21: -0.1625 S22: 0.2935 S23: 0.1806
REMARK 3 S31: -0.4452 S32: -0.8313 S33: 0.4148
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 165:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5368 19.4181 35.7513
REMARK 3 T TENSOR
REMARK 3 T11: 1.3369 T22: 1.2203
REMARK 3 T33: 0.6906 T12: 0.0412
REMARK 3 T13: 0.0642 T23: 0.1713
REMARK 3 L TENSOR
REMARK 3 L11: 0.7977 L22: 0.0720
REMARK 3 L33: 0.5975 L12: 0.2168
REMARK 3 L13: 0.6831 L23: 0.1921
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: 0.9769 S13: 0.3119
REMARK 3 S21: 0.1414 S22: 0.5578 S23: -0.5350
REMARK 3 S31: 0.9522 S32: 0.3755 S33: 0.0470
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESSEQ 180:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1983 -0.4088 33.5395
REMARK 3 T TENSOR
REMARK 3 T11: 0.3485 T22: 0.3118
REMARK 3 T33: 0.3074 T12: -0.0120
REMARK 3 T13: 0.0382 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.8043 L22: 0.6397
REMARK 3 L33: 1.2181 L12: -0.2427
REMARK 3 L13: 0.3547 L23: -0.9892
REMARK 3 S TENSOR
REMARK 3 S11: 0.0995 S12: 0.0587 S13: -0.0328
REMARK 3 S21: 0.0845 S22: 0.0918 S23: 0.1786
REMARK 3 S31: 0.0777 S32: 0.0342 S33: 0.0196
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 29:154)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2848 -32.5759 9.3381
REMARK 3 T TENSOR
REMARK 3 T11: 0.3148 T22: 0.2266
REMARK 3 T33: 0.2788 T12: -0.0247
REMARK 3 T13: -0.0452 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 1.9240 L22: 1.5205
REMARK 3 L33: 1.5161 L12: -0.3431
REMARK 3 L13: 0.7813 L23: -0.2994
REMARK 3 S TENSOR
REMARK 3 S11: 0.1081 S12: -0.0935 S13: -0.1247
REMARK 3 S21: -0.0126 S22: 0.0439 S23: 0.0496
REMARK 3 S31: 0.1798 S32: -0.1971 S33: 0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 155:179)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2456 -41.6902 3.2723
REMARK 3 T TENSOR
REMARK 3 T11: 0.7077 T22: 0.9981
REMARK 3 T33: 0.7088 T12: -0.0149
REMARK 3 T13: -0.0886 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.6649 L22: 0.0930
REMARK 3 L33: 0.1497 L12: 0.1445
REMARK 3 L13: -0.2150 L23: -0.1364
REMARK 3 S TENSOR
REMARK 3 S11: 0.4023 S12: -1.2399 S13: -0.0166
REMARK 3 S21: -0.3739 S22: -0.1474 S23: -0.0803
REMARK 3 S31: 0.1294 S32: 0.3411 S33: 0.0316
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN C AND (RESSEQ 180:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1694 -23.3949 6.1250
REMARK 3 T TENSOR
REMARK 3 T11: 0.2469 T22: 0.2204
REMARK 3 T33: 0.1966 T12: 0.0154
REMARK 3 T13: -0.0023 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 1.4448 L22: 0.9703
REMARK 3 L33: 0.8439 L12: 0.8402
REMARK 3 L13: -0.4999 L23: -0.2173
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: -0.0843 S13: -0.0534
REMARK 3 S21: 0.0723 S22: 0.0510 S23: 0.0824
REMARK 3 S31: 0.1837 S32: 0.0445 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 29:68)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3829 -24.7916 50.6537
REMARK 3 T TENSOR
REMARK 3 T11: 0.4381 T22: 0.4010
REMARK 3 T33: 0.4004 T12: 0.0025
REMARK 3 T13: 0.0290 T23: 0.0496
REMARK 3 L TENSOR
REMARK 3 L11: 0.4871 L22: 0.8318
REMARK 3 L33: 0.6618 L12: 0.4593
REMARK 3 L13: 0.1807 L23: -0.2161
REMARK 3 S TENSOR
REMARK 3 S11: 0.1538 S12: -0.1086 S13: 0.2747
REMARK 3 S21: 0.7087 S22: -0.1446 S23: 0.0861
REMARK 3 S31: -0.0279 S32: 0.1894 S33: 0.0426
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 69:229)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8046 -38.2373 37.8212
REMARK 3 T TENSOR
REMARK 3 T11: 0.4440 T22: 0.3101
REMARK 3 T33: 0.2919 T12: 0.0289
REMARK 3 T13: -0.0021 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 2.2230 L22: 0.9498
REMARK 3 L33: 1.2400 L12: -0.4108
REMARK 3 L13: 0.5498 L23: 0.0415
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: 0.0833 S13: -0.0362
REMARK 3 S21: -0.1368 S22: 0.0120 S23: -0.0204
REMARK 3 S31: 0.1546 S32: 0.1797 S33: 0.0004
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN D AND (RESSEQ 230:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0892 -26.6455 41.2907
REMARK 3 T TENSOR
REMARK 3 T11: 0.3299 T22: 0.2771
REMARK 3 T33: 0.3589 T12: 0.0183
REMARK 3 T13: -0.0241 T23: 0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.5754 L22: 0.8796
REMARK 3 L33: 0.9756 L12: -0.7460
REMARK 3 L13: 0.4783 L23: -0.2329
REMARK 3 S TENSOR
REMARK 3 S11: 0.0816 S12: 0.0781 S13: -0.2278
REMARK 3 S21: -0.0928 S22: -0.0135 S23: 0.1426
REMARK 3 S31: 0.1324 S32: -0.2461 S33: -0.0000
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 4EBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37239
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 12.040
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2GDN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 48.33600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ARG A 103 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 ARG B 33 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 103 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 114 CG CD OE1 NE2
REMARK 470 ASP B 163 CG OD1 OD2
REMARK 470 GLU B 165 CG CD OE1 OE2
REMARK 470 GLU B 168 CG CD OE1 OE2
REMARK 470 LEU B 169 CG CD1 CD2
REMARK 470 ARG B 171 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 172 CG OD1 OD2
REMARK 470 GLU B 177 CG CD OE1 OE2
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 TYR B 272 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 275 CG CD OE1 OE2
REMARK 470 ARG C 103 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 114 CG CD OE1 NE2
REMARK 470 GLU C 165 CG CD OE1 OE2
REMARK 470 GLU C 168 CG CD OE1 OE2
REMARK 470 ARG C 171 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 172 CG OD1 OD2
REMARK 470 GLU C 177 CG CD OE1 OE2
REMARK 470 ASN C 197 CG OD1 ND2
REMARK 470 ASP C 228 CG OD1 OD2
REMARK 470 GLU C 275 CG CD OE1 OE2
REMARK 470 GLU D 36 CG CD OE1 OE2
REMARK 470 GLN D 83 CG CD OE1 NE2
REMARK 470 LYS D 93 CG CD CE NZ
REMARK 470 ARG D 103 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 110 CG CD OE1 NE2
REMARK 470 GLN D 114 CG CD OE1 NE2
REMARK 470 LYS D 219 CG CD CE NZ
REMARK 470 ASP D 273 CG OD1 OD2
REMARK 470 GLU D 275 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR C 71 N - CA - CB ANGL. DEV. = 12.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 CYS A 69 -134.65 56.74
REMARK 500 GLN A 83 27.74 166.91
REMARK 500 ASN A 86 112.99 -171.01
REMARK 500 PRO A 87 143.41 -25.21
REMARK 500 SER A 104 -120.65 -126.23
REMARK 500 ARG A 220 -114.57 -102.43
REMARK 500 CYS B 69 -133.35 55.65
REMARK 500 LEU B 162 -159.61 -96.38
REMARK 500 ASP B 163 -36.44 145.92
REMARK 500 GLU B 165 -127.26 -62.72
REMARK 500 PRO B 167 27.85 -57.66
REMARK 500 LEU B 169 -20.87 97.62
REMARK 500 ARG B 220 -109.49 -109.16
REMARK 500 ASP B 246 106.74 -164.31
REMARK 500 CYS C 69 -172.70 49.05
REMARK 500 SER C 70 2.73 -45.65
REMARK 500 ASP C 172 139.55 -33.26
REMARK 500 ARG C 220 -113.92 -101.45
REMARK 500 GLU D 36 -108.88 -62.01
REMARK 500 LEU D 37 -54.44 20.33
REMARK 500 CYS D 69 -139.20 57.35
REMARK 500 SER D 99 -12.19 -40.18
REMARK 500 ILE D 105 97.18 -44.92
REMARK 500 VAL D 108 -39.94 -134.73
REMARK 500 ARG D 220 -112.67 -101.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VFF RELATED DB: PDB
REMARK 900 BLAC E166A CDC-OME ACYL-INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 3VFH RELATED DB: PDB
REMARK 900 BLAC E166A CDC-1 ACYL-INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 4EBI RELATED DB: PDB
REMARK 900 BLAC TEBIPENEM ACYL-INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 4EBL RELATED DB: PDB
REMARK 900 BLAC E166A FAROPENEM ACYL-INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 4EBM RELATED DB: PDB
REMARK 900 BLAC BIAPENEM ACYL-INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 4EBO RELATED DB: PDB
REMARK 900 BLAC E166A CEFOPERAZONE ACYL-INTERMEDIATE COMPLEX
REMARK 900 RELATED ID: 4EBP RELATED DB: PDB
REMARK 900 BLAC E166A CEFOTAXIME ACYL-INTERMEDIATE COMPLEX
DBREF 4EBN A 29 293 UNP P0C5C1 BLAC_MYCTU 43 307
DBREF 4EBN B 29 293 UNP P0C5C1 BLAC_MYCTU 43 307
DBREF 4EBN C 29 293 UNP P0C5C1 BLAC_MYCTU 43 307
DBREF 4EBN D 29 293 UNP P0C5C1 BLAC_MYCTU 43 307
SEQADV 4EBN ALA A 166 UNP P0C5C1 GLU 182 ENGINEERED MUTATION
SEQADV 4EBN ALA B 166 UNP P0C5C1 GLU 182 ENGINEERED MUTATION
SEQADV 4EBN ALA C 166 UNP P0C5C1 GLU 182 ENGINEERED MUTATION
SEQADV 4EBN ALA D 166 UNP P0C5C1 GLU 182 ENGINEERED MUTATION
SEQRES 1 A 265 ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR
SEQRES 2 A 265 ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR
SEQRES 3 A 265 THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA
SEQRES 4 A 265 PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL
SEQRES 5 A 265 LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE
SEQRES 6 A 265 THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL
SEQRES 7 A 265 ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN
SEQRES 8 A 265 LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA
SEQRES 9 A 265 ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY
SEQRES 10 A 265 GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY
SEQRES 11 A 265 ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU
SEQRES 12 A 265 ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR
SEQRES 13 A 265 PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU
SEQRES 14 A 265 GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR
SEQRES 15 A 265 ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE
SEQRES 16 A 265 ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS
SEQRES 17 A 265 THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA
SEQRES 18 A 265 VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA
SEQRES 19 A 265 VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU
SEQRES 20 A 265 PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL
SEQRES 21 A 265 ALA GLY VAL LEU ALA
SEQRES 1 B 265 ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR
SEQRES 2 B 265 ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR
SEQRES 3 B 265 THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA
SEQRES 4 B 265 PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL
SEQRES 5 B 265 LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE
SEQRES 6 B 265 THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL
SEQRES 7 B 265 ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN
SEQRES 8 B 265 LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA
SEQRES 9 B 265 ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY
SEQRES 10 B 265 GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY
SEQRES 11 B 265 ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU
SEQRES 12 B 265 ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR
SEQRES 13 B 265 PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU
SEQRES 14 B 265 GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR
SEQRES 15 B 265 ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE
SEQRES 16 B 265 ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS
SEQRES 17 B 265 THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA
SEQRES 18 B 265 VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA
SEQRES 19 B 265 VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU
SEQRES 20 B 265 PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL
SEQRES 21 B 265 ALA GLY VAL LEU ALA
SEQRES 1 C 265 ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR
SEQRES 2 C 265 ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR
SEQRES 3 C 265 THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA
SEQRES 4 C 265 PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL
SEQRES 5 C 265 LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE
SEQRES 6 C 265 THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL
SEQRES 7 C 265 ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN
SEQRES 8 C 265 LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA
SEQRES 9 C 265 ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY
SEQRES 10 C 265 GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY
SEQRES 11 C 265 ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU
SEQRES 12 C 265 ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR
SEQRES 13 C 265 PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU
SEQRES 14 C 265 GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR
SEQRES 15 C 265 ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE
SEQRES 16 C 265 ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS
SEQRES 17 C 265 THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA
SEQRES 18 C 265 VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA
SEQRES 19 C 265 VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU
SEQRES 20 C 265 PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL
SEQRES 21 C 265 ALA GLY VAL LEU ALA
SEQRES 1 D 265 ASP LEU ALA ASP ARG PHE ALA GLU LEU GLU ARG ARG TYR
SEQRES 2 D 265 ASP ALA ARG LEU GLY VAL TYR VAL PRO ALA THR GLY THR
SEQRES 3 D 265 THR ALA ALA ILE GLU TYR ARG ALA ASP GLU ARG PHE ALA
SEQRES 4 D 265 PHE CYS SER THR PHE LYS ALA PRO LEU VAL ALA ALA VAL
SEQRES 5 D 265 LEU HIS GLN ASN PRO LEU THR HIS LEU ASP LYS LEU ILE
SEQRES 6 D 265 THR TYR THR SER ASP ASP ILE ARG SER ILE SER PRO VAL
SEQRES 7 D 265 ALA GLN GLN HIS VAL GLN THR GLY MET THR ILE GLY GLN
SEQRES 8 D 265 LEU CYS ASP ALA ALA ILE ARG TYR SER ASP GLY THR ALA
SEQRES 9 D 265 ALA ASN LEU LEU LEU ALA ASP LEU GLY GLY PRO GLY GLY
SEQRES 10 D 265 GLY THR ALA ALA PHE THR GLY TYR LEU ARG SER LEU GLY
SEQRES 11 D 265 ASP THR VAL SER ARG LEU ASP ALA GLU ALA PRO GLU LEU
SEQRES 12 D 265 ASN ARG ASP PRO PRO GLY ASP GLU ARG ASP THR THR THR
SEQRES 13 D 265 PRO HIS ALA ILE ALA LEU VAL LEU GLN GLN LEU VAL LEU
SEQRES 14 D 265 GLY ASN ALA LEU PRO PRO ASP LYS ARG ALA LEU LEU THR
SEQRES 15 D 265 ASP TRP MET ALA ARG ASN THR THR GLY ALA LYS ARG ILE
SEQRES 16 D 265 ARG ALA GLY PHE PRO ALA ASP TRP LYS VAL ILE ASP LYS
SEQRES 17 D 265 THR GLY THR GLY ASP TYR GLY ARG ALA ASN ASP ILE ALA
SEQRES 18 D 265 VAL VAL TRP SER PRO THR GLY VAL PRO TYR VAL VAL ALA
SEQRES 19 D 265 VAL MET SER ASP ARG ALA GLY GLY GLY TYR ASP ALA GLU
SEQRES 20 D 265 PRO ARG GLU ALA LEU LEU ALA GLU ALA ALA THR CYS VAL
SEQRES 21 D 265 ALA GLY VAL LEU ALA
HET PO4 A 301 5
HET PO4 A 302 5
HET PO4 A 303 5
HET AXL B 301 25
HET AXL C 301 25
HET PO4 C 302 5
HET PO4 D 301 5
HET PO4 D 302 5
HETNAM PO4 PHOSPHATE ION
HETNAM AXL 2-{1-[2-AMINO-2-(4-HYDROXY-PHENYL)-ACETYLAMINO]-2-OXO-
HETNAM 2 AXL ETHYL}-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC ACID
HETSYN AXL AMOXICILLIN, BOUND FORM
FORMUL 5 PO4 6(O4 P 3-)
FORMUL 8 AXL 2(C16 H21 N3 O5 S)
HELIX 1 1 ASP A 29 ASP A 42 1 14
HELIX 2 2 PHE A 72 HIS A 82 1 11
HELIX 3 3 THR A 89 ASP A 92 5 4
HELIX 4 4 ILE A 119 TYR A 129 1 11
HELIX 5 5 ASP A 131 ASP A 141 1 11
HELIX 6 6 PRO A 145 GLY A 145B 5 3
HELIX 7 7 GLY A 145C LEU A 155 1 12
HELIX 8 8 PRO A 167 ARG A 171 5 5
HELIX 9 9 THR A 182 LEU A 195 1 14
HELIX 10 10 PRO A 200 ARG A 213 1 14
HELIX 11 11 ARG A 220 PHE A 225 1 6
HELIX 12 12 ARG A 267 ALA A 274 5 8
HELIX 13 13 ARG A 277 ALA A 293 1 17
HELIX 14 14 LEU B 30 ASP B 42 1 13
HELIX 15 15 PHE B 72 GLN B 83 1 12
HELIX 16 16 PRO B 87 ASP B 92 5 6
HELIX 17 17 VAL B 108 HIS B 112 5 5
HELIX 18 18 ILE B 119 TYR B 129 1 11
HELIX 19 19 ASP B 131 ASP B 141 1 11
HELIX 20 20 LEU B 142 GLY B 143 5 2
HELIX 21 21 GLY B 144 GLY B 145B 5 4
HELIX 22 22 GLY B 145C LEU B 155 1 12
HELIX 23 23 THR B 182 LEU B 195 1 14
HELIX 24 24 PRO B 200 ARG B 213 1 14
HELIX 25 25 ARG B 220 PHE B 225 1 6
HELIX 26 26 ARG B 267 GLY B 271 5 5
HELIX 27 27 ARG B 277 ALA B 293 1 17
HELIX 28 28 LEU C 30 ASP C 42 1 13
HELIX 29 29 CYS C 69 THR C 71 5 3
HELIX 30 30 PHE C 72 ASN C 86 1 13
HELIX 31 31 PRO C 87 ASP C 92 5 6
HELIX 32 32 THR C 98 ILE C 102 5 5
HELIX 33 33 ALA C 109 VAL C 113 5 5
HELIX 34 34 ILE C 119 TYR C 129 1 11
HELIX 35 35 GLY C 132 ASP C 141 1 10
HELIX 36 36 GLY C 144 LEU C 155 1 16
HELIX 37 37 PRO C 167 ASP C 172 1 6
HELIX 38 38 THR C 182 LEU C 195 1 14
HELIX 39 39 PRO C 200 ARG C 213 1 14
HELIX 40 40 ARG C 220 PHE C 225 1 6
HELIX 41 41 ARG C 277 ALA C 293 1 17
HELIX 42 42 LEU D 30 ASP D 42 1 13
HELIX 43 43 CYS D 69 THR D 71 5 3
HELIX 44 44 PHE D 72 GLN D 83 1 12
HELIX 45 45 PRO D 87 ASP D 92 5 6
HELIX 46 46 VAL D 108 VAL D 113 1 6
HELIX 47 47 ILE D 119 TYR D 129 1 11
HELIX 48 48 ASP D 131 GLY D 143 1 13
HELIX 49 49 PRO D 145 GLY D 145B 5 3
HELIX 50 50 GLY D 145C SER D 154 1 11
HELIX 51 51 PRO D 167 ARG D 171 5 5
HELIX 52 52 THR D 182 LEU D 195 1 14
HELIX 53 53 PRO D 200 ARG D 213 1 14
HELIX 54 54 ARG D 220 PHE D 225 1 6
HELIX 55 55 ARG D 277 ALA D 293 1 17
SHEET 1 A 5 ILE A 58 TYR A 60 0
SHEET 2 A 5 ARG A 44 VAL A 49 -1 N VAL A 47 O TYR A 60
SHEET 3 A 5 PRO A 258 ASP A 266 -1 O MET A 264 N GLY A 46
SHEET 4 A 5 ALA A 244 TRP A 251 -1 N ALA A 248 O VAL A 261
SHEET 5 A 5 LYS A 230 THR A 237 -1 N GLY A 236 O ASN A 245
SHEET 1 B 2 PHE A 66 ALA A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 LEU A 94 ILE A 95 0
SHEET 2 C 2 MET A 117 THR A 118 -1 O MET A 117 N ILE A 95
SHEET 1 D 5 ILE B 58 TYR B 60 0
SHEET 2 D 5 ARG B 44 VAL B 49 -1 N VAL B 47 O TYR B 60
SHEET 3 D 5 PRO B 258 ASP B 266 -1 O MET B 264 N GLY B 46
SHEET 4 D 5 ARG B 243 TRP B 251 -1 N ALA B 248 O VAL B 261
SHEET 5 D 5 LYS B 230 GLY B 238 -1 N LYS B 234 O ILE B 247
SHEET 1 E 2 PHE B 66 ALA B 67 0
SHEET 2 E 2 THR B 180 THR B 181 -1 O THR B 181 N PHE B 66
SHEET 1 F 2 LEU B 94 ILE B 95 0
SHEET 2 F 2 MET B 117 THR B 118 -1 O MET B 117 N ILE B 95
SHEET 1 G 5 ILE C 58 TYR C 60 0
SHEET 2 G 5 ARG C 44 VAL C 49 -1 N VAL C 47 O TYR C 60
SHEET 3 G 5 PRO C 258 ASP C 266 -1 O MET C 264 N GLY C 46
SHEET 4 G 5 ARG C 243 TRP C 251 -1 N ALA C 248 O VAL C 261
SHEET 5 G 5 LYS C 230 GLY C 238 -1 N GLY C 236 O ASN C 245
SHEET 1 H 2 PHE C 66 ALA C 67 0
SHEET 2 H 2 THR C 180 THR C 181 -1 O THR C 181 N PHE C 66
SHEET 1 I 2 LEU C 94 ILE C 95 0
SHEET 2 I 2 MET C 117 THR C 118 -1 O MET C 117 N ILE C 95
SHEET 1 J 5 ILE D 58 TYR D 60 0
SHEET 2 J 5 ARG D 44 VAL D 49 -1 N VAL D 47 O TYR D 60
SHEET 3 J 5 PRO D 258 ASP D 266 -1 O MET D 264 N GLY D 46
SHEET 4 J 5 ALA D 244 TRP D 251 -1 N ASP D 246 O VAL D 263
SHEET 5 J 5 LYS D 230 THR D 237 -1 N ILE D 232 O VAL D 249
SHEET 1 K 2 PHE D 66 ALA D 67 0
SHEET 2 K 2 THR D 180 THR D 181 -1 O THR D 181 N PHE D 66
SHEET 1 L 2 LEU D 94 ILE D 95 0
SHEET 2 L 2 MET D 117 THR D 118 -1 O MET D 117 N ILE D 95
LINK OG SER B 70 C1 AXL B 301 1555 1555 1.35
LINK OG SER C 70 C1 AXL C 301 1555 1555 1.35
CISPEP 1 ALA A 166 PRO A 167 0 1.54
CISPEP 2 ALA C 166 PRO C 167 0 5.08
CISPEP 3 ALA D 166 PRO D 167 0 8.76
SITE 1 AC1 7 SER A 70 SER A 130 THR A 216 THR A 235
SITE 2 AC1 7 THR A 237 GLN B 110 GLN B 111
SITE 1 AC2 2 ASP A 124 ARG A 213
SITE 1 AC3 3 LEU A 88 ASP A 202 LYS A 203
SITE 1 AC4 7 CYS B 69 SER B 70 SER B 130 ASN B 170
SITE 2 AC4 7 THR B 235 GLY B 236 THR B 237
SITE 1 AC5 5 SER C 70 SER C 130 ASN C 170 THR C 235
SITE 2 AC5 5 THR C 237
SITE 1 AC6 3 ASP C 124 ARG C 128 ARG C 213
SITE 1 AC7 6 GLN C 111 SER D 130 THR D 216 THR D 235
SITE 2 AC7 6 GLY D 236 THR D 237
SITE 1 AC8 3 ASP D 124 ARG D 128 ARG D 213
CRYST1 79.567 96.672 109.808 90.00 107.52 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012568 0.000000 0.003968 0.00000
SCALE2 0.000000 0.010344 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009550 0.00000
(ATOM LINES ARE NOT SHOWN.)
END