HEADER TRANSFERASE,TOXIN 20-JAN-04 1S5C
TITLE CHOLERA HOLOTOXIN WITH AN A-SUBUNIT Y30S MUTATION, CRYSTAL FORM 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLERA ENTEROTOXIN, A CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NAD(+)--DIPHTHAMIDE ADP- RIBOSYLTRANSFERASE, CHOLERA
COMPND 5 ENTEROTOXIN A SUBUNIT;
COMPND 6 EC: 2.4.2.36;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CHOLERA ENTEROTOXIN B-SUBUNIT;
COMPND 11 CHAIN: D, E, F, G, H;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 666;
SOURCE 4 GENE: CTXA, TOXA, VC1457;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PEIA154;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 12 ORGANISM_TAXID: 666;
SOURCE 13 GENE: CTXB, TOXB, VC1456;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PEIA154
KEYWDS CHOLERA TOXIN, HEAT-LABILE ENTEROTOXIN, ADP RIBOSE TRANSFERASES, AB5
KEYWDS 2 TOXINS, TRANSFERASE, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.J.O'NEAL,E.I.AMAYA,M.G.JOBLING,R.K.HOLMES,W.G.HOL
REVDAT 5 23-AUG-23 1S5C 1 REMARK
REVDAT 4 27-OCT-21 1S5C 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1S5C 1 VERSN
REVDAT 2 24-FEB-09 1S5C 1 VERSN
REVDAT 1 06-APR-04 1S5C 0
JRNL AUTH C.J.O'NEAL,E.I.AMAYA,M.G.JOBLING,R.K.HOLMES,W.G.HOL
JRNL TITL CRYSTAL STRUCTURES OF AN INTRINSICALLY ACTIVE CHOLERA TOXIN
JRNL TITL 2 MUTANT YIELD INSIGHT INTO THE TOXIN ACTIVATION MECHANISM
JRNL REF BIOCHEMISTRY V. 43 3772 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15049684
JRNL DOI 10.1021/BI0360152
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 22291
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1208
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1568
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5612
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.338
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.248
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.120
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5734 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4973 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7784 ; 1.215 ; 1.928
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11565 ; 0.873 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 722 ; 6.877 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 868 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6470 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1114 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1194 ; 0.176 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5920 ; 0.195 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3308 ; 0.084 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 196 ; 0.209 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.080 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 37 ; 0.102 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 105 ; 0.194 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.245 ; 0.500
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): 3623 ; 0.869 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5812 ; 1.425 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2111 ; 1.365 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1972 ; 2.178 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 1 A 25
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5091 50.1618 37.2870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: 0.0969
REMARK 3 T33: 0.1608 T12: -0.0300
REMARK 3 T13: 0.0729 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 4.8572 L22: 0.9164
REMARK 3 L33: 2.4556 L12: 0.6103
REMARK 3 L13: 1.8334 L23: 0.3966
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: 0.2543 S13: 0.3721
REMARK 3 S21: 0.1112 S22: 0.1517 S23: 0.2376
REMARK 3 S31: -0.1977 S32: 0.3746 S33: -0.1310
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 37 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8786 39.6345 50.2792
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.1825
REMARK 3 T33: 0.0863 T12: 0.0255
REMARK 3 T13: 0.0232 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: -1.2436 L22: 5.8612
REMARK 3 L33: 1.5758 L12: -2.5024
REMARK 3 L13: -2.8294 L23: 2.1392
REMARK 3 S TENSOR
REMARK 3 S11: 0.1862 S12: -0.2391 S13: -0.0347
REMARK 3 S21: 0.2560 S22: -0.1310 S23: -0.0720
REMARK 3 S31: -0.6554 S32: 0.1717 S33: -0.0552
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 51 A 188
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8698 43.4263 39.6357
REMARK 3 T TENSOR
REMARK 3 T11: 0.0604 T22: 0.1180
REMARK 3 T33: 0.1219 T12: 0.0306
REMARK 3 T13: 0.0328 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.1362 L22: 1.0263
REMARK 3 L33: 1.4230 L12: 0.8612
REMARK 3 L13: -0.2638 L23: -0.3808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: 0.0566 S13: 0.1597
REMARK 3 S21: 0.1264 S22: 0.0893 S23: 0.0832
REMARK 3 S31: -0.0657 S32: 0.0127 S33: -0.1355
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 196 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5273 32.5465 32.9032
REMARK 3 T TENSOR
REMARK 3 T11: 0.1212 T22: 0.1840
REMARK 3 T33: 0.0977 T12: 0.0775
REMARK 3 T13: 0.0427 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.9968 L22: 0.1139
REMARK 3 L33: 6.3171 L12: 0.6897
REMARK 3 L13: -2.9042 L23: -0.8784
REMARK 3 S TENSOR
REMARK 3 S11: -0.0264 S12: -0.1093 S13: -0.0958
REMARK 3 S21: -0.0738 S22: 0.0144 S23: 0.0433
REMARK 3 S31: 0.0984 S32: 0.1408 S33: 0.0119
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 : D 1 D 103
REMARK 3 ORIGIN FOR THE GROUP (A): 59.4254 35.6661 28.1031
REMARK 3 T TENSOR
REMARK 3 T11: 0.0663 T22: 0.1164
REMARK 3 T33: 0.1035 T12: 0.0118
REMARK 3 T13: -0.0071 T23: -0.0193
REMARK 3 L TENSOR
REMARK 3 L11: 1.1830 L22: 2.0059
REMARK 3 L33: 1.4382 L12: 0.2152
REMARK 3 L13: 0.9981 L23: -0.7148
REMARK 3 S TENSOR
REMARK 3 S11: -0.0679 S12: -0.0933 S13: 0.0209
REMARK 3 S21: -0.0057 S22: -0.0245 S23: -0.0609
REMARK 3 S31: -0.0015 S32: 0.0700 S33: 0.0924
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 : E 1 E 103
REMARK 3 ORIGIN FOR THE GROUP (A): 47.1596 18.8236 20.8257
REMARK 3 T TENSOR
REMARK 3 T11: 0.1197 T22: 0.0652
REMARK 3 T33: 0.0800 T12: 0.0087
REMARK 3 T13: -0.0260 T23: 0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 2.3064 L22: 1.3011
REMARK 3 L33: 1.7413 L12: 0.5905
REMARK 3 L13: 0.4072 L23: 0.3503
REMARK 3 S TENSOR
REMARK 3 S11: 0.0972 S12: -0.1098 S13: -0.1221
REMARK 3 S21: 0.0019 S22: 0.0245 S23: -0.0479
REMARK 3 S31: 0.1569 S32: 0.0359 S33: -0.1217
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 : F 1 F 103
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6407 26.6190 5.5000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1029 T22: 0.1221
REMARK 3 T33: 0.0608 T12: -0.0295
REMARK 3 T13: 0.0230 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.9827 L22: 2.4017
REMARK 3 L33: 0.5315 L12: -0.4141
REMARK 3 L13: 0.3851 L23: -0.1412
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.0239 S13: 0.0718
REMARK 3 S21: -0.1097 S22: -0.0126 S23: 0.0797
REMARK 3 S31: 0.1098 S32: -0.0163 S33: 0.0084
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 : G 1 G 103
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0236 47.9032 2.7548
REMARK 3 T TENSOR
REMARK 3 T11: 0.0649 T22: 0.1024
REMARK 3 T33: 0.0643 T12: 0.0002
REMARK 3 T13: 0.0612 T23: 0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 1.5219 L22: 3.4372
REMARK 3 L33: 1.3745 L12: -0.0378
REMARK 3 L13: 0.5392 L23: 0.2297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0516 S12: 0.0198 S13: -0.0276
REMARK 3 S21: -0.1078 S22: 0.0344 S23: -0.1904
REMARK 3 S31: -0.0884 S32: -0.0559 S33: 0.0172
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 : H 1 H 103
REMARK 3 ORIGIN FOR THE GROUP (A): 54.2276 53.2305 16.3289
REMARK 3 T TENSOR
REMARK 3 T11: 0.0908 T22: 0.0121
REMARK 3 T33: 0.1620 T12: -0.0309
REMARK 3 T13: -0.0834 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 2.2106 L22: 2.0199
REMARK 3 L33: 2.6727 L12: -0.6682
REMARK 3 L13: 0.9446 L23: -0.2388
REMARK 3 S TENSOR
REMARK 3 S11: -0.2392 S12: 0.1098 S13: 0.2217
REMARK 3 S21: 0.1905 S22: 0.0063 S23: -0.3428
REMARK 3 S31: -0.2903 S32: 0.0278 S33: 0.2329
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1S5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0414
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23503
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 19.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRIES 1LTG, 3CHB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 2000MME, MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 42.59950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, F, G, H
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 GLY A 26
REMARK 465 GLN A 27
REMARK 465 SER A 28
REMARK 465 GLU A 29
REMARK 465 SER A 30
REMARK 465 PHE A 31
REMARK 465 ASP A 32
REMARK 465 ARG A 33
REMARK 465 GLY A 34
REMARK 465 THR A 35
REMARK 465 GLN A 36
REMARK 465 THR A 50
REMARK 465 ALA A 190
REMARK 465 PRO A 191
REMARK 465 ARG A 192
REMARK 465 SER A 193
REMARK 465 SER A 194
REMARK 465 MET A 195
REMARK 465 ARG A 235
REMARK 465 ILE A 236
REMARK 465 LYS A 237
REMARK 465 ASP A 238
REMARK 465 GLU A 239
REMARK 465 LEU A 240
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 17 CG CD CE NZ
REMARK 470 PHE A 52 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 67 CB CG CD NE CZ NH1 NH2
REMARK 470 GLN A 74 CD OE1 NE2
REMARK 470 ILE A 76 CD1
REMARK 470 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 134 CB CG1 CG2
REMARK 470 ASP A 136 CB CG OD1 OD2
REMARK 470 GLU A 137 CB CG CD OE1 OE2
REMARK 470 ARG A 141 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 143 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 175 CB CG CD NE CZ NH1 NH2
REMARK 470 ASN A 189 CB CG OD1 ND2
REMARK 470 GLU A 201 CG CD OE1 OE2
REMARK 470 LYS A 202 CD CE NZ
REMARK 470 LYS A 217 CD CE NZ
REMARK 470 LYS A 219 CE NZ
REMARK 470 ASN A 234 CB CG OD1 ND2
REMARK 470 LYS D 34 CD CE NZ
REMARK 470 SER D 55 CB OG
REMARK 470 GLN D 56 CB CG CD OE1 NE2
REMARK 470 ILE D 58 CB CG1 CG2 CD1
REMARK 470 ASP D 59 CB CG OD1 OD2
REMARK 470 LYS D 62 CD CE NZ
REMARK 470 LYS D 63 CG CD CE NZ
REMARK 470 LYS D 81 CE NZ
REMARK 470 ASN D 103 CB CG OD1 ND2
REMARK 470 LYS E 34 CE NZ
REMARK 470 LYS E 43 CD CE NZ
REMARK 470 LYS E 62 CB CG CD CE NZ
REMARK 470 LYS E 63 CG CD CE NZ
REMARK 470 LYS E 81 CD CE NZ
REMARK 470 ASN F 103 CB CG OD1 ND2
REMARK 470 LYS G 43 CG CD CE NZ
REMARK 470 LYS G 62 CG CD CE NZ
REMARK 470 LYS G 63 CG CD CE NZ
REMARK 470 LYS G 81 CD CE NZ
REMARK 470 ASN G 103 CB CG OD1 ND2
REMARK 470 HIS H 13 CB CG ND1 CD2 CE1 NE2
REMARK 470 GLN H 16 CB CG CD OE1 NE2
REMARK 470 LYS H 34 CD CE NZ
REMARK 470 LYS H 43 CG CD CE NZ
REMARK 470 ALA H 46 CB
REMARK 470 LYS H 63 CG CD CE NZ
REMARK 470 LYS H 81 CD CE NZ
REMARK 470 LYS H 84 CG CD CE NZ
REMARK 470 LYS H 91 CB CG CD CE NZ
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 OG SER A 216 OE1 GLU E 79 2.18
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 ASP A 43 CB - CG - OD2 ANGL. DEV. = 5.4 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 ASN A 40 116.74 -160.60
REMARK 500 ARG A 54 106.62 -20.64
REMARK 500 HIS A 55 25.00 -144.47
REMARK 500 LEU A 77 31.01 -86.79
REMARK 500 PRO A 120 156.52 -49.16
REMARK 500 ASN D 44 5.13 -67.87
REMARK 500 PRO D 53 104.22 -50.94
REMARK 500 ILE D 58 -130.30 -80.49
REMARK 500 ASN F 21 56.53 33.42
REMARK 500 ASN G 21 49.58 37.38
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 NA A 241 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 1 O
REMARK 620 2 THR A 90 OG1 103.5
REMARK 620 3 THR A 90 O 159.7 66.6
REMARK 620 4 TYR A 150 O 100.6 152.0 86.0
REMARK 620 5 LEU A 153 O 76.8 88.9 85.1 82.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 241
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XTC RELATED DB: PDB
REMARK 900 CHOLERA HOLOTOXIN
REMARK 900 RELATED ID: 1LTS RELATED DB: PDB
REMARK 900 HEAT-LABILE ENTEROTOXIN
REMARK 900 RELATED ID: 1LTG RELATED DB: PDB
REMARK 900 HEAT-LABILE ENTEROTOXIN WITH AN A-SUBUNIT R7K MUTATION
REMARK 900 RELATED ID: 1LTA RELATED DB: PDB
REMARK 900 HEAT-LABILE ENTEROTOXIN COMPLEXED WITH GALACTOSE
DBREF 1S5C A 1 240 UNP P01555 CHTA_VIBCH 19 258
DBREF 1S5C D 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1S5C E 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1S5C F 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1S5C G 1 103 UNP P01556 CHTB_VIBCH 22 124
DBREF 1S5C H 1 103 UNP P01556 CHTB_VIBCH 22 124
SEQADV 1S5C SER A 30 UNP P01555 TYR 30 ENGINEERED MUTATION
SEQRES 1 A 240 ASN ASP ASP LYS LEU TYR ARG ALA ASP SER ARG PRO PRO
SEQRES 2 A 240 ASP GLU ILE LYS GLN SER GLY GLY LEU MET PRO ARG GLY
SEQRES 3 A 240 GLN SER GLU SER PHE ASP ARG GLY THR GLN MET ASN ILE
SEQRES 4 A 240 ASN LEU TYR ASP HIS ALA ARG GLY THR GLN THR GLY PHE
SEQRES 5 A 240 VAL ARG HIS ASP ASP GLY TYR VAL SER THR SER ILE SER
SEQRES 6 A 240 LEU ARG SER ALA HIS LEU VAL GLY GLN THR ILE LEU SER
SEQRES 7 A 240 GLY HIS SER THR TYR TYR ILE TYR VAL ILE ALA THR ALA
SEQRES 8 A 240 PRO ASN MET PHE ASN VAL ASN ASP VAL LEU GLY ALA TYR
SEQRES 9 A 240 SER PRO HIS PRO ASP GLU GLN GLU VAL SER ALA LEU GLY
SEQRES 10 A 240 GLY ILE PRO TYR SER GLN ILE TYR GLY TRP TYR ARG VAL
SEQRES 11 A 240 HIS PHE GLY VAL LEU ASP GLU GLN LEU HIS ARG ASN ARG
SEQRES 12 A 240 GLY TYR ARG ASP ARG TYR TYR SER ASN LEU ASP ILE ALA
SEQRES 13 A 240 PRO ALA ALA ASP GLY TYR GLY LEU ALA GLY PHE PRO PRO
SEQRES 14 A 240 GLU HIS ARG ALA TRP ARG GLU GLU PRO TRP ILE HIS HIS
SEQRES 15 A 240 ALA PRO PRO GLY CYS GLY ASN ALA PRO ARG SER SER MET
SEQRES 16 A 240 SER ASN THR CYS ASP GLU LYS THR GLN SER LEU GLY VAL
SEQRES 17 A 240 LYS PHE LEU ASP GLU TYR GLN SER LYS VAL LYS ARG GLN
SEQRES 18 A 240 ILE PHE SER GLY TYR GLN SER ASP ILE ASP THR HIS ASN
SEQRES 19 A 240 ARG ILE LYS ASP GLU LEU
SEQRES 1 D 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 D 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 D 103 TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE
SEQRES 4 D 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 D 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 D 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 D 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 D 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 E 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 E 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 E 103 TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE
SEQRES 4 E 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 E 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 E 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 E 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 E 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 F 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 F 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 F 103 TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE
SEQRES 4 F 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 F 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 F 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 F 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 F 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 G 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 G 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 G 103 TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE
SEQRES 4 G 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 G 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 G 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 G 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 G 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
SEQRES 1 H 103 THR PRO GLN ASN ILE THR ASP LEU CYS ALA GLU TYR HIS
SEQRES 2 H 103 ASN THR GLN ILE HIS THR LEU ASN ASP LYS ILE PHE SER
SEQRES 3 H 103 TYR THR GLU SER LEU ALA GLY LYS ARG GLU MET ALA ILE
SEQRES 4 H 103 ILE THR PHE LYS ASN GLY ALA THR PHE GLN VAL GLU VAL
SEQRES 5 H 103 PRO GLY SER GLN HIS ILE ASP SER GLN LYS LYS ALA ILE
SEQRES 6 H 103 GLU ARG MET LYS ASP THR LEU ARG ILE ALA TYR LEU THR
SEQRES 7 H 103 GLU ALA LYS VAL GLU LYS LEU CYS VAL TRP ASN ASN LYS
SEQRES 8 H 103 THR PRO HIS ALA ILE ALA ALA ILE SER MET ALA ASN
HET NA A 241 1
HETNAM NA SODIUM ION
FORMUL 7 NA NA 1+
FORMUL 8 HOH *94(H2 O)
HELIX 1 1 PRO A 12 GLY A 20 1 9
HELIX 2 2 ASN A 40 GLY A 47 1 8
HELIX 3 3 SER A 65 LEU A 77 1 13
HELIX 4 4 VAL A 97 GLY A 102 1 6
HELIX 5 5 ALA A 103 SER A 105 5 3
HELIX 6 6 HIS A 107 GLU A 110 5 4
HELIX 7 7 ARG A 146 ASN A 152 1 7
HELIX 8 8 PRO A 157 GLY A 163 1 7
HELIX 9 9 HIS A 171 GLU A 176 5 6
HELIX 10 10 PRO A 178 ALA A 183 5 6
HELIX 11 11 ASN A 197 GLN A 227 1 31
HELIX 12 12 ASN D 4 GLU D 11 1 8
HELIX 13 13 ASP D 59 GLU D 79 1 21
HELIX 14 14 ASN E 4 ALA E 10 1 7
HELIX 15 15 SER E 60 GLU E 79 1 20
HELIX 16 16 ASN F 4 ALA F 10 1 7
HELIX 17 17 ILE F 58 GLU F 79 1 22
HELIX 18 18 ASN G 4 ALA G 10 1 7
HELIX 19 19 ILE G 58 THR G 78 1 21
HELIX 20 20 ASN H 4 ALA H 10 1 7
HELIX 21 21 GLN H 61 GLU H 79 1 19
SHEET 1 A 4 LYS A 4 ASP A 9 0
SHEET 2 A 4 THR A 82 ALA A 89 -1 O ILE A 88 N LEU A 5
SHEET 3 A 4 ILE A 124 HIS A 131 -1 O GLY A 126 N VAL A 87
SHEET 4 A 4 VAL A 134 LEU A 135 -1 O VAL A 134 N HIS A 131
SHEET 1 B 4 LYS A 4 ASP A 9 0
SHEET 2 B 4 THR A 82 ALA A 89 -1 O ILE A 88 N LEU A 5
SHEET 3 B 4 ILE A 124 HIS A 131 -1 O GLY A 126 N VAL A 87
SHEET 4 B 4 HIS A 140 ARG A 141 -1 O HIS A 140 N TRP A 127
SHEET 1 C 2 GLY A 21 LEU A 22 0
SHEET 2 C 2 ILE A 119 PRO A 120 -1 O ILE A 119 N LEU A 22
SHEET 1 D 3 TYR A 59 SER A 63 0
SHEET 2 D 3 GLU A 112 LEU A 116 -1 O ALA A 115 N VAL A 60
SHEET 3 D 3 MET A 94 ASN A 96 -1 N PHE A 95 O SER A 114
SHEET 1 E14 THR F 15 ASP F 22 0
SHEET 2 E14 VAL F 82 TRP F 88 -1 O LEU F 85 N HIS F 18
SHEET 3 E14 HIS F 94 ALA F 102 -1 O ALA F 97 N CYS F 86
SHEET 4 E14 SER D 26 SER D 30 -1 N TYR D 27 O MET F 101
SHEET 5 E14 MET D 37 THR D 41 -1 O ILE D 39 N THR D 28
SHEET 6 E14 PHE D 48 VAL D 50 -1 O PHE D 48 N ILE D 40
SHEET 7 E14 HIS D 94 ALA D 102 1 O ILE D 96 N GLN D 49
SHEET 8 E14 VAL D 82 TRP D 88 -1 N TRP D 88 O ALA D 95
SHEET 9 E14 THR D 15 ASP D 22 -1 N GLN D 16 O VAL D 87
SHEET 10 E14 VAL D 82 TRP D 88 -1 O VAL D 87 N GLN D 16
SHEET 11 E14 HIS D 94 ALA D 102 -1 O ALA D 95 N TRP D 88
SHEET 12 E14 SER E 26 SER E 30 -1 O GLU E 29 N ILE D 99
SHEET 13 E14 MET E 37 THR E 41 -1 O ILE E 39 N THR E 28
SHEET 14 E14 THR E 47 VAL E 50 -1 O PHE E 48 N ILE E 40
SHEET 1 F11 HIS E 94 ALA E 102 0
SHEET 2 F11 VAL E 82 TRP E 88 -1 N TRP E 88 O ALA E 95
SHEET 3 F11 THR E 15 ASP E 22 -1 N HIS E 18 O LEU E 85
SHEET 4 F11 VAL E 82 TRP E 88 -1 O LEU E 85 N HIS E 18
SHEET 5 F11 HIS E 94 ALA E 102 -1 O ALA E 95 N TRP E 88
SHEET 6 F11 SER D 26 SER D 30 -1 O GLU D 29 N ILE E 99
SHEET 7 F11 ALA D 38 THR D 41 -1 O ILE D 39 N THR D 28
SHEET 8 F11 THR D 47 VAL D 50 -1 O PHE D 48 N ILE D 40
SHEET 9 F11 HIS D 94 ALA D 102 1 O ILE D 96 N GLN D 49
SHEET 10 F11 VAL D 82 TRP D 88 -1 N TRP D 88 O ALA D 95
SHEET 11 F11 THR D 15 ASP D 22 -1 N HIS D 18 O LEU D 85
SHEET 1 G11 VAL D 82 TRP D 88 0
SHEET 2 G11 HIS D 94 ALA D 102 -1 O ALA D 95 N TRP D 88
SHEET 3 G11 SER E 26 SER E 30 -1 O TYR E 27 N MET D 101
SHEET 4 G11 MET E 37 THR E 41 -1 O ILE E 39 N THR E 28
SHEET 5 G11 THR E 47 VAL E 50 -1 O PHE E 48 N ILE E 40
SHEET 6 G11 HIS E 94 ALA E 102 1 O ILE E 96 N GLN E 49
SHEET 7 G11 LYS E 81 TRP E 88 -1 N CYS E 86 O ALA E 97
SHEET 8 G11 THR E 15 LYS E 23 -1 N LEU E 20 O GLU E 83
SHEET 9 G11 LYS E 81 TRP E 88 -1 O GLU E 83 N LEU E 20
SHEET 10 G11 HIS E 94 ALA E 102 -1 O ALA E 97 N CYS E 86
SHEET 11 G11 SER F 26 SER F 30 -1 O TYR F 27 N MET E 101
SHEET 1 H 3 ALA F 38 THR F 41 0
SHEET 2 H 3 THR F 47 VAL F 50 -1 O PHE F 48 N ILE F 40
SHEET 3 H 3 HIS F 94 ALA F 102 1 O ILE F 96 N GLN F 49
SSBOND 1 CYS A 187 CYS A 199 1555 1555 2.03
SSBOND 2 CYS D 9 CYS D 86 1555 1555 2.02
SSBOND 3 CYS E 9 CYS E 86 1555 1555 2.03
SSBOND 4 CYS F 9 CYS F 86 1555 1555 2.04
SSBOND 5 CYS G 9 CYS G 86 1555 1555 2.03
SSBOND 6 CYS H 9 CYS H 86 1555 1555 2.05
LINK O ASN A 1 NA NA A 241 1555 1555 2.32
LINK OG1 THR A 90 NA NA A 241 1555 1555 2.57
LINK O THR A 90 NA NA A 241 1555 1555 2.66
LINK O TYR A 150 NA NA A 241 1555 1555 2.35
LINK O LEU A 153 NA NA A 241 1555 1555 2.62
CISPEP 1 GLU A 177 PRO A 178 0 4.79
CISPEP 2 THR D 92 PRO D 93 0 3.81
CISPEP 3 THR E 92 PRO E 93 0 -5.24
CISPEP 4 THR F 92 PRO F 93 0 -0.79
CISPEP 5 THR G 92 PRO G 93 0 -2.02
CISPEP 6 THR H 92 PRO H 93 0 -1.34
SITE 1 AC1 4 ASN A 1 THR A 90 TYR A 150 LEU A 153
CRYST1 58.818 85.199 71.255 90.00 104.48 90.00 P 1 21 1 10
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 0.017002 0.000000 0.004391 0.00000
SCALE2 0.000000 0.011737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014495 0.00000
(ATOM LINES ARE NOT SHOWN.)
END