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HEADER HYDROLASE 05-APR-10 3MGA
TITLE 2.4 ANGSTROM CRYSTAL STRUCTURE OF FERRIC ENTEROBACTIN
TITLE 2 ESTERASE (FES) FROM SALMONELLA TYPHIMURIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROCHELIN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: FERRIC ENTEROBACTIN ESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA
SOURCE 3 SEROVAR TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 90371;
SOURCE 5 STRAIN: LT2;
SOURCE 6 GENE: FES, STM0586;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES,
KEYWDS 2 CSGID, FERRIC ENTEROBACTIN ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,Z.WAWRZAK,T.SKARINA,O.ONOPRIYENKO,L.PAPAZISI,
AUTHOR 2 A.SAVCHENKO,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF
AUTHOR 3 INFECTIOUS DISEASES (CSGID)
REVDAT 1 21-APR-10 3MGA 0
JRNL AUTH G.MINASOV,Z.WAWRZAK,T.SKARINA,O.ONOPRIYENKO,
JRNL AUTH 2 L.PAPAZISI,A.SAVCHENKO,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
JRNL AUTH 4 DISEASES (CSGID)
JRNL TITL 2.4 ANGSTROM CRYSTAL STRUCTURE OF FERRIC
JRNL TITL 2 ENTEROBACTIN ESTERASE (FES) FROM SALMONELLA
JRNL TITL 3 TYPHIMURIUM.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 31524
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1677
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2299
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6337
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.09000
REMARK 3 B22 (A**2) : 0.52000
REMARK 3 B33 (A**2) : 2.62000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.99000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.544
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.277
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.649
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6705 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4602 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9180 ; 1.282 ; 1.925
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11056 ; 0.791 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 816 ; 1.906 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 330 ;23.350 ;22.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1001 ; 8.779 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ; 9.700 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 945 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7607 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1476 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 4035 ; 0.732 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1613 ; 0.170 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6517 ; 1.317 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2670 ; 2.165 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2663 ; 3.355 ; 4.500
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 : 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 7 A 102
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3159 24.2630 0.7538
REMARK 3 T TENSOR
REMARK 3 T11: 0.1815 T22: 0.1986
REMARK 3 T33: 0.1219 T12: -0.0752
REMARK 3 T13: -0.1023 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.1015 L22: 3.2307
REMARK 3 L33: 4.8843 L12: -0.0247
REMARK 3 L13: -0.3806 L23: -0.3304
REMARK 3 S TENSOR
REMARK 3 S11: -0.1040 S12: 0.4972 S13: 0.0588
REMARK 3 S21: -0.5427 S22: 0.1567 S23: 0.5409
REMARK 3 S31: -0.1218 S32: -0.3686 S33: -0.0527
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 103 A 137
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4185 19.3132 -1.2127
REMARK 3 T TENSOR
REMARK 3 T11: 0.1684 T22: 0.3131
REMARK 3 T33: 0.0602 T12: -0.1245
REMARK 3 T13: -0.0239 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 4.9141 L22: 16.3857
REMARK 3 L33: 8.0939 L12: -2.2687
REMARK 3 L13: -1.5115 L23: 5.2172
REMARK 3 S TENSOR
REMARK 3 S11: -0.1995 S12: 0.3553 S13: -0.0660
REMARK 3 S21: -0.5172 S22: 0.5925 S23: -0.7105
REMARK 3 S31: 0.2932 S32: 0.7957 S33: -0.3930
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 138 A 173
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5260 30.5980 20.7458
REMARK 3 T TENSOR
REMARK 3 T11: 0.1984 T22: 0.0572
REMARK 3 T33: 0.1156 T12: 0.0276
REMARK 3 T13: 0.0312 T23: -0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 5.1840 L22: 2.8464
REMARK 3 L33: 2.1947 L12: 3.3295
REMARK 3 L13: 2.1147 L23: 0.5469
REMARK 3 S TENSOR
REMARK 3 S11: -0.1584 S12: -0.0680 S13: 0.2198
REMARK 3 S21: 0.0413 S22: -0.0480 S23: 0.1570
REMARK 3 S31: 0.0041 S32: -0.0479 S33: 0.2065
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 174 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8917 24.8303 25.3313
REMARK 3 T TENSOR
REMARK 3 T11: 0.0231 T22: 0.0569
REMARK 3 T33: 0.0268 T12: 0.0143
REMARK 3 T13: -0.0055 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.9607 L22: 2.8516
REMARK 3 L33: 2.2889 L12: 0.7092
REMARK 3 L13: -0.4953 L23: 0.4318
REMARK 3 S TENSOR
REMARK 3 S11: -0.0538 S12: -0.1080 S13: -0.1491
REMARK 3 S21: 0.1683 S22: -0.0336 S23: -0.1919
REMARK 3 S31: 0.1591 S32: 0.3300 S33: 0.0874
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 318 A 339
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4189 3.8453 19.4158
REMARK 3 T TENSOR
REMARK 3 T11: 1.1276 T22: 0.6683
REMARK 3 T33: 2.0694 T12: 0.2697
REMARK 3 T13: 0.0289 T23: 0.2686
REMARK 3 L TENSOR
REMARK 3 L11: 0.1309 L22: 33.5707
REMARK 3 L33: 3.2688 L12: 1.8018
REMARK 3 L13: 0.5678 L23: 10.4700
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: -0.0054 S13: -0.4271
REMARK 3 S21: -0.9934 S22: 1.2032 S23: -3.4818
REMARK 3 S31: -0.2605 S32: 0.3715 S33: -1.1390
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 340 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7543 13.1275 25.4285
REMARK 3 T TENSOR
REMARK 3 T11: 0.1171 T22: 0.0273
REMARK 3 T33: 0.1064 T12: -0.0119
REMARK 3 T13: 0.0553 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.9986 L22: 4.0827
REMARK 3 L33: 4.8157 L12: 0.0494
REMARK 3 L13: 0.2915 L23: 0.7100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0321 S12: -0.0286 S13: -0.3811
REMARK 3 S21: 0.0929 S22: -0.2180 S23: -0.0332
REMARK 3 S31: 0.4779 S32: 0.1377 S33: 0.1858
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 9 B 101
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0601 60.5091 4.2434
REMARK 3 T TENSOR
REMARK 3 T11: 0.1425 T22: 0.5019
REMARK 3 T33: 0.1592 T12: 0.0289
REMARK 3 T13: 0.1135 T23: 0.1569
REMARK 3 L TENSOR
REMARK 3 L11: 5.6543 L22: 4.1028
REMARK 3 L33: 4.1540 L12: 0.6087
REMARK 3 L13: 1.4432 L23: 0.7845
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: 1.4958 S13: 0.2516
REMARK 3 S21: -0.7109 S22: 0.1265 S23: -0.5160
REMARK 3 S31: 0.0798 S32: 0.4706 S33: -0.0869
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 102 B 136
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0100 65.8202 1.7698
REMARK 3 T TENSOR
REMARK 3 T11: 0.3021 T22: 0.5980
REMARK 3 T33: 0.1002 T12: -0.0308
REMARK 3 T13: 0.0082 T23: 0.1219
REMARK 3 L TENSOR
REMARK 3 L11: 9.0057 L22: 14.8313
REMARK 3 L33: 6.9231 L12: -3.5490
REMARK 3 L13: 3.3123 L23: -0.8296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0279 S12: 0.8093 S13: 0.3308
REMARK 3 S21: -1.0314 S22: 0.0230 S23: 0.6971
REMARK 3 S31: -0.5045 S32: -0.3714 S33: 0.0049
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 137 B 173
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7337 51.3479 22.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0813 T22: 0.1052
REMARK 3 T33: 0.1311 T12: 0.0307
REMARK 3 T13: -0.0186 T23: 0.0749
REMARK 3 L TENSOR
REMARK 3 L11: 5.8012 L22: 2.5188
REMARK 3 L33: 1.5049 L12: 1.9460
REMARK 3 L13: -1.5876 L23: -0.5693
REMARK 3 S TENSOR
REMARK 3 S11: 0.0780 S12: 0.0941 S13: -0.3467
REMARK 3 S21: 0.0462 S22: -0.0792 S23: -0.2703
REMARK 3 S31: 0.1492 S32: 0.1134 S33: 0.0012
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 174 B 317
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2300 56.4325 28.2286
REMARK 3 T TENSOR
REMARK 3 T11: 0.0179 T22: 0.0757
REMARK 3 T33: 0.0303 T12: -0.0194
REMARK 3 T13: 0.0122 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.5861 L22: 3.0067
REMARK 3 L33: 1.9901 L12: 0.5221
REMARK 3 L13: 0.0333 L23: -0.1899
REMARK 3 S TENSOR
REMARK 3 S11: 0.1120 S12: -0.2548 S13: 0.1741
REMARK 3 S21: 0.1907 S22: 0.0134 S23: 0.2052
REMARK 3 S31: 0.0693 S32: -0.2764 S33: -0.1254
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 318 B 345
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1452 75.7584 28.3628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1556 T22: 0.0833
REMARK 3 T33: 0.2888 T12: 0.0335
REMARK 3 T13: 0.0250 T23: -0.0607
REMARK 3 L TENSOR
REMARK 3 L11: 5.1226 L22: 9.1822
REMARK 3 L33: 3.6803 L12: -2.0024
REMARK 3 L13: 0.4506 L23: -3.6513
REMARK 3 S TENSOR
REMARK 3 S11: 0.1349 S12: 0.0829 S13: 0.8246
REMARK 3 S21: 0.2617 S22: 0.0017 S23: 0.2809
REMARK 3 S31: -0.5588 S32: -0.2383 S33: -0.1367
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 346 B 403
REMARK 3 ORIGIN FOR THE GROUP (A): 53.2039 67.7331 29.5393
REMARK 3 T TENSOR
REMARK 3 T11: 0.2193 T22: 0.1705
REMARK 3 T33: 0.2066 T12: -0.0544
REMARK 3 T13: -0.0596 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 2.3997 L22: 3.2763
REMARK 3 L33: 2.4538 L12: 0.8104
REMARK 3 L13: -1.0082 L23: -1.7976
REMARK 3 S TENSOR
REMARK 3 S11: 0.2262 S12: -0.4212 S13: 0.4736
REMARK 3 S21: 0.6690 S22: -0.3238 S23: -0.2139
REMARK 3 S31: -0.5583 S32: 0.3443 S33: 0.0976
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3MGA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33389
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: CRANK
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 0.3M NACL, 10MM
REMARK 280 HEPES (PH 7.5); SCREEN SOLUTION: 0.2M SODIUM CHLORIDE, 0.1M
REMARK 280 SODIUM CITRATE PH 5.6, 1% DMSO, 20% PEG3350, 0.3M NDSB, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 62.77600
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 GLU A 3
REMARK 465 ALA A 4
REMARK 465 LEU A 5
REMARK 465 ALA A 6
REMARK 465 LEU A 404
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 GLU B 3
REMARK 465 ALA B 4
REMARK 465 LEU B 5
REMARK 465 ALA B 6
REMARK 465 THR B 7
REMARK 465 GLY B 8
REMARK 465 LEU B 404
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 VAL A 57 -50.14 -127.92
REMARK 500 ASP A 59 -163.55 -107.51
REMARK 500 ALA A 73 125.89 -35.76
REMARK 500 ASP A 100 24.72 -144.99
REMARK 500 VAL A 102 -60.21 -100.25
REMARK 500 ALA A 195 71.29 24.88
REMARK 500 GLU A 212 -58.33 -121.24
REMARK 500 ILE A 240 -70.50 79.33
REMARK 500 SER A 286 -122.57 61.69
REMARK 500 ASN A 365 88.32 -59.54
REMARK 500 GLN B 39 43.08 -93.99
REMARK 500 ASP B 59 -169.93 -105.92
REMARK 500 ALA B 73 114.40 -31.29
REMARK 500 VAL B 102 -68.39 -94.20
REMARK 500 ARG B 162 69.73 -118.50
REMARK 500 ALA B 195 67.26 37.83
REMARK 500 GLU B 212 -60.17 -122.99
REMARK 500 ILE B 240 -69.43 72.29
REMARK 500 PRO B 250 80.27 -68.52
REMARK 500 SER B 286 -126.09 57.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 405 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 323 O
REMARK 620 2 THR B 320 O 96.5
REMARK 620 3 TRP B 314 O 85.9 143.3
REMARK 620 4 HIS B 317 O 170.8 92.7 86.5
REMARK 620 5 HOH B 450 O 84.9 134.2 82.5 88.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 191 OG1
REMARK 620 2 PRO B 230 O 94.4
REMARK 620 3 THR B 224 OG1 86.0 110.9
REMARK 620 4 TYR B 234 OH 118.7 117.6 121.9
REMARK 620 N 1 2 3
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 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00118 RELATED DB: TARGETDB
DBREF 3MGA A 1 404 UNP Q8ZR39 Q8ZR39_SALTY 1 404
DBREF 3MGA B 1 404 UNP Q8ZR39 Q8ZR39_SALTY 1 404
SEQADV 3MGA SER A -2 UNP Q8ZR39 EXPRESSION TAG
SEQADV 3MGA ASN A -1 UNP Q8ZR39 EXPRESSION TAG
SEQADV 3MGA ALA A 0 UNP Q8ZR39 EXPRESSION TAG
SEQADV 3MGA SER B -2 UNP Q8ZR39 EXPRESSION TAG
SEQADV 3MGA ASN B -1 UNP Q8ZR39 EXPRESSION TAG
SEQADV 3MGA ALA B 0 UNP Q8ZR39 EXPRESSION TAG
SEQRES 1 A 407 SER ASN ALA MSE LYS GLU ALA LEU ALA THR GLY SER GLU
SEQRES 2 A 407 ALA TRP TRP ARG THR LYS THR GLY PRO GLU TRP ILE ARG
SEQRES 3 A 407 GLU LYS ASP GLY ASN TYR ARG VAL THR PHE TRP TRP ARG
SEQRES 4 A 407 ASP PRO GLN GLY ASN GLU THR HIS SER PRO ILE ARG ARG
SEQRES 5 A 407 VAL TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN
SEQRES 6 A 407 ASN ALA GLN PRO GLN THR MSE ALA ARG ILE ALA GLY THR
SEQRES 7 A 407 ASP VAL TRP ARG TRP SER THR ALA LEU SER ALA ASN TRP
SEQRES 8 A 407 ARG GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP
SEQRES 9 A 407 VAL PHE ALA ALA PHE ALA PRO GLY GLU THR PRO ASP ARG
SEQRES 10 A 407 ASN VAL LEU ARG GLU GLY TRP ARG GLN LEU LEU PRO GLN
SEQRES 11 A 407 ALA ILE ALA ASP PRO LEU ASN SER GLN SER TRP ARG GLY
SEQRES 12 A 407 GLY ARG GLY HIS ALA VAL SER ALA LEU GLU MSE PRO ASP
SEQRES 13 A 407 ALA PRO LEU GLN PRO GLY TRP ASP ARG PRO GLU THR PRO
SEQRES 14 A 407 TYR SER PRO PRO LEU MSE MSE GLN TRP HIS SER GLU ARG
SEQRES 15 A 407 LEU GLY ASN SER ARG ARG VAL TRP ILE LEU THR THR GLY
SEQRES 16 A 407 ASP GLU ALA PRO GLU GLU ARG PRO LEU ALA ILE LEU LEU
SEQRES 17 A 407 ASP GLY GLN PHE TRP ALA GLU ASN MSE PRO VAL TRP PRO
SEQRES 18 A 407 ALA LEU ALA SER LEU THR HIS GLN ARG LEU LEU PRO GLY
SEQRES 19 A 407 ALA VAL TYR LEU LEU ILE ASP ALA ILE ASP THR GLN HIS
SEQRES 20 A 407 ARG SER GLN GLU LEU PRO CYS ASN ALA ASP PHE TRP LEU
SEQRES 21 A 407 ALA VAL GLN GLN GLU LEU LEU PRO GLN VAL ARG ALA VAL
SEQRES 22 A 407 THR PRO PHE SER ASP ASP ALA GLY ARG THR VAL VAL ALA
SEQRES 23 A 407 GLY GLN SER PHE GLY GLY LEU SER ALA LEU TYR ALA GLY
SEQRES 24 A 407 LEU ASN TRP PRO THR ARG PHE GLY CYS VAL LEU SER GLN
SEQRES 25 A 407 SER GLY SER PHE TRP TRP PRO HIS ARG ILE THR PRO PRO
SEQRES 26 A 407 GLU GLY GLU VAL ILE THR ARG LEU LYS THR GLY ALA LEU
SEQRES 27 A 407 CYS ALA ARG GLY LEU ARG ILE VAL LEU GLU ALA GLY VAL
SEQRES 28 A 407 ARG GLU PRO ILE VAL PHE GLN ALA ASN GLN ALA LEU TYR
SEQRES 29 A 407 ALA GLN LEU ASN THR SER GLN GLN SER ILE PHE TRP ARG
SEQRES 30 A 407 GLN VAL ASP GLY GLY HIS ASP ALA LEU CYS TRP ARG GLY
SEQRES 31 A 407 GLY LEU THR GLN GLY LEU MSE LEU LEU TRP GLN PRO LEU
SEQRES 32 A 407 ILE ASP THR LEU
SEQRES 1 B 407 SER ASN ALA MSE LYS GLU ALA LEU ALA THR GLY SER GLU
SEQRES 2 B 407 ALA TRP TRP ARG THR LYS THR GLY PRO GLU TRP ILE ARG
SEQRES 3 B 407 GLU LYS ASP GLY ASN TYR ARG VAL THR PHE TRP TRP ARG
SEQRES 4 B 407 ASP PRO GLN GLY ASN GLU THR HIS SER PRO ILE ARG ARG
SEQRES 5 B 407 VAL TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN
SEQRES 6 B 407 ASN ALA GLN PRO GLN THR MSE ALA ARG ILE ALA GLY THR
SEQRES 7 B 407 ASP VAL TRP ARG TRP SER THR ALA LEU SER ALA ASN TRP
SEQRES 8 B 407 ARG GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP
SEQRES 9 B 407 VAL PHE ALA ALA PHE ALA PRO GLY GLU THR PRO ASP ARG
SEQRES 10 B 407 ASN VAL LEU ARG GLU GLY TRP ARG GLN LEU LEU PRO GLN
SEQRES 11 B 407 ALA ILE ALA ASP PRO LEU ASN SER GLN SER TRP ARG GLY
SEQRES 12 B 407 GLY ARG GLY HIS ALA VAL SER ALA LEU GLU MSE PRO ASP
SEQRES 13 B 407 ALA PRO LEU GLN PRO GLY TRP ASP ARG PRO GLU THR PRO
SEQRES 14 B 407 TYR SER PRO PRO LEU MSE MSE GLN TRP HIS SER GLU ARG
SEQRES 15 B 407 LEU GLY ASN SER ARG ARG VAL TRP ILE LEU THR THR GLY
SEQRES 16 B 407 ASP GLU ALA PRO GLU GLU ARG PRO LEU ALA ILE LEU LEU
SEQRES 17 B 407 ASP GLY GLN PHE TRP ALA GLU ASN MSE PRO VAL TRP PRO
SEQRES 18 B 407 ALA LEU ALA SER LEU THR HIS GLN ARG LEU LEU PRO GLY
SEQRES 19 B 407 ALA VAL TYR LEU LEU ILE ASP ALA ILE ASP THR GLN HIS
SEQRES 20 B 407 ARG SER GLN GLU LEU PRO CYS ASN ALA ASP PHE TRP LEU
SEQRES 21 B 407 ALA VAL GLN GLN GLU LEU LEU PRO GLN VAL ARG ALA VAL
SEQRES 22 B 407 THR PRO PHE SER ASP ASP ALA GLY ARG THR VAL VAL ALA
SEQRES 23 B 407 GLY GLN SER PHE GLY GLY LEU SER ALA LEU TYR ALA GLY
SEQRES 24 B 407 LEU ASN TRP PRO THR ARG PHE GLY CYS VAL LEU SER GLN
SEQRES 25 B 407 SER GLY SER PHE TRP TRP PRO HIS ARG ILE THR PRO PRO
SEQRES 26 B 407 GLU GLY GLU VAL ILE THR ARG LEU LYS THR GLY ALA LEU
SEQRES 27 B 407 CYS ALA ARG GLY LEU ARG ILE VAL LEU GLU ALA GLY VAL
SEQRES 28 B 407 ARG GLU PRO ILE VAL PHE GLN ALA ASN GLN ALA LEU TYR
SEQRES 29 B 407 ALA GLN LEU ASN THR SER GLN GLN SER ILE PHE TRP ARG
SEQRES 30 B 407 GLN VAL ASP GLY GLY HIS ASP ALA LEU CYS TRP ARG GLY
SEQRES 31 B 407 GLY LEU THR GLN GLY LEU MSE LEU LEU TRP GLN PRO LEU
SEQRES 32 B 407 ILE ASP THR LEU
MODRES 3MGA MSE A 69 MET SELENOMETHIONINE
MODRES 3MGA MSE A 151 MET SELENOMETHIONINE
MODRES 3MGA MSE A 172 MET SELENOMETHIONINE
MODRES 3MGA MSE A 173 MET SELENOMETHIONINE
MODRES 3MGA MSE A 214 MET SELENOMETHIONINE
MODRES 3MGA MSE A 394 MET SELENOMETHIONINE
MODRES 3MGA MSE B 69 MET SELENOMETHIONINE
MODRES 3MGA MSE B 151 MET SELENOMETHIONINE
MODRES 3MGA MSE B 172 MET SELENOMETHIONINE
MODRES 3MGA MSE B 173 MET SELENOMETHIONINE
MODRES 3MGA MSE B 214 MET SELENOMETHIONINE
MODRES 3MGA MSE B 394 MET SELENOMETHIONINE
HET MSE A 69 8
HET MSE A 151 8
HET MSE A 172 16
HET MSE A 173 8
HET MSE A 214 16
HET MSE A 394 8
HET MSE B 69 8
HET MSE B 151 8
HET MSE B 172 16
HET MSE B 173 8
HET MSE B 214 16
HET MSE B 394 8
HET CL A 405 1
HET CL A 406 1
HET GOL A 407 6
HET PEG A 408 7
HET MG B 405 1
HET NA B 406 1
HET CL B 407 1
HET GOL B 408 6
HET GOL B 409 6
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM MG MAGNESIUM ION
HETNAM NA SODIUM ION
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 CL 3(CL 1-)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 6 PEG C4 H10 O3
FORMUL 7 MG MG 2+
FORMUL 8 NA NA 1+
FORMUL 12 HOH *183(H2 O)
HELIX 1 1 SER A 9 THR A 15 1 7
HELIX 2 2 ASP A 59 ASN A 63 5 5
HELIX 3 3 ASP A 113 LEU A 125 1 13
HELIX 4 4 PRO A 126 ALA A 128 5 3
HELIX 5 5 ALA A 195 ARG A 199 5 5
HELIX 6 6 ASP A 206 GLU A 212 1 7
HELIX 7 7 VAL A 216 GLN A 226 1 11
HELIX 8 8 ASP A 241 LEU A 249 1 9
HELIX 9 9 ASN A 252 GLU A 262 1 11
HELIX 10 10 GLU A 262 THR A 271 1 10
HELIX 11 11 ASP A 276 ARG A 279 5 4
HELIX 12 12 SER A 286 TRP A 299 1 14
HELIX 13 13 GLY A 324 GLY A 333 1 10
HELIX 14 14 GLU A 350 ASN A 365 1 16
HELIX 15 15 ASP A 381 TRP A 397 1 17
HELIX 16 16 TRP A 397 ASP A 402 1 6
HELIX 17 17 ASP B 59 ASN B 63 5 5
HELIX 18 18 ASP B 113 LEU B 125 1 13
HELIX 19 19 PRO B 126 ALA B 128 5 3
HELIX 20 20 ASP B 206 GLU B 212 1 7
HELIX 21 21 VAL B 216 GLN B 226 1 11
HELIX 22 22 ASP B 241 LEU B 249 1 9
HELIX 23 23 ASN B 252 GLU B 262 1 11
HELIX 24 24 GLU B 262 THR B 271 1 10
HELIX 25 25 ASP B 276 ARG B 279 5 4
HELIX 26 26 SER B 286 TRP B 299 1 14
HELIX 27 27 GLY B 324 THR B 332 1 9
HELIX 28 28 GLU B 350 LEU B 364 1 15
HELIX 29 29 ASP B 381 TRP B 397 1 17
HELIX 30 30 TRP B 397 THR B 403 1 7
SHEET 1 A 4 GLU A 20 ARG A 23 0
SHEET 2 A 4 TYR A 29 ARG A 36 -1 O THR A 32 N GLU A 20
SHEET 3 A 4 VAL A 77 LEU A 84 -1 O TRP A 80 N PHE A 33
SHEET 4 A 4 ALA A 70 ARG A 71 -1 N ALA A 70 O ARG A 79
SHEET 1 B 4 ARG A 49 ILE A 54 0
SHEET 2 B 4 ARG A 89 THR A 97 -1 O CYS A 93 N TYR A 53
SHEET 3 B 4 ALA A 145 GLU A 150 -1 O SER A 147 N TYR A 92
SHEET 4 B 4 SER A 137 ARG A 139 -1 N TRP A 138 O VAL A 146
SHEET 1 C 8 LEU A 171 SER A 177 0
SHEET 2 C 8 ASN A 182 THR A 190 -1 O ARG A 184 N TRP A 175
SHEET 3 C 8 VAL A 233 ILE A 237 -1 O TYR A 234 N LEU A 189
SHEET 4 C 8 LEU A 201 LEU A 204 1 N LEU A 204 O LEU A 235
SHEET 5 C 8 VAL A 281 GLN A 285 1 O ALA A 283 N ILE A 203
SHEET 6 C 8 CYS A 305 GLN A 309 1 O LEU A 307 N GLY A 284
SHEET 7 C 8 ARG A 341 GLY A 347 1 O GLU A 345 N SER A 308
SHEET 8 C 8 SER A 370 VAL A 376 1 O PHE A 372 N ILE A 342
SHEET 1 D 4 GLU B 20 ARG B 23 0
SHEET 2 D 4 TYR B 29 ARG B 36 -1 O THR B 32 N GLU B 20
SHEET 3 D 4 VAL B 77 LEU B 84 -1 O LEU B 84 N TYR B 29
SHEET 4 D 4 ALA B 70 ARG B 71 -1 N ALA B 70 O ARG B 79
SHEET 1 E 4 ARG B 49 ILE B 54 0
SHEET 2 E 4 ARG B 89 THR B 97 -1 O CYS B 93 N TYR B 53
SHEET 3 E 4 ALA B 145 GLU B 150 -1 O SER B 147 N TYR B 92
SHEET 4 E 4 SER B 137 ARG B 139 -1 N TRP B 138 O VAL B 146
SHEET 1 F 8 LEU B 171 SER B 177 0
SHEET 2 F 8 ASN B 182 THR B 190 -1 O ARG B 184 N TRP B 175
SHEET 3 F 8 VAL B 233 ILE B 237 -1 O TYR B 234 N LEU B 189
SHEET 4 F 8 LEU B 201 LEU B 204 1 N ALA B 202 O LEU B 235
SHEET 5 F 8 VAL B 281 GLN B 285 1 O VAL B 281 N ILE B 203
SHEET 6 F 8 CYS B 305 GLN B 309 1 O LEU B 307 N VAL B 282
SHEET 7 F 8 ARG B 341 GLY B 347 1 O GLU B 345 N SER B 308
SHEET 8 F 8 ILE B 371 VAL B 376 1 O PHE B 372 N ILE B 342
LINK C THR A 68 N MSE A 69 1555 1555 1.33
LINK C MSE A 69 N ALA A 70 1555 1555 1.33
LINK C GLU A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N PRO A 152 1555 1555 1.34
LINK C LEU A 171 N AMSE A 172 1555 1555 1.33
LINK C LEU A 171 N BMSE A 172 1555 1555 1.33
LINK C AMSE A 172 N MSE A 173 1555 1555 1.33
LINK C BMSE A 172 N MSE A 173 1555 1555 1.32
LINK C MSE A 173 N GLN A 174 1555 1555 1.32
LINK C ASN A 213 N AMSE A 214 1555 1555 1.32
LINK C ASN A 213 N BMSE A 214 1555 1555 1.33
LINK C AMSE A 214 N PRO A 215 1555 1555 1.35
LINK C BMSE A 214 N PRO A 215 1555 1555 1.35
LINK C LEU A 393 N MSE A 394 1555 1555 1.33
LINK C MSE A 394 N LEU A 395 1555 1555 1.33
LINK C THR B 68 N MSE B 69 1555 1555 1.33
LINK C MSE B 69 N ALA B 70 1555 1555 1.32
LINK C GLU B 150 N MSE B 151 1555 1555 1.33
LINK C MSE B 151 N PRO B 152 1555 1555 1.34
LINK C LEU B 171 N AMSE B 172 1555 1555 1.32
LINK C LEU B 171 N BMSE B 172 1555 1555 1.34
LINK C AMSE B 172 N MSE B 173 1555 1555 1.32
LINK C BMSE B 172 N MSE B 173 1555 1555 1.33
LINK C MSE B 173 N GLN B 174 1555 1555 1.33
LINK C ASN B 213 N AMSE B 214 1555 1555 1.33
LINK C ASN B 213 N BMSE B 214 1555 1555 1.33
LINK C AMSE B 214 N PRO B 215 1555 1555 1.35
LINK C BMSE B 214 N PRO B 215 1555 1555 1.35
LINK C LEU B 393 N MSE B 394 1555 1555 1.33
LINK C MSE B 394 N LEU B 395 1555 1555 1.33
LINK O GLU B 323 MG MG B 405 1555 1555 2.18
LINK O THR B 320 MG MG B 405 1555 1555 2.18
LINK O TRP B 314 MG MG B 405 1555 1555 2.18
LINK O HIS B 317 MG MG B 405 1555 1555 2.19
LINK OG1 THR B 191 NA NA B 406 1555 1555 2.60
LINK O PRO B 230 NA NA B 406 1555 1555 2.64
LINK OG1 THR B 224 NA NA B 406 1555 1555 2.68
LINK OH TYR B 234 NA NA B 406 1555 1555 2.80
LINK MG MG B 405 O HOH B 450 1555 1555 2.71
CISPEP 1 TRP A 315 PRO A 316 0 0.96
CISPEP 2 TRP B 315 PRO B 316 0 2.65
SITE 1 AC1 4 TRP A 51 ASP A 100 VAL A 102 PHE A 103
SITE 1 AC2 4 ARG A 139 GLY A 141 GLY A 143 HIS A 144
SITE 1 AC3 6 ARG A 142 ARG A 245 SER A 286 PHE A 287
SITE 2 AC3 6 ARG A 318 HIS A 380
SITE 1 AC4 3 TRP A 138 ARG A 386 HOH A 501
SITE 1 AC5 5 TRP B 314 HIS B 317 THR B 320 GLU B 323
SITE 2 AC5 5 HOH B 450
SITE 1 AC6 4 THR B 191 THR B 224 PRO B 230 TYR B 234
SITE 1 AC7 4 HIS B 61 GLU B 350 PRO B 351 ILE B 352
SITE 1 AC8 4 ARG B 245 SER B 286 PHE B 287 ARG B 318
SITE 1 AC9 3 SER B 137 TRP B 138 ARG B 386
CRYST1 52.489 125.552 66.606 90.00 91.43 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 0.019052 0.000000 0.000474 0.00000
SCALE2 0.000000 0.007965 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015018 0.00000
END |