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HEADER HYDROLASE 23-MAR-15 4UHB
TITLE LABORATORY EVOLVED VARIANT R-C1 OF POTATO EPOXIDE HYDROLASE STEH1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: STEH1;
COMPND 5 EC: 3.3.2.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SOLANUM TUBEROSUM;
SOURCE 3 ORGANISM_COMMON: POTATO;
SOURCE 4 ORGANISM_TAXID: 4113;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGTAC
KEYWDS HYDROLASE, DIRECTED EVOLUTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.T.I.NILSSON,A.J.CARLSSON,D.DOBRITZSCH,M.WIDERSTEN
REVDAT 1 13-APR-16 4UHB 0
JRNL AUTH M.T.I.NILSSON,A.J.CARLSSON,D.DOBRITZSCH,M.WIDERSTEN
JRNL TITL LABORATORY EVOLVED VARIANT R-C1 OF POTATO EPOXIDE HYDROLASE
JRNL TITL 2 STEH1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.63
REMARK 3 NUMBER OF REFLECTIONS : 57139
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) : 0.19926
REMARK 3 R VALUE (WORKING SET) : 0.19865
REMARK 3 FREE R VALUE : 0.21090
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.800
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.847
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4221
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.255
REMARK 3 BIN FREE R VALUE SET COUNT : 222
REMARK 3 BIN FREE R VALUE : 0.284
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 591
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.172
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27
REMARK 3 B22 (A**2) : 0.96
REMARK 3 B33 (A**2) : -0.69
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.803
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5341 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5092 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7245 ; 1.650 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11740 ; 2.427 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 640 ; 5.985 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;33.349 ;23.833
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 850 ;13.944 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;20.247 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 773 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5931 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1241 ; 0.014 ; 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): 2560 ; 0.742 ; 1.004
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2559 ; 0.736 ; 1.004
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3197 ; 1.150 ; 1.502
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2781 ; 1.317 ; 1.183
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 320 B 3 320 19498 0.12 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
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 3 A 7
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5093 85.7954 -0.6651
REMARK 3 T TENSOR
REMARK 3 T11: 0.2131 T22: 0.1904
REMARK 3 T33: 0.4585 T12: 0.0242
REMARK 3 T13: 0.0929 T23: 0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 17.7530 L22: 5.2130
REMARK 3 L33: 18.4527 L12: -5.4640
REMARK 3 L13: -6.7090 L23: 4.4942
REMARK 3 S TENSOR
REMARK 3 S11: 0.2450 S12: 0.4496 S13: 0.5678
REMARK 3 S21: 0.2006 S22: -0.2408 S23: 1.0162
REMARK 3 S31: -0.7031 S32: -1.4869 S33: -0.0042
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 8 A 132
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8087 91.7514 1.3720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0377 T22: 0.0396
REMARK 3 T33: 0.0463 T12: 0.0007
REMARK 3 T13: -0.0052 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.6644 L22: 0.3599
REMARK 3 L33: 1.0338 L12: -0.0626
REMARK 3 L13: -0.0990 L23: 0.0180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: 0.0668 S13: 0.0198
REMARK 3 S21: -0.0379 S22: -0.0072 S23: 0.0170
REMARK 3 S31: -0.0432 S32: -0.0269 S33: 0.0022
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 133 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4631 85.3021 10.6299
REMARK 3 T TENSOR
REMARK 3 T11: 0.0575 T22: 0.1114
REMARK 3 T33: 0.0572 T12: -0.0142
REMARK 3 T13: -0.0228 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.0282 L22: 5.5162
REMARK 3 L33: 1.9652 L12: 1.7742
REMARK 3 L13: -1.6390 L23: -2.6379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0623 S12: -0.0489 S13: 0.0075
REMARK 3 S21: 0.2381 S22: -0.1587 S23: -0.2505
REMARK 3 S31: -0.1576 S32: 0.2305 S33: 0.0965
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 158 A 322
REMARK 3 ORIGIN FOR THE GROUP (A): 43.5805 85.6527 13.0699
REMARK 3 T TENSOR
REMARK 3 T11: 0.0299 T22: 0.0372
REMARK 3 T33: 0.0210 T12: 0.0041
REMARK 3 T13: -0.0095 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.5870 L22: 0.7213
REMARK 3 L33: 0.5521 L12: -0.0337
REMARK 3 L13: -0.1052 L23: -0.1922
REMARK 3 S TENSOR
REMARK 3 S11: -0.0172 S12: -0.0446 S13: -0.0188
REMARK 3 S21: 0.0675 S22: 0.0033 S23: -0.0106
REMARK 3 S31: -0.0039 S32: 0.0211 S33: 0.0138
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 : B 2 B 7
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1137 79.5646 53.6471
REMARK 3 T TENSOR
REMARK 3 T11: 0.0962 T22: 0.1663
REMARK 3 T33: 0.1789 T12: -0.0561
REMARK 3 T13: -0.0213 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 4.7601 L22: 34.4508
REMARK 3 L33: 14.5011 L12: 1.7046
REMARK 3 L13: -0.5347 L23: 9.2526
REMARK 3 S TENSOR
REMARK 3 S11: 0.3461 S12: -0.2374 S13: -0.5345
REMARK 3 S21: 0.8602 S22: -0.1645 S23: 0.7900
REMARK 3 S31: 0.8129 S32: -0.8419 S33: -0.1815
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 8 B 132
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3810 84.7018 51.0160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0461 T22: 0.0585
REMARK 3 T33: 0.0468 T12: 0.0054
REMARK 3 T13: 0.0007 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.7105 L22: 1.0242
REMARK 3 L33: 1.0151 L12: 0.0024
REMARK 3 L13: 0.1006 L23: 0.3305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0167 S12: -0.1043 S13: -0.0200
REMARK 3 S21: 0.0596 S22: 0.0312 S23: 0.0619
REMARK 3 S31: 0.1022 S32: -0.0370 S33: -0.0145
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 133 B 151
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5520 97.9584 35.4923
REMARK 3 T TENSOR
REMARK 3 T11: 0.1151 T22: 0.1731
REMARK 3 T33: 0.1228 T12: -0.0134
REMARK 3 T13: 0.0454 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 4.1575 L22: 0.6620
REMARK 3 L33: 7.0471 L12: -0.2859
REMARK 3 L13: 5.1879 L23: -0.2470
REMARK 3 S TENSOR
REMARK 3 S11: -0.1094 S12: 0.5045 S13: 0.1370
REMARK 3 S21: -0.1798 S22: -0.1121 S23: -0.1717
REMARK 3 S31: -0.1567 S32: 0.5663 S33: 0.2215
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 152 B 248
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7575 95.0352 34.3875
REMARK 3 T TENSOR
REMARK 3 T11: 0.0512 T22: 0.0760
REMARK 3 T33: 0.0505 T12: 0.0062
REMARK 3 T13: -0.0376 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.6861 L22: 0.6842
REMARK 3 L33: 1.0664 L12: 0.1804
REMARK 3 L13: 0.2842 L23: 0.2613
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: 0.0362 S13: 0.0623
REMARK 3 S21: -0.1647 S22: 0.0364 S23: 0.1312
REMARK 3 S31: -0.1235 S32: -0.1469 S33: -0.0055
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 249 B 321
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8330 77.0300 38.7461
REMARK 3 T TENSOR
REMARK 3 T11: 0.0440 T22: 0.0336
REMARK 3 T33: 0.0512 T12: 0.0177
REMARK 3 T13: 0.0016 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.6335 L22: 1.3542
REMARK 3 L33: 1.5976 L12: -0.1736
REMARK 3 L13: 0.0707 L23: -0.3097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: 0.1009 S13: -0.1277
REMARK 3 S21: -0.1169 S22: -0.0015 S23: -0.1163
REMARK 3 S31: 0.1344 S32: 0.0833 S33: -0.0198
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U
REMARK 3 VALUES RESIDUAL ONLY
REMARK 4
REMARK 4 4UHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-15.
REMARK 100 THE PDBE ID CODE IS EBI-60222.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979736
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61576
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 32.80
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.8
REMARK 200 R MERGE (I) : 0.17
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.7
REMARK 200 R MERGE FOR SHELL (I) : 0.83
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 2CJP
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN IN 30 MM TRIS-HCL, PH
REMARK 280 7.4 MIXED 1:1 WITH 0.1 M HEPES PH 7.5, 20 % PEG 10,000.
REMARK 280 THEN SOAKED IN25% (V/V) GLYCEROL, 75 MM HEPES, PH7.68, PEG
REMARK 280 10,000 22.5 % (W/V)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.90000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.89000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.16500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.89000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.90000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.16500
REMARK 290 SMTRY3 4 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 MET A 1
REMARK 465 SER A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 THR B 322
REMARK 465 SER B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS B 326
REMARK 465 HIS B 327
REMARK 465 HIS B 328
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 2140 O HOH A 2141 2.12
REMARK 500 O HOH B 2015 O HOH B 2030 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2004 O HOH A 2194 4465 2.12
REMARK 500 O HOH A 2093 O HOH A 2255 4565 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 306 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 35 -166.11 -118.25
REMARK 500 ASP A 105 -124.89 63.41
REMARK 500 SER A 129 -55.74 77.38
REMARK 500 ALA A 299 -142.18 -106.48
REMARK 500 PHE A 301 58.32 -94.81
REMARK 500 GLU B 35 -166.59 -116.42
REMARK 500 ASP B 105 -129.35 64.09
REMARK 500 SER B 129 -56.98 77.24
REMARK 500 ALA B 299 -144.05 -112.12
REMARK 500 PHE B 301 57.52 -94.37
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 A2005 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH A2065 DISTANCE = 5.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 602
DBREF 4UHB A 3 321 UNP Q41415 Q41415_SOLTU 3 321
DBREF 4UHB B 3 321 UNP Q41415 Q41415_SOLTU 3 321
SEQADV 4UHB MET A 1 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB LYS A 2 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB THR A 322 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB SER A 323 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS A 324 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS A 325 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS A 326 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS A 327 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS A 328 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB LYS A 141 UNP Q41415 VAL 141 ENGINEERED MUTATION
SEQADV 4UHB VAL A 155 UNP Q41415 ILE 155 ENGINEERED MUTATION
SEQADV 4UHB MET B 1 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB LYS B 2 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB THR B 322 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB SER B 323 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS B 324 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS B 325 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS B 326 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS B 327 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB HIS B 328 UNP Q41415 EXPRESSION TAG
SEQADV 4UHB LYS B 141 UNP Q41415 VAL 141 ENGINEERED MUTATION
SEQADV 4UHB VAL B 155 UNP Q41415 ILE 155 ENGINEERED MUTATION
SEQRES 1 A 328 MET LYS LYS ILE GLU HIS LYS MET VAL ALA VAL ASN GLY
SEQRES 2 A 328 LEU ASN MET HIS LEU ALA GLU LEU GLY GLU GLY PRO THR
SEQRES 3 A 328 ILE LEU PHE ILE HIS GLY PHE PRO GLU LEU TRP TYR SER
SEQRES 4 A 328 TRP ARG HIS GLN MET VAL TYR LEU ALA GLU ARG GLY TYR
SEQRES 5 A 328 ARG ALA VAL ALA PRO ASP LEU ARG GLY TYR GLY ASP THR
SEQRES 6 A 328 THR GLY ALA PRO LEU ASN ASP PRO SER LYS PHE SER ILE
SEQRES 7 A 328 LEU HIS LEU VAL GLY ASP VAL VAL ALA LEU LEU GLU ALA
SEQRES 8 A 328 ILE ALA PRO ASN GLU GLU LYS VAL PHE VAL VAL ALA HIS
SEQRES 9 A 328 ASP TRP GLY ALA LEU ILE ALA TRP HIS LEU CYS LEU PHE
SEQRES 10 A 328 ARG PRO ASP LYS VAL LYS ALA LEU VAL ASN LEU SER VAL
SEQRES 11 A 328 HIS PHE SER LYS ARG ASN PRO LYS MET ASN LYS VAL GLU
SEQRES 12 A 328 GLY LEU LYS ALA ILE TYR GLY GLU ASP HIS TYR VAL SER
SEQRES 13 A 328 ARG PHE GLN VAL PRO GLY GLU ILE GLU ALA GLU PHE ALA
SEQRES 14 A 328 PRO ILE GLY ALA LYS SER VAL LEU LYS LYS ILE LEU THR
SEQRES 15 A 328 TYR ARG ASP PRO ALA PRO PHE TYR PHE PRO LYS GLY LYS
SEQRES 16 A 328 GLY LEU GLU ALA ILE PRO ASP ALA PRO VAL ALA LEU SER
SEQRES 17 A 328 SER TRP LEU SER GLU GLU GLU LEU ASP TYR TYR ALA ASN
SEQRES 18 A 328 LYS PHE GLU GLN THR GLY PHE THR GLY ALA VAL ASN TYR
SEQRES 19 A 328 TYR ARG ALA LEU PRO ILE ASN TRP GLU LEU THR ALA PRO
SEQRES 20 A 328 TRP THR GLY ALA GLN VAL LYS VAL PRO THR LYS PHE ILE
SEQRES 21 A 328 VAL GLY GLU PHE ASP LEU VAL TYR HIS ILE PRO GLY ALA
SEQRES 22 A 328 LYS GLU TYR ILE HIS ASN GLY GLY PHE LYS LYS ASP VAL
SEQRES 23 A 328 PRO LEU LEU GLU GLU VAL VAL VAL LEU GLU GLY ALA ALA
SEQRES 24 A 328 HIS PHE VAL SER GLN GLU ARG PRO HIS GLU ILE SER LYS
SEQRES 25 A 328 HIS ILE TYR ASP PHE ILE GLN LYS PHE THR SER HIS HIS
SEQRES 26 A 328 HIS HIS HIS
SEQRES 1 B 328 MET LYS LYS ILE GLU HIS LYS MET VAL ALA VAL ASN GLY
SEQRES 2 B 328 LEU ASN MET HIS LEU ALA GLU LEU GLY GLU GLY PRO THR
SEQRES 3 B 328 ILE LEU PHE ILE HIS GLY PHE PRO GLU LEU TRP TYR SER
SEQRES 4 B 328 TRP ARG HIS GLN MET VAL TYR LEU ALA GLU ARG GLY TYR
SEQRES 5 B 328 ARG ALA VAL ALA PRO ASP LEU ARG GLY TYR GLY ASP THR
SEQRES 6 B 328 THR GLY ALA PRO LEU ASN ASP PRO SER LYS PHE SER ILE
SEQRES 7 B 328 LEU HIS LEU VAL GLY ASP VAL VAL ALA LEU LEU GLU ALA
SEQRES 8 B 328 ILE ALA PRO ASN GLU GLU LYS VAL PHE VAL VAL ALA HIS
SEQRES 9 B 328 ASP TRP GLY ALA LEU ILE ALA TRP HIS LEU CYS LEU PHE
SEQRES 10 B 328 ARG PRO ASP LYS VAL LYS ALA LEU VAL ASN LEU SER VAL
SEQRES 11 B 328 HIS PHE SER LYS ARG ASN PRO LYS MET ASN LYS VAL GLU
SEQRES 12 B 328 GLY LEU LYS ALA ILE TYR GLY GLU ASP HIS TYR VAL SER
SEQRES 13 B 328 ARG PHE GLN VAL PRO GLY GLU ILE GLU ALA GLU PHE ALA
SEQRES 14 B 328 PRO ILE GLY ALA LYS SER VAL LEU LYS LYS ILE LEU THR
SEQRES 15 B 328 TYR ARG ASP PRO ALA PRO PHE TYR PHE PRO LYS GLY LYS
SEQRES 16 B 328 GLY LEU GLU ALA ILE PRO ASP ALA PRO VAL ALA LEU SER
SEQRES 17 B 328 SER TRP LEU SER GLU GLU GLU LEU ASP TYR TYR ALA ASN
SEQRES 18 B 328 LYS PHE GLU GLN THR GLY PHE THR GLY ALA VAL ASN TYR
SEQRES 19 B 328 TYR ARG ALA LEU PRO ILE ASN TRP GLU LEU THR ALA PRO
SEQRES 20 B 328 TRP THR GLY ALA GLN VAL LYS VAL PRO THR LYS PHE ILE
SEQRES 21 B 328 VAL GLY GLU PHE ASP LEU VAL TYR HIS ILE PRO GLY ALA
SEQRES 22 B 328 LYS GLU TYR ILE HIS ASN GLY GLY PHE LYS LYS ASP VAL
SEQRES 23 B 328 PRO LEU LEU GLU GLU VAL VAL VAL LEU GLU GLY ALA ALA
SEQRES 24 B 328 HIS PHE VAL SER GLN GLU ARG PRO HIS GLU ILE SER LYS
SEQRES 25 B 328 HIS ILE TYR ASP PHE ILE GLN LYS PHE THR SER HIS HIS
SEQRES 26 B 328 HIS HIS HIS
HET GOL A 501 6
HET GOL A 502 6
HET GOL A 503 6
HET GOL A 505 6
HET EDO A 601 4
HET GOL B 501 6
HET GOL B 502 6
HET GOL B 503 6
HET GOL B 504 6
HET GOL B 506 6
HET EDO B 602 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EDO 2(C2 H6 O2)
FORMUL 3 GOL 9(C3 H8 O3)
FORMUL 4 HOH *591(H2 O)
HELIX 1 1 LEU A 36 SER A 39 5 4
HELIX 2 2 TRP A 40 GLU A 49 1 10
HELIX 3 3 ASP A 72 PHE A 76 5 5
HELIX 4 4 SER A 77 ALA A 93 1 17
HELIX 5 5 ASP A 105 ARG A 118 1 14
HELIX 6 6 ASN A 140 GLY A 150 1 11
HELIX 7 7 HIS A 153 PHE A 158 1 6
HELIX 8 8 GLY A 162 ALA A 169 1 8
HELIX 9 9 GLY A 172 THR A 182 1 11
HELIX 10 10 PRO A 204 SER A 209 5 6
HELIX 11 11 SER A 212 GLY A 227 1 16
HELIX 12 12 PHE A 228 ALA A 237 1 10
HELIX 13 13 ALA A 237 THR A 245 1 9
HELIX 14 14 ALA A 246 THR A 249 5 4
HELIX 15 15 ASP A 265 ILE A 270 5 6
HELIX 16 16 GLY A 272 ASN A 279 1 8
HELIX 17 17 GLY A 280 VAL A 286 1 7
HELIX 18 18 PHE A 301 ARG A 306 1 6
HELIX 19 19 ARG A 306 GLN A 319 1 14
HELIX 20 20 LYS A 320 THR A 322 5 3
HELIX 21 21 LEU B 36 SER B 39 5 4
HELIX 22 22 TRP B 40 ARG B 50 1 11
HELIX 23 23 ASP B 72 PHE B 76 5 5
HELIX 24 24 SER B 77 ALA B 93 1 17
HELIX 25 25 ASP B 105 ARG B 118 1 14
HELIX 26 26 ASN B 140 GLY B 150 1 11
HELIX 27 27 HIS B 153 PHE B 158 1 6
HELIX 28 28 GLY B 162 ALA B 169 1 8
HELIX 29 29 GLY B 172 THR B 182 1 11
HELIX 30 30 PRO B 204 SER B 209 5 6
HELIX 31 31 SER B 212 GLY B 227 1 16
HELIX 32 32 PHE B 228 ALA B 237 1 10
HELIX 33 33 ALA B 237 THR B 245 1 9
HELIX 34 34 ALA B 246 THR B 249 5 4
HELIX 35 35 ASP B 265 ILE B 270 5 6
HELIX 36 36 GLY B 272 ASN B 279 1 8
HELIX 37 37 GLY B 280 VAL B 286 1 7
HELIX 38 38 PHE B 301 ARG B 306 1 6
HELIX 39 39 ARG B 306 GLN B 319 1 14
SHEET 1 AA 8 GLU A 5 VAL A 11 0
SHEET 2 AA 8 LEU A 14 LEU A 21 -1 O LEU A 14 N VAL A 11
SHEET 3 AA 8 ARG A 53 PRO A 57 -1 O ALA A 54 N LEU A 21
SHEET 4 AA 8 THR A 26 ILE A 30 1 O ILE A 27 N VAL A 55
SHEET 5 AA 8 VAL A 99 HIS A 104 1 O PHE A 100 N LEU A 28
SHEET 6 AA 8 VAL A 122 LEU A 128 1 N LYS A 123 O VAL A 99
SHEET 7 AA 8 THR A 257 GLY A 262 1 O LYS A 258 N ASN A 127
SHEET 8 AA 8 VAL A 293 LEU A 295 1 O VAL A 293 N VAL A 261
SHEET 1 BA 8 GLU B 5 VAL B 11 0
SHEET 2 BA 8 LEU B 14 LEU B 21 -1 O LEU B 14 N VAL B 11
SHEET 3 BA 8 ARG B 53 PRO B 57 -1 O ALA B 54 N LEU B 21
SHEET 4 BA 8 THR B 26 ILE B 30 1 O ILE B 27 N VAL B 55
SHEET 5 BA 8 VAL B 99 HIS B 104 1 O PHE B 100 N LEU B 28
SHEET 6 BA 8 VAL B 122 LEU B 128 1 N LYS B 123 O VAL B 99
SHEET 7 BA 8 THR B 257 GLY B 262 1 O LYS B 258 N ASN B 127
SHEET 8 BA 8 VAL B 293 LEU B 295 1 O VAL B 293 N VAL B 261
CISPEP 1 PHE A 33 PRO A 34 0 -9.51
CISPEP 2 PHE B 33 PRO B 34 0 -13.44
SITE 1 AC1 6 PHE A 33 ASP A 105 TYR A 154 TYR A 235
SITE 2 AC1 6 HIS A 300 GOL A 502
SITE 1 AC2 5 ASP A 105 TRP A 106 TYR A 235 GOL A 501
SITE 2 AC2 5 HOH A2163
SITE 1 AC3 6 ASN A 12 ARG A 60 PRO A 69 HOH A2026
SITE 2 AC3 6 HOH A2028 GLU B 243
SITE 1 AC4 10 LEU A 89 GLU A 90 ALA A 93 PRO A 94
SITE 2 AC4 10 GLU A 96 GLU A 97 LYS A 121 HOH A2112
SITE 3 AC4 10 HOH A2125 HOH A2336
SITE 1 AC5 5 ASP A 64 GLY A 162 TYR A 218 HOH A2188
SITE 2 AC5 5 HOH A2337
SITE 1 AC6 6 PHE B 33 ASP B 105 TYR B 154 TYR B 235
SITE 2 AC6 6 HIS B 300 GOL B 502
SITE 1 AC7 3 ASP B 105 TYR B 235 GOL B 501
SITE 1 AC8 4 THR B 66 GLY B 67 ALA B 68 HOH B2044
SITE 1 AC9 6 HIS B 113 LEU B 116 SER B 133 ARG B 135
SITE 2 AC9 6 TRP B 248 HOH B2203
SITE 1 BC1 8 PRO A 256 HOH A2145 PRO B 25 ARG B 50
SITE 2 BC1 8 GLY B 51 TYR B 52 GLN B 319 HOH B2033
SITE 1 BC2 3 LYS A 283 TYR B 46 ARG B 50
CRYST1 55.800 96.330 121.780 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010381 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008212 0.00000
MTRIX1 1 0.708800 0.654300 -0.263700 -17.52260 1
MTRIX2 1 0.688100 -0.559000 0.462600 103.52810 1
MTRIX3 1 0.155200 -0.509400 -0.846400 85.04300 1
TER 2574 THR A 322
TER 5129 PHE B 321
MASTER 572 0 11 39 16 0 20 9 5780 2 62 52
END |