HEADER HYDROLASE 27-APR-09 2WGV
TITLE CRYSTAL STRUCTURE OF THE OXA-10 V117T MUTANT AT PH 6.5 INHIBITED BY A
TITLE 2 CHLORIDE ION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE OXA-10;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-LACTAMASE PSE-2;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET 22B
KEYWDS ANTIBIOTIC RESISTANCE, PLASMID ENCODED, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.VERCHEVAL,F.KERFF,C.BAUVOIS,E.SAUVAGE,R.GUIET,P.CHARLIER,M.GALLENI
REVDAT 4 13-DEC-23 2WGV 1 REMARK
REVDAT 3 13-JUL-11 2WGV 1 VERSN
REVDAT 2 08-DEC-10 2WGV 1 KEYWDS JRNL REMARK SITE
REVDAT 1 19-MAY-10 2WGV 0
JRNL AUTH L.VERCHEVAL,C.BAUVOIS,A.DI PAOLO,F.BOREL,J.L.FERRER,
JRNL AUTH 2 E.SAUVAGE,A.MATAGNE,J.M.FRERE,P.CHARLIER,M.GALLENI,F.KERFF
JRNL TITL THREE FACTORS THAT MODULATE THE ACTIVITY OF CLASS D
JRNL TITL 2 BETA-LACTAMASES AND INTERFERE WITH THE POST- TRANSLATIONAL
JRNL TITL 3 CARBOXYLATION OF LYS70.
JRNL REF BIOCHEM.J. V. 432 495 2010
JRNL REFN ISSN 0264-6021
JRNL PMID 21108605
JRNL DOI 10.1042/BJ20101122
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 55922
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2979
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3877
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 25.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.606
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4058 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5495 ; 1.262 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 510 ; 5.398 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;39.763 ;25.056
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 733 ;13.815 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;15.620 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 601 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3021 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1842 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2820 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 297 ; 0.155 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 15 ; 0.274 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.147 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2570 ; 0.591 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4002 ; 0.935 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1746 ; 1.513 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1483 ; 2.400 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 20 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0840 51.6950 42.8650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1775 T22: 0.1596
REMARK 3 T33: 0.0819 T12: 0.0273
REMARK 3 T13: 0.0792 T23: 0.0901
REMARK 3 L TENSOR
REMARK 3 L11: 19.9395 L22: 2.3281
REMARK 3 L33: 10.8735 L12: -1.5090
REMARK 3 L13: 13.4532 L23: -3.0125
REMARK 3 S TENSOR
REMARK 3 S11: -0.1484 S12: 0.9026 S13: 1.3758
REMARK 3 S21: -0.3127 S22: -0.4545 S23: -0.3359
REMARK 3 S31: -0.2830 S32: 0.8172 S33: 0.6029
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 34 A 83
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5290 42.1100 53.8890
REMARK 3 T TENSOR
REMARK 3 T11: -0.0111 T22: -0.0126
REMARK 3 T33: 0.0295 T12: 0.0102
REMARK 3 T13: -0.0116 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 0.7055 L22: 1.1880
REMARK 3 L33: 2.8165 L12: 0.1398
REMARK 3 L13: -0.9892 L23: -0.8087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0395 S12: 0.1075 S13: 0.0381
REMARK 3 S21: -0.0750 S22: -0.0470 S23: 0.0159
REMARK 3 S31: -0.1034 S32: -0.0533 S33: 0.0075
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 84 A 104
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8900 32.5490 76.9360
REMARK 3 T TENSOR
REMARK 3 T11: -0.0022 T22: -0.0705
REMARK 3 T33: -0.0228 T12: 0.0334
REMARK 3 T13: 0.0059 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 11.2033 L22: 5.8295
REMARK 3 L33: 4.7446 L12: -7.0019
REMARK 3 L13: -1.2378 L23: 1.5217
REMARK 3 S TENSOR
REMARK 3 S11: -0.5371 S12: -0.4534 S13: 0.0967
REMARK 3 S21: 0.4791 S22: 0.4493 S23: -0.0994
REMARK 3 S31: 0.1404 S32: 0.1875 S33: 0.0878
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 105 A 133
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0990 32.1820 69.0090
REMARK 3 T TENSOR
REMARK 3 T11: -0.0065 T22: -0.0209
REMARK 3 T33: 0.0213 T12: 0.0143
REMARK 3 T13: 0.0113 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 2.7078 L22: 0.9108
REMARK 3 L33: 1.2688 L12: 0.3532
REMARK 3 L13: 0.6265 L23: 0.1301
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: -0.0158 S13: -0.0811
REMARK 3 S21: 0.0728 S22: 0.1015 S23: 0.0290
REMARK 3 S31: 0.0495 S32: 0.0125 S33: -0.0726
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 134 A 205
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9770 40.5210 59.8990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0152 T22: -0.0325
REMARK 3 T33: 0.0212 T12: 0.0174
REMARK 3 T13: 0.0028 T23: 0.0249
REMARK 3 L TENSOR
REMARK 3 L11: 1.0333 L22: 1.6421
REMARK 3 L33: 1.6278 L12: -0.0787
REMARK 3 L13: -0.2254 L23: 0.2054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: 0.0469 S13: 0.0378
REMARK 3 S21: -0.0384 S22: 0.0103 S23: 0.0808
REMARK 3 S31: -0.1706 S32: -0.0860 S33: -0.0303
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 206 A 229
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5500 41.0480 55.5610
REMARK 3 T TENSOR
REMARK 3 T11: -0.0017 T22: -0.0233
REMARK 3 T33: 0.0322 T12: -0.0041
REMARK 3 T13: 0.0070 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 4.2114 L22: 7.8521
REMARK 3 L33: 2.4590 L12: -5.1397
REMARK 3 L13: -1.1706 L23: 1.0297
REMARK 3 S TENSOR
REMARK 3 S11: 0.1974 S12: 0.2045 S13: 0.0771
REMARK 3 S21: -0.2266 S22: -0.2230 S23: -0.1162
REMARK 3 S31: -0.1259 S32: 0.0706 S33: 0.0257
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 230 A 248
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1910 46.1150 54.5620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0220 T22: -0.0534
REMARK 3 T33: 0.0232 T12: -0.0247
REMARK 3 T13: 0.0143 T23: 0.0292
REMARK 3 L TENSOR
REMARK 3 L11: 4.2762 L22: 4.9525
REMARK 3 L33: 1.8696 L12: -3.8425
REMARK 3 L13: -0.2640 L23: -0.0229
REMARK 3 S TENSOR
REMARK 3 S11: 0.0896 S12: 0.0780 S13: 0.2268
REMARK 3 S21: -0.0581 S22: -0.1073 S23: -0.2022
REMARK 3 S31: -0.2920 S32: 0.1456 S33: 0.0177
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 249 A 264
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0100 53.3620 54.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0452 T22: -0.0080
REMARK 3 T33: 0.1022 T12: -0.0656
REMARK 3 T13: 0.0445 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 2.9356 L22: 10.9601
REMARK 3 L33: 0.6236 L12: -4.3102
REMARK 3 L13: 0.9535 L23: -1.2317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0521 S12: -0.0396 S13: 0.4288
REMARK 3 S21: 0.0667 S22: -0.0594 S23: -0.5792
REMARK 3 S31: -0.3129 S32: 0.2446 S33: 0.0074
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 19 B 34
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1360 58.2860 99.0370
REMARK 3 T TENSOR
REMARK 3 T11: 0.1866 T22: 0.3041
REMARK 3 T33: -0.0182 T12: -0.0771
REMARK 3 T13: 0.0008 T23: -0.1861
REMARK 3 L TENSOR
REMARK 3 L11: 11.7794 L22: 12.3964
REMARK 3 L33: 7.5034 L12: 6.1953
REMARK 3 L13: -8.2577 L23: -8.3013
REMARK 3 S TENSOR
REMARK 3 S11: 0.2081 S12: -0.3501 S13: -0.3119
REMARK 3 S21: 0.5405 S22: -0.1255 S23: -1.1053
REMARK 3 S31: -0.3356 S32: 1.4187 S33: -0.0827
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 35 B 79
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0780 60.8680 90.0150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1262 T22: -0.0925
REMARK 3 T33: 0.0296 T12: -0.0166
REMARK 3 T13: 0.0956 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 0.8587 L22: 1.0128
REMARK 3 L33: 3.8893 L12: -0.5511
REMARK 3 L13: -0.4514 L23: 0.2621
REMARK 3 S TENSOR
REMARK 3 S11: 0.1970 S12: -0.0737 S13: 0.2429
REMARK 3 S21: -0.0326 S22: 0.0176 S23: 0.0299
REMARK 3 S31: -0.5851 S32: 0.1558 S33: -0.2146
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 80 B 95
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5710 66.3090 65.1470
REMARK 3 T TENSOR
REMARK 3 T11: 0.5719 T22: 0.1221
REMARK 3 T33: 0.2625 T12: 0.2324
REMARK 3 T13: 0.0274 T23: 0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 9.0968 L22: 1.6628
REMARK 3 L33: 7.5294 L12: 0.7081
REMARK 3 L13: -4.7837 L23: -3.2115
REMARK 3 S TENSOR
REMARK 3 S11: 0.3103 S12: 0.2600 S13: 0.8208
REMARK 3 S21: -0.3666 S22: -0.2139 S23: 0.2329
REMARK 3 S31: -1.0306 S32: -0.4958 S33: -0.0964
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 96 B 104
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2650 75.9300 68.3070
REMARK 3 T TENSOR
REMARK 3 T11: 0.4630 T22: 0.2181
REMARK 3 T33: 0.4819 T12: -0.0584
REMARK 3 T13: 0.0874 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 17.8992 L22: 56.8741
REMARK 3 L33: 38.0071 L12: -8.6227
REMARK 3 L13: -2.5698 L23: 2.0286
REMARK 3 S TENSOR
REMARK 3 S11: -0.7314 S12: -1.0003 S13: 1.2881
REMARK 3 S21: 0.3047 S22: 0.6537 S23: -1.1368
REMARK 3 S31: -1.0706 S32: 2.2636 S33: 0.0777
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 105 B 131
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3470 67.7370 73.0940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5379 T22: 0.1135
REMARK 3 T33: 0.2211 T12: 0.1952
REMARK 3 T13: 0.0604 T23: 0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 4.7103 L22: 0.9017
REMARK 3 L33: 2.5139 L12: 0.3268
REMARK 3 L13: -2.7693 L23: 0.6405
REMARK 3 S TENSOR
REMARK 3 S11: 0.2859 S12: 0.0558 S13: 0.4073
REMARK 3 S21: -0.2136 S22: -0.0313 S23: 0.1012
REMARK 3 S31: -1.0313 S32: -0.3775 S33: -0.2546
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 132 B 210
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9140 59.7130 83.0260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1470 T22: -0.0718
REMARK 3 T33: 0.0274 T12: 0.0814
REMARK 3 T13: 0.0655 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.3049 L22: 1.6636
REMARK 3 L33: 3.5670 L12: -0.4542
REMARK 3 L13: -0.3577 L23: 1.0409
REMARK 3 S TENSOR
REMARK 3 S11: 0.1692 S12: -0.0347 S13: 0.1461
REMARK 3 S21: -0.1109 S22: -0.0595 S23: 0.1265
REMARK 3 S31: -0.5491 S32: -0.2712 S33: -0.1097
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 211 B 245
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6240 63.5190 87.9440
REMARK 3 T TENSOR
REMARK 3 T11: 0.1727 T22: -0.0393
REMARK 3 T33: 0.0366 T12: -0.0917
REMARK 3 T13: 0.1416 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 1.6288 L22: 10.9734
REMARK 3 L33: 4.2053 L12: -0.4684
REMARK 3 L13: -0.7225 L23: 3.0141
REMARK 3 S TENSOR
REMARK 3 S11: 0.2722 S12: -0.1530 S13: 0.3555
REMARK 3 S21: -0.1506 S22: 0.0082 S23: -0.2162
REMARK 3 S31: -0.7789 S32: 0.3234 S33: -0.2804
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 246 B 264
REMARK 3 ORIGIN FOR THE GROUP (A): 25.0990 61.0540 87.5250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0566 T22: 0.0976
REMARK 3 T33: 0.0261 T12: -0.1650
REMARK 3 T13: 0.1654 T23: -0.1718
REMARK 3 L TENSOR
REMARK 3 L11: 3.1351 L22: 18.8104
REMARK 3 L33: 3.1596 L12: -5.4643
REMARK 3 L13: 0.5395 L23: -0.9509
REMARK 3 S TENSOR
REMARK 3 S11: 0.1074 S12: -0.0699 S13: 0.4583
REMARK 3 S21: -0.6610 S22: 0.3718 S23: -1.2054
REMARK 3 S31: -0.6712 S32: 0.9318 S33: -0.4792
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2WGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1290039567.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979742
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59000
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 47.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 1.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1K4F
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AS BUFFER, CITRATE 0.1 M PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 24.37500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.30000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.30000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.37500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 117 TO THR
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 117 TO THR
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 265
REMARK 465 GLY A 266
REMARK 465 GLY B 266
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2128 O HOH A 2130 1.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 125 CZ ARG B 125 NH2 0.217
REMARK 500
REMARK 500 REMARK: NULL
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 ARG B 125 NE - CZ - NH1 ANGL. DEV. = -6.1 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 ALA A 66 -137.97 48.08
REMARK 500 PHE A 208 113.80 -160.87
REMARK 500 GLU A 229 -119.93 43.55
REMARK 500 ALA B 66 -137.41 42.60
REMARK 500 LYS B 152 -1.48 -161.19
REMARK 500 SER B 215 -8.34 82.50
REMARK 500 GLU B 229 -127.66 49.48
REMARK 500 ILE B 264 14.56 93.16
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 GOL A 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 1272
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K55 RELATED DB: PDB
REMARK 900 OXA 10 CLASS D BETA-LACTAMASE AT PH 7. 5
REMARK 900 RELATED ID: 1K56 RELATED DB: PDB
REMARK 900 OXA 10 CLASS D BETA-LACTAMASE AT PH 6. 5
REMARK 900 RELATED ID: 1E3U RELATED DB: PDB
REMARK 900 MAD STRUCTURE OF OXA10 CLASS D BETA- LACTAMASE
REMARK 900 RELATED ID: 1FOF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CLASS D BETA- LACTAMASE OXA-10
REMARK 900 RELATED ID: 1E4D RELATED DB: PDB
REMARK 900 STRUCTURE OF OXA10 BETA-LACTAMASE AT PH 8 .3
REMARK 900 RELATED ID: 2WGI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ACYL-ENZYME OXA- 10 W154A-BENZYLPENICILLIN
REMARK 900 AT PH 6
REMARK 900 RELATED ID: 1EWZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE OXA-10 BETA- LACTAMASE FROM PSEUDOMONAS
REMARK 900 AERUGINOSA
REMARK 900 RELATED ID: 1K4F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CLASS D BETA- LACTAMASE OXA-10 AT1.6 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 2WGW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE OXA-10 V117T MUTANT AT PH 8.0
REMARK 900 RELATED ID: 1K6S RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10 IN COMPLEXWITH A
REMARK 900 PHENYLBORONIC ACID
REMARK 900 RELATED ID: 1K4E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CLASS D BETA- LACTAMASES OXA-10DETERMINED
REMARK 900 BY MAD PHASING WITH SELENOMETHIONINE
REMARK 900 RELATED ID: 1K57 RELATED DB: PDB
REMARK 900 OXA 10 CLASS D BETA-LACTAMASE AT PH 6. 0
REMARK 900 RELATED ID: 1K54 RELATED DB: PDB
REMARK 900 OXA-10 CLASS D BETA-LACTAMASE PARTIALLY ACYLATED WITHREACTED 6BETA-
REMARK 900 (1-HYDROXY-1- METHYLETHYL) PENICILLANIC ACID
REMARK 900 RELATED ID: 1K6R RELATED DB: PDB
REMARK 900 STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10 IN COMPLEXWITH
REMARK 900 MOXALACTAM
REMARK 900 RELATED ID: 2WKI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE OXA-10 K70C MUTANT AT PH 7.0
REMARK 900 RELATED ID: 2WKH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ACYL-ENZYME OXA- 10 K70C-AMPICILLIN AT PH 7
DBREF 2WGV A 19 19 PDB 2WGV 2WGV 19 19
DBREF 2WGV A 20 266 UNP P14489 BLO10_PSEAE 20 266
DBREF 2WGV B 19 19 PDB 2WGV 2WGV 19 19
DBREF 2WGV B 20 266 UNP P14489 BLO10_PSEAE 20 266
SEQADV 2WGV THR A 117 UNP P14489 VAL 117 ENGINEERED MUTATION
SEQADV 2WGV THR B 117 UNP P14489 VAL 117 ENGINEERED MUTATION
SEQRES 1 A 248 MET GLY SER ILE THR GLU ASN THR SER TRP ASN LYS GLU
SEQRES 2 A 248 PHE SER ALA GLU ALA VAL ASN GLY VAL PHE VAL LEU CYS
SEQRES 3 A 248 LYS SER SER SER LYS SER CYS ALA THR ASN ASP LEU ALA
SEQRES 4 A 248 ARG ALA SER LYS GLU TYR LEU PRO ALA SER THR PHE LYS
SEQRES 5 A 248 ILE PRO ASN ALA ILE ILE GLY LEU GLU THR GLY VAL ILE
SEQRES 6 A 248 LYS ASN GLU HIS GLN VAL PHE LYS TRP ASP GLY LYS PRO
SEQRES 7 A 248 ARG ALA MET LYS GLN TRP GLU ARG ASP LEU THR LEU ARG
SEQRES 8 A 248 GLY ALA ILE GLN VAL SER ALA THR PRO VAL PHE GLN GLN
SEQRES 9 A 248 ILE ALA ARG GLU VAL GLY GLU VAL ARG MET GLN LYS TYR
SEQRES 10 A 248 LEU LYS LYS PHE SER TYR GLY ASN GLN ASN ILE SER GLY
SEQRES 11 A 248 GLY ILE ASP LYS PHE TRP LEU GLU GLY GLN LEU ARG ILE
SEQRES 12 A 248 SER ALA VAL ASN GLN VAL GLU PHE LEU GLU SER LEU TYR
SEQRES 13 A 248 LEU ASN LYS LEU SER ALA SER LYS GLU ASN GLN LEU ILE
SEQRES 14 A 248 VAL LYS GLU ALA LEU VAL THR GLU ALA ALA PRO GLU TYR
SEQRES 15 A 248 LEU VAL HIS SER LYS THR GLY PHE SER GLY VAL GLY THR
SEQRES 16 A 248 GLU SER ASN PRO GLY VAL ALA TRP TRP VAL GLY TRP VAL
SEQRES 17 A 248 GLU LYS GLU THR GLU VAL TYR PHE PHE ALA PHE ASN MET
SEQRES 18 A 248 ASP ILE ASP ASN GLU SER LYS LEU PRO LEU ARG LYS SER
SEQRES 19 A 248 ILE PRO THR LYS ILE MET GLU SER GLU GLY ILE ILE GLY
SEQRES 20 A 248 GLY
SEQRES 1 B 248 MET GLY SER ILE THR GLU ASN THR SER TRP ASN LYS GLU
SEQRES 2 B 248 PHE SER ALA GLU ALA VAL ASN GLY VAL PHE VAL LEU CYS
SEQRES 3 B 248 LYS SER SER SER LYS SER CYS ALA THR ASN ASP LEU ALA
SEQRES 4 B 248 ARG ALA SER LYS GLU TYR LEU PRO ALA SER THR PHE LYS
SEQRES 5 B 248 ILE PRO ASN ALA ILE ILE GLY LEU GLU THR GLY VAL ILE
SEQRES 6 B 248 LYS ASN GLU HIS GLN VAL PHE LYS TRP ASP GLY LYS PRO
SEQRES 7 B 248 ARG ALA MET LYS GLN TRP GLU ARG ASP LEU THR LEU ARG
SEQRES 8 B 248 GLY ALA ILE GLN VAL SER ALA THR PRO VAL PHE GLN GLN
SEQRES 9 B 248 ILE ALA ARG GLU VAL GLY GLU VAL ARG MET GLN LYS TYR
SEQRES 10 B 248 LEU LYS LYS PHE SER TYR GLY ASN GLN ASN ILE SER GLY
SEQRES 11 B 248 GLY ILE ASP LYS PHE TRP LEU GLU GLY GLN LEU ARG ILE
SEQRES 12 B 248 SER ALA VAL ASN GLN VAL GLU PHE LEU GLU SER LEU TYR
SEQRES 13 B 248 LEU ASN LYS LEU SER ALA SER LYS GLU ASN GLN LEU ILE
SEQRES 14 B 248 VAL LYS GLU ALA LEU VAL THR GLU ALA ALA PRO GLU TYR
SEQRES 15 B 248 LEU VAL HIS SER LYS THR GLY PHE SER GLY VAL GLY THR
SEQRES 16 B 248 GLU SER ASN PRO GLY VAL ALA TRP TRP VAL GLY TRP VAL
SEQRES 17 B 248 GLU LYS GLU THR GLU VAL TYR PHE PHE ALA PHE ASN MET
SEQRES 18 B 248 ASP ILE ASP ASN GLU SER LYS LEU PRO LEU ARG LYS SER
SEQRES 19 B 248 ILE PRO THR LYS ILE MET GLU SER GLU GLY ILE ILE GLY
SEQRES 20 B 248 GLY
HET GOL A1265 6
HET GOL A1266 6
HET GOL A1267 6
HET CL A1268 1
HET CL A1269 1
HET CL A1270 1
HET CL A1271 1
HET CIT A1272 13
HET CL B1266 1
HET SO4 B1267 5
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM CIT CITRIC ACID
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 CL 5(CL 1-)
FORMUL 10 CIT C6 H8 O7
FORMUL 12 SO4 O4 S 2-
FORMUL 13 HOH *353(H2 O)
HELIX 1 1 TRP A 28 ALA A 34 1 7
HELIX 2 2 ASP A 55 SER A 60 1 6
HELIX 3 3 PRO A 65 THR A 68 5 4
HELIX 4 4 PHE A 69 THR A 80 1 12
HELIX 5 5 MET A 99 GLU A 103 5 5
HELIX 6 6 THR A 107 VAL A 114 1 8
HELIX 7 7 ALA A 116 GLY A 128 1 13
HELIX 8 8 GLY A 128 PHE A 139 1 12
HELIX 9 9 ALA A 163 LEU A 175 1 13
HELIX 10 10 SER A 181 LEU A 192 1 12
HELIX 11 11 ASN A 243 LEU A 247 5 5
HELIX 12 12 PRO A 248 GLU A 261 1 14
HELIX 13 13 THR B 26 TRP B 28 5 3
HELIX 14 14 ASN B 29 ALA B 34 1 6
HELIX 15 15 ASP B 55 SER B 60 1 6
HELIX 16 16 PRO B 65 THR B 68 5 4
HELIX 17 17 PHE B 69 THR B 80 1 12
HELIX 18 18 MET B 99 GLU B 103 5 5
HELIX 19 19 THR B 107 VAL B 114 1 8
HELIX 20 20 ALA B 116 GLY B 128 1 13
HELIX 21 21 GLY B 128 PHE B 139 1 12
HELIX 22 22 ALA B 163 LEU B 175 1 13
HELIX 23 23 SER B 181 LEU B 192 1 12
HELIX 24 24 ASN B 243 LEU B 247 5 5
HELIX 25 25 PRO B 248 GLU B 261 1 14
SHEET 1 AA 7 SER A 21 GLU A 24 0
SHEET 2 AA 7 SER A 50 THR A 53 1 O CYS A 51 N THR A 23
SHEET 3 AA 7 GLY A 39 LYS A 45 -1 O LEU A 43 N ALA A 52
SHEET 4 AA 7 GLU A 231 ILE A 241 -1 O PHE A 234 N CYS A 44
SHEET 5 AA 7 GLY A 218 LYS A 228 -1 O GLY A 218 N ILE A 241
SHEET 6 AA 7 TYR A 200 PHE A 208 -1 O LEU A 201 N GLU A 227
SHEET 7 AA 7 VAL A 193 ALA A 197 -1 N THR A 194 O VAL A 202
SHEET 1 AB 2 GLU A 62 TYR A 63 0
SHEET 2 AB 2 ILE A 161 SER A 162 -1 O ILE A 161 N TYR A 63
SHEET 1 BA 7 SER B 21 GLU B 24 0
SHEET 2 BA 7 SER B 50 THR B 53 1 O CYS B 51 N THR B 23
SHEET 3 BA 7 GLY B 39 LYS B 45 -1 O LEU B 43 N ALA B 52
SHEET 4 BA 7 GLU B 231 ILE B 241 -1 O PHE B 234 N CYS B 44
SHEET 5 BA 7 GLY B 218 LYS B 228 -1 O GLY B 218 N ILE B 241
SHEET 6 BA 7 TYR B 200 PHE B 208 -1 O LEU B 201 N GLU B 227
SHEET 7 BA 7 VAL B 193 ALA B 197 -1 N THR B 194 O VAL B 202
SHEET 1 BB 2 GLU B 62 TYR B 63 0
SHEET 2 BB 2 ILE B 161 SER B 162 -1 O ILE B 161 N TYR B 63
SSBOND 1 CYS A 44 CYS A 51 1555 1555 2.06
SSBOND 2 CYS B 44 CYS B 51 1555 1555 2.07
SITE 1 AC1 11 THR A 107 ARG A 109 GLY A 110 HOH A2225
SITE 2 AC1 11 ALA B 197 PRO B 198 GLU B 199 TYR B 200
SITE 3 AC1 11 GLU B 227 GLU B 229 HOH B2106
SITE 1 AC2 9 ALA A 197 PRO A 198 GLU A 199 TYR A 200
SITE 2 AC2 9 GLU A 227 GLU A 229 HOH A2190 THR B 107
SITE 3 AC2 9 ARG B 109
SITE 1 AC3 4 LYS A 138 SER A 140 SER A 172 HOH A2226
SITE 1 AC4 3 LYS A 70 TRP A 154 HOH A2053
SITE 1 AC5 3 LYS B 70 TRP B 154 HOH B2030
SITE 1 AC6 2 ALA A 98 HOH A2122
SITE 1 AC7 2 ARG A 250 HOH A2215
SITE 1 AC8 3 ARG A 131 LYS A 152 HOH A2120
SITE 1 AC9 8 SER B 67 SER B 115 LYS B 205 THR B 206
SITE 2 AC9 8 GLY B 207 PHE B 208 ARG B 250 HOH B2124
SITE 1 BC1 11 ALA A 66 SER A 67 SER A 115 LYS A 205
SITE 2 BC1 11 THR A 206 GLY A 207 PHE A 208 ARG A 250
SITE 3 BC1 11 HOH A2099 HOH A2227 HOH A2228
CRYST1 48.750 101.700 126.600 90.00 90.00 90.00 P 21 21 21 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 0.020513 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009833 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007899 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
