HEADER ISOMERASE 25-JUL-13 4BZE
TITLE CRYSTAL STRUCTURE OF GALACTOSE MUTAROTASE GALM FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE 1-EPIMERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GALACTOSE MUTAROTASE;
COMPND 5 EC: 5.1.3.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 GENE: GALM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KRX;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET20B
KEYWDS ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VANDEN BROECK,E.SAUVAGE,R.HERMAN,F.KERFF,C.DUEZ,P.CHARLIER
REVDAT 3 20-DEC-23 4BZE 1 REMARK
REVDAT 2 13-SEP-17 4BZE 1 REMARK
REVDAT 1 13-AUG-14 4BZE 0
JRNL AUTH A.VANDEN BROECK,E.SAUVAGE,R.HERMAN,F.KERFF,C.DUEZ,P.CHARLIER
JRNL TITL CRYSTAL STRUCTURE OF GALACTOSE MUTAROTASE GALM FROM BACILLUS
JRNL TITL 2 SUBTILIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 54861
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2932
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3714
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 214
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 312
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.13000
REMARK 3 B33 (A**2) : 0.16000
REMARK 3 B12 (A**2) : 0.00000
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): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.629
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5388 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7333 ; 1.477 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 643 ; 6.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 263 ;41.601 ;24.791
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 891 ;13.599 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;21.215 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 803 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4128 ; 0.007 ; 0.021
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 53
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4547 20.6277 -17.4057
REMARK 3 T TENSOR
REMARK 3 T11: 0.0909 T22: 0.0944
REMARK 3 T33: 0.2067 T12: 0.0124
REMARK 3 T13: 0.0435 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.3047 L22: 1.4852
REMARK 3 L33: 1.4431 L12: -0.4331
REMARK 3 L13: -0.2742 L23: -0.3034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0559 S12: -0.0574 S13: -0.0475
REMARK 3 S21: -0.1360 S22: -0.0722 S23: -0.2187
REMARK 3 S31: -0.0974 S32: 0.2237 S33: 0.0163
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 54 A 126
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2106 9.8923 -11.4937
REMARK 3 T TENSOR
REMARK 3 T11: 0.1133 T22: 0.0392
REMARK 3 T33: 0.1775 T12: 0.0259
REMARK 3 T13: 0.0069 T23: -0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 0.8948 L22: 0.6936
REMARK 3 L33: 0.7592 L12: 0.4281
REMARK 3 L13: -0.4961 L23: -0.3918
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: 0.0509 S13: -0.1135
REMARK 3 S21: -0.0574 S22: -0.0220 S23: -0.0360
REMARK 3 S31: 0.0843 S32: 0.0280 S33: -0.0312
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 127 A 219
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6996 17.9425 -7.2484
REMARK 3 T TENSOR
REMARK 3 T11: 0.0915 T22: 0.0543
REMARK 3 T33: 0.1489 T12: 0.0084
REMARK 3 T13: 0.0023 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.6693 L22: 0.8482
REMARK 3 L33: 0.3951 L12: 0.0796
REMARK 3 L13: 0.0252 L23: 0.1901
REMARK 3 S TENSOR
REMARK 3 S11: 0.0157 S12: 0.0115 S13: -0.0035
REMARK 3 S21: -0.0278 S22: -0.0117 S23: 0.0135
REMARK 3 S31: 0.0129 S32: 0.0213 S33: -0.0039
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 220 A 240
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7453 26.3158 5.5208
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: 0.0728
REMARK 3 T33: 0.1260 T12: -0.0199
REMARK 3 T13: 0.0144 T23: 0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 3.3922 L22: 1.5574
REMARK 3 L33: 0.4829 L12: -0.6369
REMARK 3 L13: -0.2423 L23: 0.2245
REMARK 3 S TENSOR
REMARK 3 S11: 0.1407 S12: -0.1962 S13: 0.1207
REMARK 3 S21: 0.1509 S22: -0.1489 S23: 0.0093
REMARK 3 S31: 0.0788 S32: 0.0454 S33: 0.0082
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 241 A 317
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1759 22.4923 -4.8764
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.0589
REMARK 3 T33: 0.1732 T12: 0.0059
REMARK 3 T13: -0.0016 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.6768 L22: 0.4990
REMARK 3 L33: 0.1967 L12: 0.0995
REMARK 3 L13: -0.3049 L23: 0.1021
REMARK 3 S TENSOR
REMARK 3 S11: 0.0355 S12: -0.0082 S13: 0.0317
REMARK 3 S21: 0.0071 S22: -0.0327 S23: -0.0006
REMARK 3 S31: 0.0156 S32: 0.0131 S33: -0.0027
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 318 A 323
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4721 35.0568 -9.4511
REMARK 3 T TENSOR
REMARK 3 T11: 0.1899 T22: 0.0469
REMARK 3 T33: 0.1914 T12: 0.0332
REMARK 3 T13: 0.0576 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 6.5578 L22: 13.8433
REMARK 3 L33: 3.7950 L12: 7.1080
REMARK 3 L13: 3.1811 L23: 4.5528
REMARK 3 S TENSOR
REMARK 3 S11: 0.0357 S12: -0.1581 S13: 0.1814
REMARK 3 S21: 0.2365 S22: 0.2504 S23: -0.1510
REMARK 3 S31: -0.5185 S32: -0.0440 S33: -0.2862
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 63
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8654 20.1998 -46.0368
REMARK 3 T TENSOR
REMARK 3 T11: 0.1895 T22: 0.1275
REMARK 3 T33: 0.1309 T12: -0.0309
REMARK 3 T13: 0.0731 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 0.0810 L22: 1.9979
REMARK 3 L33: 2.9973 L12: 0.2718
REMARK 3 L13: 0.3278 L23: 0.5147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0278 S12: -0.0029 S13: -0.0141
REMARK 3 S21: -0.1201 S22: -0.0257 S23: 0.1915
REMARK 3 S31: 0.0684 S32: -0.3549 S33: 0.0535
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 64 B 105
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3031 6.8167 -53.7663
REMARK 3 T TENSOR
REMARK 3 T11: 0.3899 T22: 0.0907
REMARK 3 T33: 0.1564 T12: 0.0621
REMARK 3 T13: 0.1231 T23: -0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 1.8535 L22: 0.5379
REMARK 3 L33: 0.9544 L12: 0.5874
REMARK 3 L13: -1.3256 L23: -0.4040
REMARK 3 S TENSOR
REMARK 3 S11: -0.2328 S12: -0.1186 S13: -0.2507
REMARK 3 S21: -0.3206 S22: 0.0142 S23: -0.1639
REMARK 3 S31: 0.1684 S32: 0.0679 S33: 0.2186
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 106 B 122
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1126 22.2414 -36.4195
REMARK 3 T TENSOR
REMARK 3 T11: 0.1836 T22: 0.0804
REMARK 3 T33: 0.1311 T12: -0.0159
REMARK 3 T13: 0.0866 T23: 0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 1.2635 L22: 1.8640
REMARK 3 L33: 4.5788 L12: -1.5095
REMARK 3 L13: -1.4801 L23: 1.3788
REMARK 3 S TENSOR
REMARK 3 S11: -0.0872 S12: -0.1319 S13: 0.0536
REMARK 3 S21: 0.0661 S22: 0.1334 S23: -0.0928
REMARK 3 S31: -0.0190 S32: 0.2082 S33: -0.0462
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 123 B 221
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0356 19.1596 -53.3351
REMARK 3 T TENSOR
REMARK 3 T11: 0.2457 T22: 0.0709
REMARK 3 T33: 0.0765 T12: 0.0114
REMARK 3 T13: 0.1073 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.9826 L22: 1.1166
REMARK 3 L33: 0.7149 L12: -0.3515
REMARK 3 L13: -0.1562 L23: -0.3174
REMARK 3 S TENSOR
REMARK 3 S11: -0.0649 S12: 0.0344 S13: 0.0528
REMARK 3 S21: -0.1562 S22: 0.0084 S23: -0.1259
REMARK 3 S31: 0.1555 S32: 0.0747 S33: 0.0565
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 222 B 271
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0114 27.5674 -62.0104
REMARK 3 T TENSOR
REMARK 3 T11: 0.3528 T22: 0.1532
REMARK 3 T33: 0.2405 T12: 0.0264
REMARK 3 T13: 0.1052 T23: 0.0704
REMARK 3 L TENSOR
REMARK 3 L11: 1.7233 L22: 0.7280
REMARK 3 L33: 0.6619 L12: 0.4701
REMARK 3 L13: -0.7571 L23: -0.6171
REMARK 3 S TENSOR
REMARK 3 S11: -0.1200 S12: 0.2136 S13: 0.2773
REMARK 3 S21: -0.3931 S22: -0.0281 S23: -0.2375
REMARK 3 S31: 0.2327 S32: -0.0468 S33: 0.1480
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 272 B 324
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3974 21.0921 -55.1818
REMARK 3 T TENSOR
REMARK 3 T11: 0.2533 T22: 0.0886
REMARK 3 T33: 0.1657 T12: 0.0203
REMARK 3 T13: 0.1105 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.9209 L22: 0.8655
REMARK 3 L33: 0.8365 L12: -0.3291
REMARK 3 L13: -0.7215 L23: 0.2201
REMARK 3 S TENSOR
REMARK 3 S11: -0.0668 S12: -0.0428 S13: 0.1584
REMARK 3 S21: -0.3624 S22: 0.0364 S23: -0.2579
REMARK 3 S31: 0.0812 S32: -0.0331 S33: 0.0304
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 RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4BZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1290057808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-12
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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98011
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 42.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.20
REMARK 200 R MERGE FOR SHELL (I) : 0.97000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3MWX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 41.17000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.45300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.17000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.45300
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2107 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2217 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2008 LIES ON A SPECIAL POSITION.
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 HIS A 324
REMARK 465 GLN A 325
REMARK 465 MET B 1
REMARK 465 GLN B 325
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 OE1 GLU A 185 O HOH A 2055 4555 1.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 97 CG HIS A 97 CD2 0.057
REMARK 500 HIS A 106 CG HIS A 106 CD2 0.060
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 20 -155.08 -131.13
REMARK 500 TRP A 31 57.79 -95.08
REMARK 500 ASN A 73 -151.13 68.82
REMARK 500 HIS A 101 5.08 81.41
REMARK 500 GLU A 153 -118.05 47.00
REMARK 500 HIS A 177 32.78 -96.59
REMARK 500 TYR A 214 30.01 -93.00
REMARK 500 HIS A 226 -9.91 72.28
REMARK 500 ALA A 273 -125.27 52.99
REMARK 500 ASN B 20 -156.74 -140.37
REMARK 500 TRP B 31 54.14 -98.56
REMARK 500 ASN B 73 -153.33 61.41
REMARK 500 HIS B 101 6.78 80.57
REMARK 500 GLU B 153 -127.14 50.71
REMARK 500 HIS B 177 37.07 -89.46
REMARK 500 HIS B 226 -42.63 76.56
REMARK 500 ASP B 230 55.01 -151.60
REMARK 500 ALA B 273 -119.19 61.19
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 A2219 DISTANCE = 7.61 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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BZF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GALACTOSE MUTAROTASE GALM FROM BACILLUS
REMARK 900 SUBTILIS WITH TREHALOSE
REMARK 900 RELATED ID: 4BZG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GALACTOSE MUTAROTASE GALM FROM BACILLUS
REMARK 900 SUBTILIS IN COMPLEX WITH MALTOSE
REMARK 900 RELATED ID: 4BZH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GALACTOSE MUTAROTASE GALM FROM BACILLUS
REMARK 900 SUBTILIS IN COMPLEX WITH MALTOSE AND TREHALOSE
DBREF 4BZE A 1 325 UNP P39840 GALM_BACSU 1 325
DBREF 4BZE B 1 325 UNP P39840 GALM_BACSU 1 325
SEQRES 1 A 325 MET ALA ASN PHE ILE GLU LYS ILE THR TYR LEU GLY THR
SEQRES 2 A 325 PRO ALA ILE LYS ALA GLY ASN GLU HIS LEU GLU MET ILE
SEQRES 3 A 325 VAL VAL PRO GLU TRP GLY SER ASN VAL ILE SER LEU VAL
SEQRES 4 A 325 ASP LYS THR THR ASN VAL GLN LEU LEU ARG GLU PRO GLU
SEQRES 5 A 325 THR ALA GLU SER PHE HIS ASP THR PRO THR LEU TYR GLY
SEQRES 6 A 325 ILE PRO ILE LEU PHE PRO PRO ASN ARG ILE SER ASP GLY
SEQRES 7 A 325 THR PHE SER PHE ARG GLY ARG THR TYR HIS PHE ASP ILE
SEQRES 8 A 325 ASN GLU LYS ASP LYS HIS ASN HIS LEU HIS GLY PHE LEU
SEQRES 9 A 325 TYR HIS GLU LYS TRP ASN VAL VAL THR THR LYS GLN THR
SEQRES 10 A 325 ASP GLU GLY VAL ILE VAL GLU THR GLU ILE ASP LEU SER
SEQRES 11 A 325 GLU LEU PRO HIS VAL GLN LYS GLN PHE PRO HIS HIS ALA
SEQRES 12 A 325 VAL VAL ARG MET THR TYR THR ILE LYS GLU ASN THR LEU
SEQRES 13 A 325 PHE LYS HIS ALA THR VAL MET ASN LYS GLY LYS GLU ALA
SEQRES 14 A 325 PHE PRO TRP GLY ILE GLY TYR HIS THR THR PHE ILE PHE
SEQRES 15 A 325 PRO ALA GLU SER SER LEU PHE SER LEU THR ALA ASP GLN
SEQRES 16 A 325 GLN TRP GLU LEU ASP GLU ARG LEU LEU PRO THR GLY LYS
SEQRES 17 A 325 LEU MET ASP VAL PRO TYR LYS GLU ALA LEU HIS GLU GLY
SEQRES 18 A 325 MET ASP LEU ARG HIS LYS GLN LEU ASP ASP VAL PHE LEU
SEQRES 19 A 325 SER SER TYR GLN LYS ARG GLY GLY GLU ASN GLN ALA VAL
SEQRES 20 A 325 ILE TYR HIS GLN HIS ALA HIS ILE SER ILE ILE TYR LYS
SEQRES 21 A 325 ALA ASP GLU GLN PHE LYS HIS TRP VAL VAL TYR ASN ALA
SEQRES 22 A 325 ASP GLY LYS GLN GLY TYR LEU CYS PRO GLU PRO TYR THR
SEQRES 23 A 325 TRP VAL THR ASN ALA VAL ASN LEU ASP LEU PRO SER SER
SEQRES 24 A 325 LEU THR GLY LEU GLN VAL LEU GLU PRO GLY GLU GLU THR
SEQRES 25 A 325 THR ALA LYS SER SER ILE THR ILE GLU LEU ASN HIS GLN
SEQRES 1 B 325 MET ALA ASN PHE ILE GLU LYS ILE THR TYR LEU GLY THR
SEQRES 2 B 325 PRO ALA ILE LYS ALA GLY ASN GLU HIS LEU GLU MET ILE
SEQRES 3 B 325 VAL VAL PRO GLU TRP GLY SER ASN VAL ILE SER LEU VAL
SEQRES 4 B 325 ASP LYS THR THR ASN VAL GLN LEU LEU ARG GLU PRO GLU
SEQRES 5 B 325 THR ALA GLU SER PHE HIS ASP THR PRO THR LEU TYR GLY
SEQRES 6 B 325 ILE PRO ILE LEU PHE PRO PRO ASN ARG ILE SER ASP GLY
SEQRES 7 B 325 THR PHE SER PHE ARG GLY ARG THR TYR HIS PHE ASP ILE
SEQRES 8 B 325 ASN GLU LYS ASP LYS HIS ASN HIS LEU HIS GLY PHE LEU
SEQRES 9 B 325 TYR HIS GLU LYS TRP ASN VAL VAL THR THR LYS GLN THR
SEQRES 10 B 325 ASP GLU GLY VAL ILE VAL GLU THR GLU ILE ASP LEU SER
SEQRES 11 B 325 GLU LEU PRO HIS VAL GLN LYS GLN PHE PRO HIS HIS ALA
SEQRES 12 B 325 VAL VAL ARG MET THR TYR THR ILE LYS GLU ASN THR LEU
SEQRES 13 B 325 PHE LYS HIS ALA THR VAL MET ASN LYS GLY LYS GLU ALA
SEQRES 14 B 325 PHE PRO TRP GLY ILE GLY TYR HIS THR THR PHE ILE PHE
SEQRES 15 B 325 PRO ALA GLU SER SER LEU PHE SER LEU THR ALA ASP GLN
SEQRES 16 B 325 GLN TRP GLU LEU ASP GLU ARG LEU LEU PRO THR GLY LYS
SEQRES 17 B 325 LEU MET ASP VAL PRO TYR LYS GLU ALA LEU HIS GLU GLY
SEQRES 18 B 325 MET ASP LEU ARG HIS LYS GLN LEU ASP ASP VAL PHE LEU
SEQRES 19 B 325 SER SER TYR GLN LYS ARG GLY GLY GLU ASN GLN ALA VAL
SEQRES 20 B 325 ILE TYR HIS GLN HIS ALA HIS ILE SER ILE ILE TYR LYS
SEQRES 21 B 325 ALA ASP GLU GLN PHE LYS HIS TRP VAL VAL TYR ASN ALA
SEQRES 22 B 325 ASP GLY LYS GLN GLY TYR LEU CYS PRO GLU PRO TYR THR
SEQRES 23 B 325 TRP VAL THR ASN ALA VAL ASN LEU ASP LEU PRO SER SER
SEQRES 24 B 325 LEU THR GLY LEU GLN VAL LEU GLU PRO GLY GLU GLU THR
SEQRES 25 B 325 THR ALA LYS SER SER ILE THR ILE GLU LEU ASN HIS GLN
HET GOL A 500 6
HET CIT B 500 13
HETNAM GOL GLYCEROL
HETNAM CIT CITRIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 CIT C6 H8 O7
FORMUL 5 HOH *312(H2 O)
HELIX 1 1 THR A 53 THR A 60 1 8
HELIX 2 2 LEU A 132 PHE A 139 1 8
HELIX 3 3 TYR A 214 GLY A 221 1 8
HELIX 4 4 SER A 236 GLY A 241 1 6
HELIX 5 5 ASN A 290 LEU A 294 5 5
HELIX 6 6 PRO A 297 GLY A 302 1 6
HELIX 7 7 THR B 53 THR B 60 1 8
HELIX 8 8 LEU B 132 PHE B 139 1 8
HELIX 9 9 TYR B 214 GLY B 221 1 8
HELIX 10 10 SER B 236 GLY B 241 1 6
HELIX 11 11 ASN B 290 LEU B 294 5 5
HELIX 12 12 PRO B 297 GLY B 302 1 6
SHEET 1 AA13 VAL A 45 GLN A 46 0
SHEET 2 AA13 ASN A 34 ASP A 40 -1 N ASP A 40 O VAL A 45
SHEET 3 AA13 LEU A 23 VAL A 28 -1 O GLU A 24 N VAL A 39
SHEET 4 AA13 THR A 13 ASN A 20 -1 O ILE A 16 N VAL A 27
SHEET 5 AA13 ASN A 3 TYR A 10 -1 O PHE A 4 N GLY A 19
SHEET 6 AA13 ASN B 110 GLN B 116 -1 O VAL B 112 N LYS A 7
SHEET 7 AA13 VAL B 121 ASP B 128 -1 O ILE B 122 N LYS B 115
SHEET 8 AA13 ALA B 143 LYS B 152 -1 O VAL B 145 N ILE B 127
SHEET 9 AA13 THR B 155 ASN B 164 -1 O THR B 155 N LYS B 152
SHEET 10 AA13 GLU B 311 LEU B 322 -1 O THR B 312 N VAL B 162
SHEET 11 AA13 ILE B 255 ALA B 261 -1 O SER B 256 N GLU B 321
SHEET 12 AA13 GLN B 245 HIS B 250 -1 O ALA B 246 N TYR B 259
SHEET 13 AA13 SER B 187 LEU B 191 -1 O LEU B 188 N TYR B 249
SHEET 1 AB 2 ILE A 68 LEU A 69 0
SHEET 2 AB 2 GLY A 175 TYR A 176 -1 O GLY A 175 N LEU A 69
SHEET 1 AC 2 ARG A 74 SER A 76 0
SHEET 2 AC 2 ASN A 98 LEU A 100 -1 O HIS A 99 N ILE A 75
SHEET 1 AD 2 THR A 79 PHE A 82 0
SHEET 2 AD 2 ARG A 85 HIS A 88 -1 O ARG A 85 N PHE A 82
SHEET 1 AE13 SER A 187 LEU A 191 0
SHEET 2 AE13 GLN A 245 HIS A 250 -1 O VAL A 247 N SER A 190
SHEET 3 AE13 ILE A 255 ALA A 261 -1 O ILE A 255 N HIS A 250
SHEET 4 AE13 GLU A 311 LEU A 322 -1 O SER A 317 N LYS A 260
SHEET 5 AE13 THR A 155 ASN A 164 -1 O LEU A 156 N ILE A 318
SHEET 6 AE13 ALA A 143 LYS A 152 -1 O VAL A 144 N MET A 163
SHEET 7 AE13 GLY A 120 ASP A 128 -1 O VAL A 121 N ILE A 151
SHEET 8 AE13 ASN A 110 THR A 117 -1 O ASN A 110 N GLU A 126
SHEET 9 AE13 PHE B 4 TYR B 10 -1 O ILE B 5 N GLN A 116
SHEET 10 AE13 THR B 13 GLY B 19 -1 O THR B 13 N TYR B 10
SHEET 11 AE13 LEU B 23 VAL B 28 -1 O MET B 25 N ALA B 18
SHEET 12 AE13 ASN B 34 ASP B 40 -1 O ASN B 34 N VAL B 28
SHEET 13 AE13 VAL B 45 GLN B 46 -1 O VAL B 45 N ASP B 40
SHEET 1 AF 2 PHE A 170 TRP A 172 0
SHEET 2 AF 2 GLN A 304 LEU A 306 -1 O GLN A 304 N TRP A 172
SHEET 1 AG 6 PHE A 180 ILE A 181 0
SHEET 2 AG 6 TYR A 279 TYR A 285 -1 O LEU A 280 N PHE A 180
SHEET 3 AG 6 HIS A 267 TYR A 271 -1 O HIS A 267 N TYR A 285
SHEET 4 AG 6 ASP A 230 SER A 235 -1 O ASP A 231 N VAL A 270
SHEET 5 AG 6 ALA A 193 LEU A 199 -1 N ASP A 194 O LEU A 234
SHEET 6 AG 6 PRO A 205 ASP A 211 -1 N THR A 206 O GLU A 198
SHEET 1 BA 2 ILE B 68 LEU B 69 0
SHEET 2 BA 2 GLY B 175 TYR B 176 -1 O GLY B 175 N LEU B 69
SHEET 1 BB 2 ARG B 74 SER B 76 0
SHEET 2 BB 2 ASN B 98 LEU B 100 -1 O HIS B 99 N ILE B 75
SHEET 1 BC 2 THR B 79 PHE B 82 0
SHEET 2 BC 2 ARG B 85 HIS B 88 -1 O ARG B 85 N PHE B 82
SHEET 1 BD 2 PHE B 170 TRP B 172 0
SHEET 2 BD 2 GLN B 304 LEU B 306 -1 O GLN B 304 N TRP B 172
SHEET 1 BE 6 PHE B 180 ILE B 181 0
SHEET 2 BE 6 TYR B 279 TYR B 285 -1 O LEU B 280 N PHE B 180
SHEET 3 BE 6 HIS B 267 TYR B 271 -1 O HIS B 267 N TYR B 285
SHEET 4 BE 6 ASP B 230 SER B 235 -1 O ASP B 231 N VAL B 270
SHEET 5 BE 6 ALA B 193 LEU B 199 -1 N ASP B 194 O LEU B 234
SHEET 6 BE 6 PRO B 205 ASP B 211 -1 N THR B 206 O GLU B 198
CISPEP 1 PHE A 70 PRO A 71 0 -8.96
CISPEP 2 PHE B 70 PRO B 71 0 -2.42
SITE 1 AC1 6 ASN A 73 ARG A 74 HIS A 101 HIS A 177
SITE 2 AC1 6 ASP A 230 GLU A 283
SITE 1 AC2 5 LEU B 188 GLU B 220 TYR B 249 ASN B 323
SITE 2 AC2 5 HIS B 324
CRYST1 82.340 82.906 123.419 90.00 90.00 90.00 P 21 21 2 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 0.012145 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008102 0.00000
(ATOM LINES ARE NOT SHOWN.)
END