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HEADER HYDROLASE 30-SEP-11 3U1T
TITLE HALOALKANE DEHALOGENASE, DMMA, OF MARINE MICROBIAL ORIGIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DMMA HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DMMASHORT;
COMPND 5 EC: 3.8.1.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-24B
KEYWDS ALPHA/BETA-HYDROLASE, HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J GEHRET,J.L.SMITH
REVDAT 1 28-DEC-11 3U1T 0
JRNL AUTH J.J.GEHRET,L.GU,T.W.GEDERS,W.C.BROWN,L.GERWICK,W.H.GERWICK,
JRNL AUTH 2 D.H.SHERMAN,J.L.SMITH
JRNL TITL STRUCTURE AND ACTIVITY OF DMMA, A MARINE HALOALKANE
JRNL TITL 2 DEHALOGENASE.
JRNL REF PROTEIN SCI. 2011
JRNL REFN ESSN 1469-896X
JRNL PMID 22124946
JRNL DOI 10.1002/PRO.2009
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 33173
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1746
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2408
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4628
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 497
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.10000
REMARK 3 B22 (A**2) : 1.10000
REMARK 3 B33 (A**2) : -1.66000
REMARK 3 B12 (A**2) : 0.55000
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): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.157
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.240
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4801 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6556 ; 1.195 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 603 ; 4.974 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 215 ;31.819 ;23.395
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 729 ;13.124 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;16.544 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 705 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3777 ; 0.005 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3003 ; 0.362 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4848 ; 0.718 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1798 ; 1.479 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1704 ; 2.369 ; 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 : 10
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 44 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6973 23.6756 50.2337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0670 T22: 0.1005
REMARK 3 T33: 0.0240 T12: -0.0087
REMARK 3 T13: 0.0054 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.4868 L22: 0.5360
REMARK 3 L33: 1.1181 L12: 0.3750
REMARK 3 L13: -0.3495 L23: -0.5319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: 0.1047 S13: -0.0084
REMARK 3 S21: -0.0696 S22: -0.0127 S23: 0.0334
REMARK 3 S31: 0.0493 S32: -0.0194 S33: 0.0145
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 114 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9589 33.7999 59.9725
REMARK 3 T TENSOR
REMARK 3 T11: 0.0806 T22: 0.0760
REMARK 3 T33: 0.0641 T12: -0.0111
REMARK 3 T13: 0.0115 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 0.9853 L22: 0.7046
REMARK 3 L33: 1.1528 L12: 0.2497
REMARK 3 L13: -0.2853 L23: 0.1640
REMARK 3 S TENSOR
REMARK 3 S11: 0.0185 S12: 0.0450 S13: 0.0871
REMARK 3 S21: 0.0606 S22: -0.0568 S23: 0.0122
REMARK 3 S31: -0.2264 S32: 0.0197 S33: 0.0383
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 178 A 256
REMARK 3 ORIGIN FOR THE GROUP (A): 63.5302 22.6696 64.0506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0347 T22: 0.1314
REMARK 3 T33: 0.0488 T12: -0.0282
REMARK 3 T13: 0.0150 T23: 0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 0.7738 L22: 0.6435
REMARK 3 L33: 1.4357 L12: -0.0607
REMARK 3 L13: 0.1786 L23: 0.1995
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: 0.0537 S13: -0.0530
REMARK 3 S21: 0.0567 S22: -0.0529 S23: -0.0577
REMARK 3 S31: -0.0290 S32: 0.1202 S33: 0.0312
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 257 A 273
REMARK 3 ORIGIN FOR THE GROUP (A): 48.9805 38.3874 70.2081
REMARK 3 T TENSOR
REMARK 3 T11: 0.1938 T22: 0.0422
REMARK 3 T33: 0.0779 T12: -0.0246
REMARK 3 T13: -0.0013 T23: -0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 15.2278 L22: 2.2439
REMARK 3 L33: 2.0057 L12: 0.2964
REMARK 3 L13: -2.7779 L23: 1.3074
REMARK 3 S TENSOR
REMARK 3 S11: 0.1226 S12: -0.1837 S13: 0.3421
REMARK 3 S21: 0.2074 S22: -0.1326 S23: 0.0428
REMARK 3 S31: -0.2200 S32: -0.0686 S33: 0.0099
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 274 A 341
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7606 21.5180 68.3103
REMARK 3 T TENSOR
REMARK 3 T11: 0.0603 T22: 0.0876
REMARK 3 T33: 0.0378 T12: -0.0187
REMARK 3 T13: 0.0289 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 1.4247 L22: 0.9816
REMARK 3 L33: 0.8556 L12: 0.3010
REMARK 3 L13: -0.0075 L23: -0.1163
REMARK 3 S TENSOR
REMARK 3 S11: 0.0574 S12: -0.0433 S13: 0.0631
REMARK 3 S21: 0.0819 S22: -0.0648 S23: 0.0636
REMARK 3 S31: 0.0037 S32: -0.0594 S33: 0.0074
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 : B 44 B 118
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9821 1.3443 86.7254
REMARK 3 T TENSOR
REMARK 3 T11: 0.0667 T22: 0.1125
REMARK 3 T33: 0.0518 T12: -0.0487
REMARK 3 T13: 0.0466 T23: -0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 0.3806 L22: 1.5435
REMARK 3 L33: 1.3494 L12: -0.1713
REMARK 3 L13: -0.1389 L23: -0.6606
REMARK 3 S TENSOR
REMARK 3 S11: 0.0351 S12: -0.1000 S13: 0.0199
REMARK 3 S21: 0.2490 S22: -0.0280 S23: 0.1529
REMARK 3 S31: -0.0265 S32: -0.0838 S33: -0.0071
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 119 B 176
REMARK 3 ORIGIN FOR THE GROUP (A): 14.9855 4.5110 77.4791
REMARK 3 T TENSOR
REMARK 3 T11: 0.0328 T22: 0.1528
REMARK 3 T33: 0.1410 T12: -0.0361
REMARK 3 T13: 0.0194 T23: -0.0648
REMARK 3 L TENSOR
REMARK 3 L11: 0.5018 L22: 1.1225
REMARK 3 L33: 1.4130 L12: -0.1122
REMARK 3 L13: -0.0885 L23: -0.3363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0782 S12: -0.0821 S13: -0.0203
REMARK 3 S21: -0.0374 S22: -0.0276 S23: 0.3102
REMARK 3 S31: -0.0515 S32: -0.2581 S33: -0.0506
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 177 B 196
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1927 -13.4015 62.1826
REMARK 3 T TENSOR
REMARK 3 T11: 0.4719 T22: 0.3442
REMARK 3 T33: 0.1630 T12: 0.0174
REMARK 3 T13: -0.0082 T23: -0.1097
REMARK 3 L TENSOR
REMARK 3 L11: 17.7836 L22: 4.2399
REMARK 3 L33: 19.2650 L12: -6.6739
REMARK 3 L13: -0.0033 L23: -5.7763
REMARK 3 S TENSOR
REMARK 3 S11: 1.0609 S12: 0.8466 S13: 0.7152
REMARK 3 S21: -0.3391 S22: -0.9366 S23: -0.2451
REMARK 3 S31: -0.3869 S32: 1.6550 S33: -0.1243
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 197 B 251
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7442 -14.2107 77.7459
REMARK 3 T TENSOR
REMARK 3 T11: 0.1207 T22: 0.0904
REMARK 3 T33: 0.0572 T12: -0.0411
REMARK 3 T13: -0.0016 T23: -0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 0.1288 L22: 2.4588
REMARK 3 L33: 0.8922 L12: -0.0664
REMARK 3 L13: -0.2973 L23: 0.1510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: -0.0190 S13: -0.0446
REMARK 3 S21: -0.0585 S22: -0.0529 S23: 0.0209
REMARK 3 S31: 0.2113 S32: 0.0023 S33: 0.0759
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 252 B 341
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0585 7.5968 68.5527
REMARK 3 T TENSOR
REMARK 3 T11: 0.0438 T22: 0.0976
REMARK 3 T33: 0.0383 T12: 0.0031
REMARK 3 T13: -0.0098 T23: -0.0523
REMARK 3 L TENSOR
REMARK 3 L11: 1.1022 L22: 2.3050
REMARK 3 L33: 0.9864 L12: 0.4081
REMARK 3 L13: -0.2505 L23: -0.3365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0932 S12: 0.0596 S13: 0.0381
REMARK 3 S21: -0.2272 S22: -0.0986 S23: 0.1901
REMARK 3 S31: -0.0080 S32: -0.0652 S33: 0.0053
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3U1T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-11.
REMARK 100 THE RCSB ID CODE IS RCSB068198.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-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) : 0.97939
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35045
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.54900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): 51.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M SODIUM MALONATE PH 7.0, 5%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.33600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.66800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 81.33600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.66800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 99.78400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 41
REMARK 465 ALA A 42
REMARK 465 SER A 43
REMARK 465 LEU A 342
REMARK 465 GLU A 343
REMARK 465 HIS A 344
REMARK 465 HIS A 345
REMARK 465 HIS A 346
REMARK 465 HIS A 347
REMARK 465 HIS A 348
REMARK 465 HIS A 349
REMARK 465 MSE B 41
REMARK 465 ALA B 42
REMARK 465 LEU B 342
REMARK 465 GLU B 343
REMARK 465 HIS B 344
REMARK 465 HIS B 345
REMARK 465 HIS B 346
REMARK 465 HIS B 347
REMARK 465 HIS B 348
REMARK 465 HIS B 349
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 PRO A 48 40.57 -85.22
REMARK 500 PRO A 79 51.01 -108.83
REMARK 500 THR A 80 -160.25 -100.22
REMARK 500 LYS A 112 67.86 -117.20
REMARK 500 ASP A 144 -127.94 57.73
REMARK 500 GLN A 186 -63.29 -100.33
REMARK 500 ASP A 198 -49.50 76.83
REMARK 500 THR A 213 -58.19 -126.04
REMARK 500 ALA A 288 -71.60 -135.05
REMARK 500 THR A 314 -81.11 -115.79
REMARK 500 HIS A 321 57.74 -141.22
REMARK 500 LYS A 337 55.61 38.46
REMARK 500 PRO B 79 48.95 -107.91
REMARK 500 THR B 80 -159.09 -100.52
REMARK 500 LYS B 112 67.17 -118.71
REMARK 500 ASP B 144 -130.08 54.35
REMARK 500 ASP B 198 -50.16 77.23
REMARK 500 THR B 213 -53.49 -128.42
REMARK 500 ALA B 288 -72.58 -132.63
REMARK 500 THR B 314 -82.16 -112.74
REMARK 500 HIS B 321 53.49 -140.71
REMARK 500 LYS B 337 59.11 35.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 455 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH A 456 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 493 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH A 610 DISTANCE = 5.60 ANGSTROMS
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI B 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 351
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SQUENCE WAS ORIGINALLY ANNOTATED AS CURN FROM CYANOBACTERIA LYNGBYA
REMARK 999 MAJUSCULA. IT IS NOW THOUGHT THAT CURN GENETIC MATERIAL IS FROM A
REMARK 999 BACTERIA THAT WAS GROWING IN ASSOCIATION WITH L. MAJUSCULA AT THE
REMARK 999 TIME OF COSMID PREPARATION. CURN HAS BEEN RENAMED DMMA.
DBREF 3U1T A 44 341 UNP Q6DND9 Q6DND9_9CYAN 44 341
DBREF 3U1T B 44 341 UNP Q6DND9 Q6DND9_9CYAN 44 341
SEQADV 3U1T MSE A 41 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T ALA A 42 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T SER A 43 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T LEU A 342 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T GLU A 343 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS A 344 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS A 345 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS A 346 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS A 347 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS A 348 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS A 349 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T MSE B 41 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T ALA B 42 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T SER B 43 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T LEU B 342 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T GLU B 343 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS B 344 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS B 345 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS B 346 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS B 347 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS B 348 UNP Q6DND9 EXPRESSION TAG
SEQADV 3U1T HIS B 349 UNP Q6DND9 EXPRESSION TAG
SEQRES 1 A 309 MSE ALA SER SER SER GLU PHE PRO PHE ALA LYS ARG THR
SEQRES 2 A 309 VAL GLU VAL GLU GLY ALA THR ILE ALA TYR VAL ASP GLU
SEQRES 3 A 309 GLY SER GLY GLN PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 A 309 THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO TYR VAL
SEQRES 5 A 309 VAL ALA ALA GLY TYR ARG ALA VAL ALA PRO ASP LEU ILE
SEQRES 6 A 309 GLY MSE GLY ASP SER ALA LYS PRO ASP ILE GLU TYR ARG
SEQRES 7 A 309 LEU GLN ASP HIS VAL ALA TYR MSE ASP GLY PHE ILE ASP
SEQRES 8 A 309 ALA LEU GLY LEU ASP ASP MSE VAL LEU VAL ILE HIS ASP
SEQRES 9 A 309 TRP GLY SER VAL ILE GLY MSE ARG HIS ALA ARG LEU ASN
SEQRES 10 A 309 PRO ASP ARG VAL ALA ALA VAL ALA PHE MSE GLU ALA LEU
SEQRES 11 A 309 VAL PRO PRO ALA LEU PRO MSE PRO SER TYR GLU ALA MSE
SEQRES 12 A 309 GLY PRO GLN LEU GLY PRO LEU PHE ARG ASP LEU ARG THR
SEQRES 13 A 309 ALA ASP VAL GLY GLU LYS MSE VAL LEU ASP GLY ASN PHE
SEQRES 14 A 309 PHE VAL GLU THR ILE LEU PRO GLU MSE GLY VAL VAL ARG
SEQRES 15 A 309 SER LEU SER GLU ALA GLU MSE ALA ALA TYR ARG ALA PRO
SEQRES 16 A 309 PHE PRO THR ARG GLN SER ARG LEU PRO THR LEU GLN TRP
SEQRES 17 A 309 PRO ARG GLU VAL PRO ILE GLY GLY GLU PRO ALA PHE ALA
SEQRES 18 A 309 GLU ALA GLU VAL LEU LYS ASN GLY GLU TRP LEU MSE ALA
SEQRES 19 A 309 SER PRO ILE PRO LYS LEU LEU PHE HIS ALA GLU PRO GLY
SEQRES 20 A 309 ALA LEU ALA PRO LYS PRO VAL VAL ASP TYR LEU SER GLU
SEQRES 21 A 309 ASN VAL PRO ASN LEU GLU VAL ARG PHE VAL GLY ALA GLY
SEQRES 22 A 309 THR HIS PHE LEU GLN GLU ASP HIS PRO HIS LEU ILE GLY
SEQRES 23 A 309 GLN GLY ILE ALA ASP TRP LEU ARG ARG ASN LYS PRO HIS
SEQRES 24 A 309 ALA SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 309 MSE ALA SER SER SER GLU PHE PRO PHE ALA LYS ARG THR
SEQRES 2 B 309 VAL GLU VAL GLU GLY ALA THR ILE ALA TYR VAL ASP GLU
SEQRES 3 B 309 GLY SER GLY GLN PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 4 B 309 THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO TYR VAL
SEQRES 5 B 309 VAL ALA ALA GLY TYR ARG ALA VAL ALA PRO ASP LEU ILE
SEQRES 6 B 309 GLY MSE GLY ASP SER ALA LYS PRO ASP ILE GLU TYR ARG
SEQRES 7 B 309 LEU GLN ASP HIS VAL ALA TYR MSE ASP GLY PHE ILE ASP
SEQRES 8 B 309 ALA LEU GLY LEU ASP ASP MSE VAL LEU VAL ILE HIS ASP
SEQRES 9 B 309 TRP GLY SER VAL ILE GLY MSE ARG HIS ALA ARG LEU ASN
SEQRES 10 B 309 PRO ASP ARG VAL ALA ALA VAL ALA PHE MSE GLU ALA LEU
SEQRES 11 B 309 VAL PRO PRO ALA LEU PRO MSE PRO SER TYR GLU ALA MSE
SEQRES 12 B 309 GLY PRO GLN LEU GLY PRO LEU PHE ARG ASP LEU ARG THR
SEQRES 13 B 309 ALA ASP VAL GLY GLU LYS MSE VAL LEU ASP GLY ASN PHE
SEQRES 14 B 309 PHE VAL GLU THR ILE LEU PRO GLU MSE GLY VAL VAL ARG
SEQRES 15 B 309 SER LEU SER GLU ALA GLU MSE ALA ALA TYR ARG ALA PRO
SEQRES 16 B 309 PHE PRO THR ARG GLN SER ARG LEU PRO THR LEU GLN TRP
SEQRES 17 B 309 PRO ARG GLU VAL PRO ILE GLY GLY GLU PRO ALA PHE ALA
SEQRES 18 B 309 GLU ALA GLU VAL LEU LYS ASN GLY GLU TRP LEU MSE ALA
SEQRES 19 B 309 SER PRO ILE PRO LYS LEU LEU PHE HIS ALA GLU PRO GLY
SEQRES 20 B 309 ALA LEU ALA PRO LYS PRO VAL VAL ASP TYR LEU SER GLU
SEQRES 21 B 309 ASN VAL PRO ASN LEU GLU VAL ARG PHE VAL GLY ALA GLY
SEQRES 22 B 309 THR HIS PHE LEU GLN GLU ASP HIS PRO HIS LEU ILE GLY
SEQRES 23 B 309 GLN GLY ILE ALA ASP TRP LEU ARG ARG ASN LYS PRO HIS
SEQRES 24 B 309 ALA SER LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3U1T MSE A 107 MET SELENOMETHIONINE
MODRES 3U1T MSE A 126 MET SELENOMETHIONINE
MODRES 3U1T MSE A 138 MET SELENOMETHIONINE
MODRES 3U1T MSE A 151 MET SELENOMETHIONINE
MODRES 3U1T MSE A 167 MET SELENOMETHIONINE
MODRES 3U1T MSE A 177 MET SELENOMETHIONINE
MODRES 3U1T MSE A 183 MET SELENOMETHIONINE
MODRES 3U1T MSE A 203 MET SELENOMETHIONINE
MODRES 3U1T MSE A 218 MET SELENOMETHIONINE
MODRES 3U1T MSE A 229 MET SELENOMETHIONINE
MODRES 3U1T MSE A 273 MET SELENOMETHIONINE
MODRES 3U1T MSE B 107 MET SELENOMETHIONINE
MODRES 3U1T MSE B 126 MET SELENOMETHIONINE
MODRES 3U1T MSE B 138 MET SELENOMETHIONINE
MODRES 3U1T MSE B 151 MET SELENOMETHIONINE
MODRES 3U1T MSE B 167 MET SELENOMETHIONINE
MODRES 3U1T MSE B 177 MET SELENOMETHIONINE
MODRES 3U1T MSE B 183 MET SELENOMETHIONINE
MODRES 3U1T MSE B 203 MET SELENOMETHIONINE
MODRES 3U1T MSE B 218 MET SELENOMETHIONINE
MODRES 3U1T MSE B 229 MET SELENOMETHIONINE
MODRES 3U1T MSE B 273 MET SELENOMETHIONINE
HET MSE A 107 8
HET MSE A 126 8
HET MSE A 138 8
HET MSE A 151 8
HET MSE A 167 8
HET MSE A 177 8
HET MSE A 183 8
HET MSE A 203 8
HET MSE A 218 8
HET MSE A 229 8
HET MSE A 273 8
HET MSE B 107 8
HET MSE B 126 8
HET MSE B 138 8
HET MSE B 151 8
HET MSE B 167 8
HET MSE B 177 8
HET MSE B 183 8
HET MSE B 203 8
HET MSE B 218 8
HET MSE B 229 8
HET MSE B 273 8
HET CL A 1 1
HET CL A 350 1
HET MLI A 351 7
HET CL B 1 1
HET CL B 351 1
HET MLI B 350 7
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM MLI MALONATE ION
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 CL 4(CL 1-)
FORMUL 5 MLI 2(C3 H2 O4 2-)
FORMUL 9 HOH *497(H2 O)
HELIX 1 1 SER A 81 ARG A 86 5 6
HELIX 2 2 ILE A 88 ALA A 95 1 8
HELIX 3 3 ARG A 118 GLY A 134 1 17
HELIX 4 4 ASP A 144 ASN A 157 1 14
HELIX 5 5 TYR A 180 ALA A 182 5 3
HELIX 6 6 MSE A 183 ARG A 195 1 13
HELIX 7 7 ASP A 198 LEU A 205 1 8
HELIX 8 8 ASN A 208 THR A 213 1 6
HELIX 9 9 THR A 213 MSE A 218 1 6
HELIX 10 10 SER A 225 ALA A 234 1 10
HELIX 11 11 ARG A 239 SER A 241 5 3
HELIX 12 12 ARG A 242 VAL A 252 1 11
HELIX 13 13 PRO A 258 SER A 275 1 18
HELIX 14 14 PRO A 291 VAL A 302 1 12
HELIX 15 15 PHE A 316 HIS A 321 1 6
HELIX 16 16 HIS A 321 LYS A 337 1 17
HELIX 17 17 SER B 81 ARG B 86 5 6
HELIX 18 18 ILE B 88 ALA B 95 1 8
HELIX 19 19 ARG B 118 GLY B 134 1 17
HELIX 20 20 TRP B 145 ASN B 157 1 13
HELIX 21 21 TYR B 180 ALA B 182 5 3
HELIX 22 22 MSE B 183 ARG B 195 1 13
HELIX 23 23 ASP B 198 LEU B 205 1 8
HELIX 24 24 ASN B 208 THR B 213 1 6
HELIX 25 25 THR B 213 MSE B 218 1 6
HELIX 26 26 SER B 225 ALA B 234 1 10
HELIX 27 27 ARG B 239 SER B 241 5 3
HELIX 28 28 ARG B 242 VAL B 252 1 11
HELIX 29 29 PRO B 258 SER B 275 1 18
HELIX 30 30 PRO B 291 VAL B 302 1 12
HELIX 31 31 PHE B 316 HIS B 321 1 6
HELIX 32 32 HIS B 321 LYS B 337 1 17
SHEET 1 A 8 ARG A 52 VAL A 56 0
SHEET 2 A 8 ALA A 59 GLY A 67 -1 O ALA A 59 N VAL A 56
SHEET 3 A 8 ARG A 98 PRO A 102 -1 O ALA A 99 N GLU A 66
SHEET 4 A 8 PRO A 71 LEU A 75 1 N VAL A 72 O ARG A 98
SHEET 5 A 8 MSE A 138 HIS A 143 1 O VAL A 139 N LEU A 73
SHEET 6 A 8 VAL A 161 MSE A 167 1 O ALA A 165 N LEU A 140
SHEET 7 A 8 LYS A 279 PRO A 286 1 O LEU A 280 N PHE A 166
SHEET 8 A 8 LEU A 305 GLY A 313 1 O ARG A 308 N LEU A 281
SHEET 1 B 8 ARG B 52 VAL B 56 0
SHEET 2 B 8 ALA B 59 GLU B 66 -1 O TYR B 63 N ARG B 52
SHEET 3 B 8 ARG B 98 PRO B 102 -1 O ALA B 99 N GLU B 66
SHEET 4 B 8 PRO B 71 LEU B 75 1 N VAL B 72 O ARG B 98
SHEET 5 B 8 MSE B 138 ASP B 144 1 O VAL B 139 N LEU B 73
SHEET 6 B 8 VAL B 161 ALA B 169 1 O ALA B 165 N LEU B 140
SHEET 7 B 8 LYS B 279 PRO B 286 1 O LEU B 280 N PHE B 166
SHEET 8 B 8 LEU B 305 GLY B 313 1 O ARG B 308 N LEU B 281
LINK C GLY A 106 N MSE A 107 1555 1555 1.33
LINK C MSE A 107 N GLY A 108 1555 1555 1.33
LINK C TYR A 125 N MSE A 126 1555 1555 1.33
LINK C MSE A 126 N ASP A 127 1555 1555 1.33
LINK C ASP A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N VAL A 139 1555 1555 1.33
LINK C GLY A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N ARG A 152 1555 1555 1.34
LINK C PHE A 166 N MSE A 167 1555 1555 1.33
LINK C MSE A 167 N GLU A 168 1555 1555 1.33
LINK C PRO A 176 N MSE A 177 1555 1555 1.32
LINK C MSE A 177 N PRO A 178 1555 1555 1.35
LINK C ALA A 182 N MSE A 183 1555 1555 1.33
LINK C MSE A 183 N GLY A 184 1555 1555 1.33
LINK C LYS A 202 N MSE A 203 1555 1555 1.33
LINK C MSE A 203 N VAL A 204 1555 1555 1.32
LINK C GLU A 217 N MSE A 218 1555 1555 1.32
LINK C MSE A 218 N GLY A 219 1555 1555 1.33
LINK C GLU A 228 N MSE A 229 1555 1555 1.33
LINK C MSE A 229 N ALA A 230 1555 1555 1.33
LINK C LEU A 272 N MSE A 273 1555 1555 1.34
LINK C MSE A 273 N ALA A 274 1555 1555 1.33
LINK C GLY B 106 N MSE B 107 1555 1555 1.33
LINK C MSE B 107 N GLY B 108 1555 1555 1.33
LINK C TYR B 125 N MSE B 126 1555 1555 1.33
LINK C MSE B 126 N ASP B 127 1555 1555 1.34
LINK C ASP B 137 N MSE B 138 1555 1555 1.33
LINK C MSE B 138 N VAL B 139 1555 1555 1.33
LINK C GLY B 150 N MSE B 151 1555 1555 1.33
LINK C MSE B 151 N ARG B 152 1555 1555 1.34
LINK C PHE B 166 N MSE B 167 1555 1555 1.33
LINK C MSE B 167 N GLU B 168 1555 1555 1.34
LINK C PRO B 176 N MSE B 177 1555 1555 1.33
LINK C MSE B 177 N PRO B 178 1555 1555 1.35
LINK C ALA B 182 N MSE B 183 1555 1555 1.33
LINK C MSE B 183 N GLY B 184 1555 1555 1.33
LINK C LYS B 202 N MSE B 203 1555 1555 1.33
LINK C MSE B 203 N VAL B 204 1555 1555 1.33
LINK C GLU B 217 N MSE B 218 1555 1555 1.33
LINK C MSE B 218 N GLY B 219 1555 1555 1.33
LINK C GLU B 228 N MSE B 229 1555 1555 1.33
LINK C MSE B 229 N ALA B 230 1555 1555 1.33
LINK C LEU B 272 N MSE B 273 1555 1555 1.33
LINK C MSE B 273 N ALA B 274 1555 1555 1.33
CISPEP 1 ASN A 78 PRO A 79 0 -3.46
CISPEP 2 PRO A 172 PRO A 173 0 8.57
CISPEP 3 LEU A 175 PRO A 176 0 -2.04
CISPEP 4 GLU A 257 PRO A 258 0 -2.98
CISPEP 5 GLU A 285 PRO A 286 0 3.01
CISPEP 6 ASN B 78 PRO B 79 0 -2.68
CISPEP 7 PRO B 172 PRO B 173 0 5.22
CISPEP 8 LEU B 175 PRO B 176 0 -1.49
CISPEP 9 GLU B 257 PRO B 258 0 -4.39
CISPEP 10 GLU B 285 PRO B 286 0 1.41
SITE 1 AC1 4 HIS A 321 PRO A 322 HIS A 323 LEU A 324
SITE 1 AC2 5 HIS B 321 PRO B 322 HIS B 323 LEU B 324
SITE 2 AC2 5 HOH B 502
SITE 1 AC3 5 ASN A 78 TRP A 145 PHE A 210 PRO A 249
SITE 2 AC3 5 HOH A 621
SITE 1 AC4 7 LEU A 187 MSE A 218 GLY A 219 THR A 314
SITE 2 AC4 7 HIS A 315 HOH A 492 HOH A 498
SITE 1 AC5 5 LEU B 187 GLY B 219 HIS B 315 HOH B 407
SITE 2 AC5 5 HOH B 515
SITE 1 AC6 4 TRP B 145 TRP B 248 PRO B 249 HOH B 407
CRYST1 99.784 99.784 122.004 90.00 90.00 120.00 P 62 12
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 0.010022 0.005786 0.000000 0.00000
SCALE2 0.000000 0.011572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008196 0.00000
TER 2325 SER A 341
TER 4651 SER B 341
MASTER 551 0 28 32 16 0 10 6 5143 2 234 48
END |