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HEADER HYDROLASE 18-DEC-08 3FLA
TITLE RIFR - TYPE II THIOESTERASE FROM RIFAMYCIN NRPS/PKS
TITLE 2 BIOSYNTHETIC PATHWAY - FORM 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIFR;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.2.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AMYCOLATOPSIS MEDITERRANEI;
SOURCE 3 ORGANISM_COMMON: NOCARDIA MEDITERRANEI;
SOURCE 4 ORGANISM_TAXID: 33910;
SOURCE 5 GENE: RIFR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET25B,PMS25
KEYWDS ALPHA-BETA HYDROLASE THIOESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.SMITH,D.L.AKEY
REVDAT 1 06-JAN-09 3FLA 0
JRNL AUTH H.B.CLAXTON,D.L.AKEY,M.K.SILVER,S.J.ADMIRAAL,
JRNL AUTH 2 J.L.SMITH
JRNL TITL STRUCTURE AND FUNCTIONAL ANALYSIS OF RIFR, THE
JRNL TITL 2 TYPE II THIOESTERASE FROM THE RIFAMYCIN
JRNL TITL 3 BIOSYNTHETIC PATHWAY.
JRNL REF J.BIOL.CHEM. 2008
JRNL REFN ESSN 1083-351X
JRNL PMID 19103602
JRNL DOI 10.1074/JBC.M808604200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 39950
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2126
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2619
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 134
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4372
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.50000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.255
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3997 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5442 ; 1.199 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 510 ; 5.117 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;24.964 ;21.027
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 624 ;13.794 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;15.235 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 582 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3165 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2066 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2768 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 473 ; 0.131 ; 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): 110 ; 0.174 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.128 ; 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 ; 3.385 ; 8.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4050 ; 3.917 ;12.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1553 ; 4.784 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1392 ; 6.819 ;12.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 2 B 247 4
REMARK 3 1 A 2 A 247 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1916 ; 0.25 ; 0.50
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1916 ; 0.49 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 2 A 14
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2350 52.7875 46.6399
REMARK 3 T TENSOR
REMARK 3 T11: 0.0528 T22: 0.0021
REMARK 3 T33: -0.0833 T12: 0.0912
REMARK 3 T13: -0.0098 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 3.0408 L22: 6.1734
REMARK 3 L33: 4.6386 L12: -2.8248
REMARK 3 L13: -1.7959 L23: 1.0604
REMARK 3 S TENSOR
REMARK 3 S11: -0.1506 S12: -0.3566 S13: -0.0344
REMARK 3 S21: 0.9752 S22: 0.3979 S23: 0.0292
REMARK 3 S31: 0.1151 S32: 0.3626 S33: -0.2473
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 15 A 51
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6579 62.4751 39.0561
REMARK 3 T TENSOR
REMARK 3 T11: 0.0048 T22: -0.0540
REMARK 3 T33: -0.0390 T12: 0.0160
REMARK 3 T13: 0.0551 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 1.5257 L22: 3.7062
REMARK 3 L33: 3.0111 L12: -0.8394
REMARK 3 L13: -0.2794 L23: 2.8583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: -0.0377 S13: 0.2065
REMARK 3 S21: -0.0884 S22: 0.1133 S23: -0.2424
REMARK 3 S31: -0.0647 S32: 0.2099 S33: -0.1610
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 52 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6802 51.1031 36.5084
REMARK 3 T TENSOR
REMARK 3 T11: 0.0067 T22: -0.0347
REMARK 3 T33: -0.0125 T12: 0.0166
REMARK 3 T13: 0.0365 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.3158 L22: 0.3424
REMARK 3 L33: 0.6384 L12: 0.2381
REMARK 3 L13: 0.2627 L23: 0.1626
REMARK 3 S TENSOR
REMARK 3 S11: -0.0311 S12: -0.0133 S13: -0.0590
REMARK 3 S21: 0.1439 S22: -0.0194 S23: 0.0878
REMARK 3 S31: -0.0090 S32: -0.0278 S33: 0.0505
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 143 A 174
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1264 45.9147 25.2374
REMARK 3 T TENSOR
REMARK 3 T11: -0.0503 T22: 0.0087
REMARK 3 T33: -0.0120 T12: 0.0170
REMARK 3 T13: -0.0036 T23: -0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 2.2166 L22: 1.7218
REMARK 3 L33: 1.1542 L12: 0.8172
REMARK 3 L13: 0.8121 L23: -0.7178
REMARK 3 S TENSOR
REMARK 3 S11: 0.0524 S12: -0.1362 S13: 0.0877
REMARK 3 S21: 0.0959 S22: -0.0520 S23: -0.0549
REMARK 3 S31: 0.0310 S32: 0.0630 S33: -0.0004
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 175 A 189
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1134 48.4575 33.9610
REMARK 3 T TENSOR
REMARK 3 T11: -0.1249 T22: -0.0308
REMARK 3 T33: -0.0046 T12: 0.0069
REMARK 3 T13: 0.0209 T23: 0.0679
REMARK 3 L TENSOR
REMARK 3 L11: 4.7673 L22: 8.8596
REMARK 3 L33: 2.8499 L12: -4.2532
REMARK 3 L13: -1.3611 L23: 1.8159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0920 S12: -0.1449 S13: -0.2110
REMARK 3 S21: 0.1720 S22: 0.2243 S23: 0.5998
REMARK 3 S31: -0.0380 S32: -0.1189 S33: -0.1324
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 190 A 247
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7501 63.4860 27.4313
REMARK 3 T TENSOR
REMARK 3 T11: 0.0267 T22: -0.0688
REMARK 3 T33: -0.0265 T12: 0.0022
REMARK 3 T13: 0.0082 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5206 L22: 1.4209
REMARK 3 L33: 1.8210 L12: -0.1481
REMARK 3 L13: 0.3470 L23: -0.2540
REMARK 3 S TENSOR
REMARK 3 S11: -0.0907 S12: 0.0318 S13: 0.1010
REMARK 3 S21: 0.0233 S22: 0.0232 S23: 0.0869
REMARK 3 S31: -0.4195 S32: -0.0004 S33: 0.0675
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 : B 2 B 14
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2949 35.7744 48.1030
REMARK 3 T TENSOR
REMARK 3 T11: 0.1266 T22: 0.0589
REMARK 3 T33: -0.0608 T12: -0.1038
REMARK 3 T13: 0.0686 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 6.7726 L22: 13.2904
REMARK 3 L33: 2.3442 L12: 3.6031
REMARK 3 L13: 3.4554 L23: 1.9661
REMARK 3 S TENSOR
REMARK 3 S11: -0.4278 S12: 0.7700 S13: 0.1856
REMARK 3 S21: -1.6515 S22: 0.6240 S23: -0.4376
REMARK 3 S31: -0.2787 S32: 0.5057 S33: -0.1963
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 : B 15 B 51
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5897 25.9396 55.8113
REMARK 3 T TENSOR
REMARK 3 T11: -0.0099 T22: -0.0478
REMARK 3 T33: -0.0408 T12: -0.0070
REMARK 3 T13: -0.0493 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.5154 L22: 5.0034
REMARK 3 L33: 3.2785 L12: 1.1194
REMARK 3 L13: 0.5780 L23: 3.4066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0672 S12: 0.0048 S13: -0.2295
REMARK 3 S21: 0.1750 S22: 0.1409 S23: -0.3197
REMARK 3 S31: 0.1149 S32: 0.2170 S33: -0.2081
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 52 B 142
REMARK 3 ORIGIN FOR THE GROUP (A): -8.4506 37.2787 58.2169
REMARK 3 T TENSOR
REMARK 3 T11: -0.0069 T22: -0.0359
REMARK 3 T33: -0.0117 T12: -0.0076
REMARK 3 T13: -0.0338 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 0.3966 L22: 0.2366
REMARK 3 L33: 0.8186 L12: -0.3021
REMARK 3 L13: -0.2968 L23: 0.1638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0229 S13: 0.0644
REMARK 3 S21: -0.0992 S22: -0.0410 S23: 0.0870
REMARK 3 S31: 0.0212 S32: -0.0273 S33: 0.0396
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 143 B 174
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8863 42.5448 69.4557
REMARK 3 T TENSOR
REMARK 3 T11: -0.0563 T22: -0.0067
REMARK 3 T33: -0.0177 T12: -0.0129
REMARK 3 T13: 0.0037 T23: -0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 2.0203 L22: 1.4894
REMARK 3 L33: 1.3202 L12: -1.1826
REMARK 3 L13: -0.6962 L23: -0.5204
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: 0.1350 S13: -0.0533
REMARK 3 S21: -0.0713 S22: -0.0251 S23: -0.0452
REMARK 3 S31: 0.0377 S32: 0.0832 S33: 0.0088
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 175 B 189
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0554 39.8993 60.6807
REMARK 3 T TENSOR
REMARK 3 T11: -0.1513 T22: -0.0163
REMARK 3 T33: 0.0189 T12: 0.0022
REMARK 3 T13: -0.0239 T23: 0.0696
REMARK 3 L TENSOR
REMARK 3 L11: 3.8697 L22: 10.2021
REMARK 3 L33: 4.4465 L12: 3.9716
REMARK 3 L13: 1.9560 L23: 1.7878
REMARK 3 S TENSOR
REMARK 3 S11: -0.1428 S12: 0.1575 S13: 0.2270
REMARK 3 S21: -0.2801 S22: 0.3079 S23: 0.8016
REMARK 3 S31: -0.0020 S32: -0.1303 S33: -0.1652
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 190 B 247
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5199 24.8977 67.3084
REMARK 3 T TENSOR
REMARK 3 T11: 0.0214 T22: -0.0676
REMARK 3 T33: -0.0268 T12: -0.0074
REMARK 3 T13: -0.0018 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.6216 L22: 1.6682
REMARK 3 L33: 1.6669 L12: -0.0069
REMARK 3 L13: -0.3320 L23: -0.3381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0680 S12: -0.0159 S13: -0.1163
REMARK 3 S21: 0.0163 S22: 0.0254 S23: 0.1032
REMARK 3 S31: 0.3773 S32: -0.0146 S33: 0.0425
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3FLA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050729.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97942, 0.97959, 0.95446
REMARK 200 MONOCHROMATOR : APS BEAMLINE 23-ID-D
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39950
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11500
REMARK 200 FOR THE DATA SET : 10.5000
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) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.54000
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0, 12% PEG 8000,
REMARK 280 50 MM CACL2, 2 MM DTT , VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 47.32400
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
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 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 MSE A 1
REMARK 465 GLY A 248
REMARK 465 PRO A 249
REMARK 465 ALA A 250
REMARK 465 LEU A 251
REMARK 465 THR A 252
REMARK 465 GLY A 253
REMARK 465 SER A 254
REMARK 465 THR A 255
REMARK 465 GLY A 256
REMARK 465 GLY A 257
REMARK 465 ASN A 258
REMARK 465 SER A 259
REMARK 465 LEU A 260
REMARK 465 GLU A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 MSE B 1
REMARK 465 GLY B 248
REMARK 465 PRO B 249
REMARK 465 ALA B 250
REMARK 465 LEU B 251
REMARK 465 THR B 252
REMARK 465 GLY B 253
REMARK 465 SER B 254
REMARK 465 THR B 255
REMARK 465 GLY B 256
REMARK 465 GLY B 257
REMARK 465 ASN B 258
REMARK 465 SER B 259
REMARK 465 LEU B 260
REMARK 465 GLU B 261
REMARK 465 HIS B 262
REMARK 465 HIS B 263
REMARK 465 HIS B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG A 15 CG CD NE CZ NH1 NH2
REMARK 480 ARG B 15 CG CD NE CZ NH1 NH2
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 394 O HOH A 466 2.14
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 GLN A 58 -116.06 49.02
REMARK 500 GLN B 58 -117.06 49.64
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 CL A 268
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 268
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FLB RELATED DB: PDB
DBREF 3FLA A 1 259 UNP Q7BUF9 Q7BUF9_AMYMD 1 259
DBREF 3FLA B 1 259 UNP Q7BUF9 Q7BUF9_AMYMD 1 259
SEQADV 3FLA LEU A 260 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA GLU A 261 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS A 262 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS A 263 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS A 264 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS A 265 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS A 266 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS A 267 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA LEU B 260 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA GLU B 261 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS B 262 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS B 263 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS B 264 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS B 265 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS B 266 UNP Q7BUF9 EXPRESSION TAG
SEQADV 3FLA HIS B 267 UNP Q7BUF9 EXPRESSION TAG
SEQRES 1 A 267 MSE HIS ARG PRO GLU ALA GLU LYS TRP LEU ARG ARG PHE
SEQRES 2 A 267 GLU ARG ALA PRO ASP ALA ARG ALA ARG LEU VAL CYS LEU
SEQRES 3 A 267 PRO HIS ALA GLY GLY SER ALA SER PHE PHE PHE PRO LEU
SEQRES 4 A 267 ALA LYS ALA LEU ALA PRO ALA VAL GLU VAL LEU ALA VAL
SEQRES 5 A 267 GLN TYR PRO GLY ARG GLN ASP ARG ARG HIS GLU PRO PRO
SEQRES 6 A 267 VAL ASP SER ILE GLY GLY LEU THR ASN ARG LEU LEU GLU
SEQRES 7 A 267 VAL LEU ARG PRO PHE GLY ASP ARG PRO LEU ALA LEU PHE
SEQRES 8 A 267 GLY HIS SER MSE GLY ALA ILE ILE GLY TYR GLU LEU ALA
SEQRES 9 A 267 LEU ARG MSE PRO GLU ALA GLY LEU PRO ALA PRO VAL HIS
SEQRES 10 A 267 LEU PHE ALA SER GLY ARG ARG ALA PRO SER ARG TYR ARG
SEQRES 11 A 267 ASP ASP ASP VAL ARG GLY ALA SER ASP GLU ARG LEU VAL
SEQRES 12 A 267 ALA GLU LEU ARG LYS LEU GLY GLY SER ASP ALA ALA MSE
SEQRES 13 A 267 LEU ALA ASP PRO GLU LEU LEU ALA MSE VAL LEU PRO ALA
SEQRES 14 A 267 ILE ARG SER ASP TYR ARG ALA VAL GLU THR TYR ARG HIS
SEQRES 15 A 267 GLU PRO GLY ARG ARG VAL ASP CYS PRO VAL THR VAL PHE
SEQRES 16 A 267 THR GLY ASP HIS ASP PRO ARG VAL SER VAL GLY GLU ALA
SEQRES 17 A 267 ARG ALA TRP GLU GLU HIS THR THR GLY PRO ALA ASP LEU
SEQRES 18 A 267 ARG VAL LEU PRO GLY GLY HIS PHE PHE LEU VAL ASP GLN
SEQRES 19 A 267 ALA ALA PRO MSE ILE ALA THR MSE THR GLU LYS LEU ALA
SEQRES 20 A 267 GLY PRO ALA LEU THR GLY SER THR GLY GLY ASN SER LEU
SEQRES 21 A 267 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 267 MSE HIS ARG PRO GLU ALA GLU LYS TRP LEU ARG ARG PHE
SEQRES 2 B 267 GLU ARG ALA PRO ASP ALA ARG ALA ARG LEU VAL CYS LEU
SEQRES 3 B 267 PRO HIS ALA GLY GLY SER ALA SER PHE PHE PHE PRO LEU
SEQRES 4 B 267 ALA LYS ALA LEU ALA PRO ALA VAL GLU VAL LEU ALA VAL
SEQRES 5 B 267 GLN TYR PRO GLY ARG GLN ASP ARG ARG HIS GLU PRO PRO
SEQRES 6 B 267 VAL ASP SER ILE GLY GLY LEU THR ASN ARG LEU LEU GLU
SEQRES 7 B 267 VAL LEU ARG PRO PHE GLY ASP ARG PRO LEU ALA LEU PHE
SEQRES 8 B 267 GLY HIS SER MSE GLY ALA ILE ILE GLY TYR GLU LEU ALA
SEQRES 9 B 267 LEU ARG MSE PRO GLU ALA GLY LEU PRO ALA PRO VAL HIS
SEQRES 10 B 267 LEU PHE ALA SER GLY ARG ARG ALA PRO SER ARG TYR ARG
SEQRES 11 B 267 ASP ASP ASP VAL ARG GLY ALA SER ASP GLU ARG LEU VAL
SEQRES 12 B 267 ALA GLU LEU ARG LYS LEU GLY GLY SER ASP ALA ALA MSE
SEQRES 13 B 267 LEU ALA ASP PRO GLU LEU LEU ALA MSE VAL LEU PRO ALA
SEQRES 14 B 267 ILE ARG SER ASP TYR ARG ALA VAL GLU THR TYR ARG HIS
SEQRES 15 B 267 GLU PRO GLY ARG ARG VAL ASP CYS PRO VAL THR VAL PHE
SEQRES 16 B 267 THR GLY ASP HIS ASP PRO ARG VAL SER VAL GLY GLU ALA
SEQRES 17 B 267 ARG ALA TRP GLU GLU HIS THR THR GLY PRO ALA ASP LEU
SEQRES 18 B 267 ARG VAL LEU PRO GLY GLY HIS PHE PHE LEU VAL ASP GLN
SEQRES 19 B 267 ALA ALA PRO MSE ILE ALA THR MSE THR GLU LYS LEU ALA
SEQRES 20 B 267 GLY PRO ALA LEU THR GLY SER THR GLY GLY ASN SER LEU
SEQRES 21 B 267 GLU HIS HIS HIS HIS HIS HIS
MODRES 3FLA MSE A 95 MET SELENOMETHIONINE
MODRES 3FLA MSE A 107 MET SELENOMETHIONINE
MODRES 3FLA MSE A 156 MET SELENOMETHIONINE
MODRES 3FLA MSE A 165 MET SELENOMETHIONINE
MODRES 3FLA MSE A 238 MET SELENOMETHIONINE
MODRES 3FLA MSE A 242 MET SELENOMETHIONINE
MODRES 3FLA MSE B 95 MET SELENOMETHIONINE
MODRES 3FLA MSE B 107 MET SELENOMETHIONINE
MODRES 3FLA MSE B 156 MET SELENOMETHIONINE
MODRES 3FLA MSE B 165 MET SELENOMETHIONINE
MODRES 3FLA MSE B 238 MET SELENOMETHIONINE
MODRES 3FLA MSE B 242 MET SELENOMETHIONINE
HET MSE A 95 8
HET MSE A 107 8
HET MSE A 156 8
HET MSE A 165 8
HET MSE A 238 8
HET MSE A 242 8
HET MSE B 95 8
HET MSE B 107 8
HET MSE B 156 16
HET MSE B 165 8
HET MSE B 238 8
HET MSE B 242 8
HET CL A 268 1
HET CL B 268 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *481(H2 O)
HELIX 1 1 HIS A 2 LYS A 8 1 7
HELIX 2 2 SER A 32 PHE A 35 5 4
HELIX 3 3 PHE A 36 ALA A 44 1 9
HELIX 4 4 ARG A 57 ARG A 61 5 5
HELIX 5 5 SER A 68 LEU A 80 1 13
HELIX 6 6 ARG A 81 GLY A 84 5 4
HELIX 7 7 SER A 94 MSE A 107 1 14
HELIX 8 8 SER A 138 LEU A 149 1 12
HELIX 9 9 GLY A 150 ASP A 159 1 10
HELIX 10 10 ASP A 159 TYR A 180 1 22
HELIX 11 11 SER A 204 ALA A 210 1 7
HELIX 12 12 TRP A 211 THR A 215 5 5
HELIX 13 13 PHE A 229 GLN A 234 1 6
HELIX 14 14 GLN A 234 LEU A 246 1 13
HELIX 15 15 HIS B 2 GLU B 7 1 6
HELIX 16 16 SER B 32 PHE B 35 5 4
HELIX 17 17 PHE B 36 ALA B 44 1 9
HELIX 18 18 ARG B 57 ARG B 61 5 5
HELIX 19 19 SER B 68 LEU B 80 1 13
HELIX 20 20 ARG B 81 GLY B 84 5 4
HELIX 21 21 SER B 94 GLY B 111 1 18
HELIX 22 22 SER B 138 GLY B 150 1 13
HELIX 23 23 GLY B 150 ASP B 159 1 10
HELIX 24 24 ASP B 159 TYR B 180 1 22
HELIX 25 25 SER B 204 ALA B 210 1 7
HELIX 26 26 TRP B 211 THR B 215 5 5
HELIX 27 27 GLN B 234 LEU B 246 1 13
SHEET 1 A 7 LEU A 10 ARG A 11 0
SHEET 2 A 7 VAL A 47 VAL A 52 -1 O ALA A 51 N ARG A 11
SHEET 3 A 7 ALA A 21 LEU A 26 1 N LEU A 23 O GLU A 48
SHEET 4 A 7 LEU A 88 HIS A 93 1 O PHE A 91 N VAL A 24
SHEET 5 A 7 HIS A 117 SER A 121 1 O SER A 121 N GLY A 92
SHEET 6 A 7 VAL A 192 GLY A 197 1 O THR A 193 N LEU A 118
SHEET 7 A 7 ALA A 219 LEU A 224 1 O ASP A 220 N VAL A 194
SHEET 1 B 7 LEU B 10 ARG B 11 0
SHEET 2 B 7 VAL B 47 VAL B 52 -1 O ALA B 51 N ARG B 11
SHEET 3 B 7 ALA B 21 LEU B 26 1 N CYS B 25 O LEU B 50
SHEET 4 B 7 LEU B 88 HIS B 93 1 O PHE B 91 N VAL B 24
SHEET 5 B 7 LEU B 118 SER B 121 1 O SER B 121 N GLY B 92
SHEET 6 B 7 VAL B 192 GLY B 197 1 O THR B 193 N LEU B 118
SHEET 7 B 7 ALA B 219 LEU B 224 1 O ASP B 220 N VAL B 194
LINK C SER B 94 N MSE B 95 1555 1555 1.33
LINK C MSE B 95 N GLY B 96 1555 1555 1.34
LINK C ARG B 106 N MSE B 107 1555 1555 1.33
LINK C MSE B 107 N PRO B 108 1555 1555 1.34
LINK C ALA B 155 N AMSE B 156 1555 1555 1.33
LINK C ALA B 155 N BMSE B 156 1555 1555 1.33
LINK C AMSE B 156 N LEU B 157 1555 1555 1.33
LINK C BMSE B 156 N LEU B 157 1555 1555 1.34
LINK C ALA B 164 N MSE B 165 1555 1555 1.33
LINK C MSE B 165 N VAL B 166 1555 1555 1.33
LINK C PRO B 237 N MSE B 238 1555 1555 1.33
LINK C MSE B 238 N ILE B 239 1555 1555 1.33
LINK C THR B 241 N MSE B 242 1555 1555 1.33
LINK C MSE B 242 N THR B 243 1555 1555 1.33
LINK C SER A 94 N MSE A 95 1555 1555 1.33
LINK C MSE A 95 N GLY A 96 1555 1555 1.33
LINK C ARG A 106 N MSE A 107 1555 1555 1.33
LINK C MSE A 107 N PRO A 108 1555 1555 1.34
LINK C ALA A 155 N MSE A 156 1555 1555 1.33
LINK C MSE A 156 N LEU A 157 1555 1555 1.33
LINK C ALA A 164 N MSE A 165 1555 1555 1.32
LINK C MSE A 165 N VAL A 166 1555 1555 1.33
LINK C PRO A 237 N MSE A 238 1555 1555 1.33
LINK C MSE A 238 N ILE A 239 1555 1555 1.33
LINK C THR A 241 N MSE A 242 1555 1555 1.34
LINK C MSE A 242 N THR A 243 1555 1555 1.33
CISPEP 1 ALA A 44 PRO A 45 0 1.45
CISPEP 2 ALA B 44 PRO B 45 0 3.16
SITE 1 AC1 4 ALA A 29 SER A 94 MSE A 95 HOH A 414
SITE 1 AC2 4 ALA B 29 SER B 94 MSE B 95 HOH B 450
CRYST1 39.507 94.648 63.174 90.00 90.55 90.00 P 1 21 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 0.025312 0.000000 0.000243 0.00000
SCALE2 0.000000 0.010565 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015830 0.00000
TER 1936 ALA A 247
TER 3891 ALA B 247
MASTER 554 0 14 27 14 0 2 6 4372 2 128 42
END |