HEADER HYDROLASE 19-AUG-13 4MB1
TITLE THE STRUCTURE OF MALL MUTANT ENZYME G202P FROM BACILLUS SUBTILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OLIGO-1,6-GLUCOSIDASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DEXTRIN 6-ALPHA-D-GLUCANOHYDROLASE, OLIGOSACCHARIDE ALPHA-1,
COMPND 5 6-GLUCOSIDASE 1, SUCRASE-ISOMALTASE 1, ISOMALTASE 1;
COMPND 6 EC: 3.2.1.10;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: MALL, YVDL, BSU34560;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB
KEYWDS TIM BARREL, ALPHA GLUCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.HOBBS,W.JIAO,A.D.EASTER,E.J.PARKER,L.A.SCHIPPER,V.L.ARCUS
REVDAT 3 28-FEB-24 4MB1 1 REMARK SEQADV LINK
REVDAT 2 27-NOV-13 4MB1 1 JRNL
REVDAT 1 25-SEP-13 4MB1 0
JRNL AUTH J.K.HOBBS,W.JIAO,A.D.EASTER,E.J.PARKER,L.A.SCHIPPER,
JRNL AUTH 2 V.L.ARCUS
JRNL TITL CHANGE IN HEAT CAPACITY FOR ENZYME CATALYSIS DETERMINES
JRNL TITL 2 TEMPERATURE DEPENDENCE OF ENZYME CATALYZED RATES.
JRNL REF ACS CHEM.BIOL. V. 8 2388 2013
JRNL REFN ISSN 1554-8929
JRNL PMID 24015933
JRNL DOI 10.1021/CB4005029
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 104495
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5251
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7169
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 353
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4613
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 498
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37000
REMARK 3 B22 (A**2) : 0.67000
REMARK 3 B33 (A**2) : -0.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.772
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4788 ; 0.022 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4352 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6493 ; 2.142 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10038 ; 0.962 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 571 ; 6.829 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 260 ;35.243 ;24.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 824 ;12.406 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;15.799 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 651 ; 0.142 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5481 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1166 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 : 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 206
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6587 -15.9800 26.8146
REMARK 3 T TENSOR
REMARK 3 T11: 0.0720 T22: 0.0011
REMARK 3 T33: 0.0779 T12: -0.0027
REMARK 3 T13: 0.0119 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.5558 L22: 0.7990
REMARK 3 L33: 0.6831 L12: -0.1618
REMARK 3 L13: 0.2192 L23: -0.4107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: 0.0154 S13: -0.0802
REMARK 3 S21: 0.0279 S22: -0.0052 S23: 0.0429
REMARK 3 S31: 0.0513 S32: -0.0067 S33: -0.0314
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 207 A 214
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2469 -13.6841 39.2847
REMARK 3 T TENSOR
REMARK 3 T11: 0.1285 T22: 0.1471
REMARK 3 T33: 0.2285 T12: -0.0048
REMARK 3 T13: -0.0826 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 2.7496 L22: 7.9025
REMARK 3 L33: 6.6062 L12: -0.7635
REMARK 3 L13: 2.1198 L23: 4.2630
REMARK 3 S TENSOR
REMARK 3 S11: -0.0587 S12: 0.0619 S13: -0.0418
REMARK 3 S21: 0.5645 S22: 0.2465 S23: -0.9106
REMARK 3 S31: 0.1166 S32: 0.4423 S33: -0.1878
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 215 A 240
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3488 -16.7426 28.5404
REMARK 3 T TENSOR
REMARK 3 T11: 0.0924 T22: 0.0922
REMARK 3 T33: 0.1319 T12: 0.0138
REMARK 3 T13: -0.0002 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.3944 L22: 4.2675
REMARK 3 L33: 3.8413 L12: 0.4467
REMARK 3 L13: 0.5359 L23: 2.6558
REMARK 3 S TENSOR
REMARK 3 S11: -0.0291 S12: -0.0027 S13: -0.0160
REMARK 3 S21: 0.0389 S22: 0.1227 S23: -0.2967
REMARK 3 S31: -0.0932 S32: 0.4415 S33: -0.0936
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 241 A 388
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7076 -1.5124 16.6449
REMARK 3 T TENSOR
REMARK 3 T11: 0.0619 T22: 0.0236
REMARK 3 T33: 0.0646 T12: 0.0051
REMARK 3 T13: 0.0130 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.5082 L22: 0.7648
REMARK 3 L33: 0.6655 L12: 0.2038
REMARK 3 L13: 0.0360 L23: -0.1318
REMARK 3 S TENSOR
REMARK 3 S11: 0.0238 S12: 0.0066 S13: -0.0313
REMARK 3 S21: 0.0097 S22: -0.0251 S23: -0.0769
REMARK 3 S31: 0.0252 S32: 0.0792 S33: 0.0013
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 389 A 452
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9248 7.3571 28.3159
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.0106
REMARK 3 T33: 0.0753 T12: -0.0013
REMARK 3 T13: 0.0319 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.8149 L22: 0.2399
REMARK 3 L33: 1.0355 L12: -0.1688
REMARK 3 L13: 0.9415 L23: -0.1429
REMARK 3 S TENSOR
REMARK 3 S11: 0.0059 S12: -0.1051 S13: 0.0845
REMARK 3 S21: 0.0847 S22: -0.0107 S23: 0.0104
REMARK 3 S31: -0.0895 S32: -0.0309 S33: 0.0048
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 453 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5638 3.6314 0.9020
REMARK 3 T TENSOR
REMARK 3 T11: 0.1047 T22: 0.0484
REMARK 3 T33: 0.0515 T12: 0.0020
REMARK 3 T13: 0.0137 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.4190 L22: 0.7271
REMARK 3 L33: 0.9623 L12: -0.4086
REMARK 3 L13: -0.7501 L23: 0.3932
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: 0.2427 S13: -0.0864
REMARK 3 S21: -0.0637 S22: 0.0173 S23: -0.0166
REMARK 3 S31: 0.0436 S32: -0.0398 S33: 0.0242
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 : A 501 A 537
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8100 10.0306 -4.2346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1048 T22: 0.0575
REMARK 3 T33: 0.0861 T12: -0.0082
REMARK 3 T13: 0.0248 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 2.0927 L22: 1.2363
REMARK 3 L33: 2.3594 L12: -0.3587
REMARK 3 L13: -0.6958 L23: 0.0734
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: 0.1299 S13: 0.0552
REMARK 3 S21: -0.1192 S22: 0.0751 S23: -0.1204
REMARK 3 S31: -0.0536 S32: 0.0314 S33: -0.0719
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 : A 538 A 543
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5374 15.8557 -8.6295
REMARK 3 T TENSOR
REMARK 3 T11: 0.7429 T22: 0.8039
REMARK 3 T33: 0.6311 T12: 0.1697
REMARK 3 T13: 0.1258 T23: 0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 6.5699 L22: 0.4731
REMARK 3 L33: 1.8700 L12: -1.7346
REMARK 3 L13: 3.4909 L23: -0.9244
REMARK 3 S TENSOR
REMARK 3 S11: 0.5439 S12: 0.9266 S13: -0.5635
REMARK 3 S21: -0.1308 S22: -0.2194 S23: 0.2416
REMARK 3 S31: 0.2167 S32: 0.4113 S33: -0.3245
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 : A 544 A 559
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1211 13.2525 -2.8565
REMARK 3 T TENSOR
REMARK 3 T11: 0.1286 T22: 0.0710
REMARK 3 T33: 0.1203 T12: -0.0084
REMARK 3 T13: 0.0065 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 1.8262 L22: 3.1558
REMARK 3 L33: 7.2201 L12: -0.4559
REMARK 3 L13: -1.0246 L23: 4.7392
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: 0.2110 S13: 0.0146
REMARK 3 S21: -0.2193 S22: 0.1434 S23: -0.0507
REMARK 3 S31: -0.2893 S32: 0.1543 S33: -0.1338
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 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4MB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000081689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104533
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 56.992
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.58400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 24% (W/V) PEG
REMARK 280 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 50.53500
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: 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 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 2
REMARK 465 GLU A 541
REMARK 465 ARG A 542
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 GLU A 153 CG CD OE1 OE2
REMARK 470 GLU A 214 CG CD OE1 OE2
REMARK 470 ASP A 216 CB CG OD1 OD2
REMARK 470 LYS A 517 CE NZ
REMARK 470 GLN A 540 CG CD OE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 345 NZ
REMARK 480 LYS A 411 CD CE NZ
REMARK 480 LYS A 478 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 OD1 ASP A 85 O HOH A 1013 1.86
REMARK 500 OE1 GLU A 400 O HOH A 1185 2.13
REMARK 500 NE ARG A 395 O HOH A 1172 2.14
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 ARG A 179 CZ ARG A 179 NH1 0.096
REMARK 500 LYS A 345 CE LYS A 345 NZ -0.239
REMARK 500 GLN A 489 CD GLN A 489 OE1 0.141
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 GLU A 112 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP A 123 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 179 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 179 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP A 209 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 225 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ASP A 285 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 313 CD - NE - CZ ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG A 313 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 339 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 344 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LYS A 345 CD - CE - NZ ANGL. DEV. = 15.0 DEGREES
REMARK 500 ASP A 379 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 386 CB - CG - OD1 ANGL. DEV. = -9.8 DEGREES
REMARK 500 ARG A 395 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 395 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 GLU A 396 OE1 - CD - OE2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 LYS A 411 CG - CD - CE ANGL. DEV. = -19.2 DEGREES
REMARK 500 ASP A 428 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 450 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 450 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 474 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 LYS A 478 CB - CG - CD ANGL. DEV. = 16.7 DEGREES
REMARK 500 ARG A 500 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLU A 516 CG - CD - OE1 ANGL. DEV. = -15.1 DEGREES
REMARK 500 MET A 557 CG - SD - CE ANGL. DEV. = -10.2 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 PHE A 18 -69.50 -94.55
REMARK 500 SER A 55 141.63 -171.04
REMARK 500 ASP A 66 113.79 -161.75
REMARK 500 SER A 145 154.39 80.96
REMARK 500 PHE A 163 -134.29 -103.98
REMARK 500 VAL A 200 53.73 30.52
REMARK 500 HIS A 217 -13.63 101.57
REMARK 500 VAL A 244 -64.26 -132.36
REMARK 500 GLU A 274 -103.29 -116.80
REMARK 500 ASN A 291 53.47 -159.00
REMARK 500 ARG A 344 -106.41 -124.65
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 CA A 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASN A 22 OD1 85.6
REMARK 620 3 ASP A 24 OD1 88.7 82.9
REMARK 620 4 PHE A 26 O 86.8 169.3 89.4
REMARK 620 5 ASP A 28 OD2 89.7 84.8 167.7 102.6
REMARK 620 6 HOH A 822 O 167.4 87.6 79.9 98.3 100.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MAZ RELATED DB: PDB
REMARK 900 RELATED ID: 4M8U RELATED DB: PDB
REMARK 900 RELATED ID: 4M56 RELATED DB: PDB
DBREF 4MB1 A 1 561 UNP O06994 O16G1_BACSU 1 561
SEQADV 4MB1 PRO A 202 UNP O06994 GLY 202 ENGINEERED MUTATION
SEQRES 1 A 561 MET SER GLU TRP TRP LYS GLU ALA VAL VAL TYR GLN ILE
SEQRES 2 A 561 TYR PRO ARG SER PHE TYR ASP ALA ASN GLY ASP GLY PHE
SEQRES 3 A 561 GLY ASP LEU GLN GLY VAL ILE GLN LYS LEU ASP TYR ILE
SEQRES 4 A 561 LYS ASN LEU GLY ALA ASP VAL ILE TRP LEU SER PRO VAL
SEQRES 5 A 561 PHE ASP SER PRO GLN ASP ASP ASN GLY TYR ASP ILE SER
SEQRES 6 A 561 ASP TYR LYS ASN MET TYR GLU LYS PHE GLY THR ASN GLU
SEQRES 7 A 561 ASP MET PHE GLN LEU ILE ASP GLU VAL HIS LYS ARG GLY
SEQRES 8 A 561 MET LYS ILE VAL MET ASP LEU VAL VAL ASN HIS THR SER
SEQRES 9 A 561 ASP GLU HIS ALA TRP PHE ALA GLU SER ARG LYS SER LYS
SEQRES 10 A 561 ASP ASN PRO TYR ARG ASP TYR TYR LEU TRP LYS ASP PRO
SEQRES 11 A 561 LYS PRO ASP GLY SER GLU PRO ASN ASN TRP GLY SER ILE
SEQRES 12 A 561 PHE SER GLY SER ALA TRP THR TYR ASP GLU GLY THR GLY
SEQRES 13 A 561 GLN TYR TYR LEU HIS TYR PHE SER LYS LYS GLN PRO ASP
SEQRES 14 A 561 LEU ASN TRP GLU ASN GLU ALA VAL ARG ARG GLU VAL TYR
SEQRES 15 A 561 ASP VAL MET ARG PHE TRP MET ASP ARG GLY VAL ASP GLY
SEQRES 16 A 561 TRP ARG MET ASP VAL ILE PRO SER ILE SER LYS TYR THR
SEQRES 17 A 561 ASP PHE PRO ASP TYR GLU THR ASP HIS SER ARG SER TYR
SEQRES 18 A 561 ILE VAL GLY ARG TYR HIS SER ASN GLY PRO ARG LEU HIS
SEQRES 19 A 561 GLU PHE ILE GLN GLU MET ASN ARG GLU VAL LEU SER HIS
SEQRES 20 A 561 TYR ASP CYS MET THR VAL GLY GLU ALA ASN GLY SER ASP
SEQRES 21 A 561 ILE GLU GLU ALA LYS LYS TYR THR ASP ALA SER ARG GLN
SEQRES 22 A 561 GLU LEU ASN MET ILE PHE THR PHE GLU HIS MET ASP ILE
SEQRES 23 A 561 ASP LYS GLU GLN ASN SER PRO ASN GLY LYS TRP GLN ILE
SEQRES 24 A 561 LYS PRO PHE ASP LEU ILE ALA LEU LYS LYS THR MET THR
SEQRES 25 A 561 ARG TRP GLN THR GLY LEU MET ASN VAL GLY TRP ASN THR
SEQRES 26 A 561 LEU TYR PHE GLU ASN HIS ASP GLN PRO ARG VAL ILE SER
SEQRES 27 A 561 ARG TRP GLY ASN ASP ARG LYS LEU ARG LYS GLU CYS ALA
SEQRES 28 A 561 LYS ALA PHE ALA THR VAL LEU HIS GLY MET LYS GLY THR
SEQRES 29 A 561 PRO PHE ILE TYR GLN GLY GLU GLU ILE GLY MET VAL ASN
SEQRES 30 A 561 SER ASP MET PRO LEU GLU MET TYR ASP ASP LEU GLU ILE
SEQRES 31 A 561 LYS ASN ALA TYR ARG GLU LEU VAL VAL GLU ASN LYS THR
SEQRES 32 A 561 MET SER GLU LYS GLU PHE VAL LYS ALA VAL MET ILE LYS
SEQRES 33 A 561 GLY ARG ASP HIS ALA ARG THR PRO MET GLN TRP ASP ALA
SEQRES 34 A 561 GLY LYS HIS ALA GLY PHE THR ALA GLY ASP PRO TRP ILE
SEQRES 35 A 561 PRO VAL ASN SER ARG TYR GLN ASP ILE ASN VAL LYS GLU
SEQRES 36 A 561 SER LEU GLU ASP GLN ASP SER ILE PHE PHE TYR TYR GLN
SEQRES 37 A 561 LYS LEU ILE GLN LEU ARG LYS GLN TYR LYS ILE MET ILE
SEQRES 38 A 561 TYR GLY ASP TYR GLN LEU LEU GLN GLU ASN ASP PRO GLN
SEQRES 39 A 561 VAL PHE SER TYR LEU ARG GLU TYR ARG GLY GLU LYS LEU
SEQRES 40 A 561 LEU VAL VAL VAL ASN LEU SER GLU GLU LYS ALA LEU PHE
SEQRES 41 A 561 GLU ALA PRO PRO GLU LEU ILE HIS GLU ARG TRP LYS VAL
SEQRES 42 A 561 LEU ILE SER ASN TYR PRO GLN GLU ARG ALA ASP LEU LYS
SEQRES 43 A 561 SER ILE SER LEU LYS PRO TYR GLU ALA VAL MET GLY ILE
SEQRES 44 A 561 SER ILE
HET TRS A 601 8
HET CA A 602 1
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM CA CALCIUM ION
HETSYN TRS TRIS BUFFER
FORMUL 2 TRS C4 H12 N O3 1+
FORMUL 3 CA CA 2+
FORMUL 4 HOH *498(H2 O)
HELIX 1 1 TYR A 14 PHE A 18 5 5
HELIX 2 2 ASP A 28 GLY A 43 1 16
HELIX 3 3 THR A 76 ARG A 90 1 15
HELIX 4 4 HIS A 107 ARG A 114 1 8
HELIX 5 5 TYR A 121 TYR A 125 5 5
HELIX 6 6 ASN A 174 ARG A 191 1 18
HELIX 7 7 VAL A 200 ILE A 204 5 5
HELIX 8 8 GLY A 224 SER A 228 5 5
HELIX 9 9 ARG A 232 VAL A 244 1 13
HELIX 10 10 LEU A 245 TYR A 248 5 4
HELIX 11 11 ASP A 260 ASP A 269 1 10
HELIX 12 12 ALA A 270 GLN A 273 5 4
HELIX 13 13 ASN A 294 GLN A 298 5 5
HELIX 14 14 ASP A 303 LEU A 318 1 16
HELIX 15 15 ARG A 335 GLY A 341 1 7
HELIX 16 16 LEU A 346 GLY A 360 1 15
HELIX 17 17 GLY A 370 GLY A 374 5 5
HELIX 18 18 PRO A 381 TYR A 385 5 5
HELIX 19 19 ASP A 387 VAL A 398 1 12
HELIX 20 20 SER A 405 GLY A 417 1 13
HELIX 21 21 ARG A 418 ARG A 422 5 5
HELIX 22 22 GLY A 430 PHE A 435 5 6
HELIX 23 23 ASN A 452 ASP A 459 1 8
HELIX 24 24 SER A 462 TYR A 477 1 16
HELIX 25 25 LYS A 478 GLY A 483 1 6
HELIX 26 26 PRO A 523 ILE A 527 5 5
SHEET 1 A 8 MET A 277 PHE A 279 0
SHEET 2 A 8 MET A 251 GLU A 255 1 N GLY A 254 O PHE A 279
SHEET 3 A 8 GLY A 195 MET A 198 1 N MET A 198 O VAL A 253
SHEET 4 A 8 LYS A 93 LEU A 98 1 N LEU A 98 O ARG A 197
SHEET 5 A 8 VAL A 46 LEU A 49 1 N ILE A 47 O VAL A 95
SHEET 6 A 8 VAL A 10 ILE A 13 1 N TYR A 11 O VAL A 46
SHEET 7 A 8 THR A 364 TYR A 368 1 O ILE A 367 N VAL A 10
SHEET 8 A 8 THR A 325 LEU A 326 1 N LEU A 326 O PHE A 366
SHEET 1 B 2 PHE A 53 ASP A 54 0
SHEET 2 B 2 ASP A 66 MET A 70 -1 O ASN A 69 N ASP A 54
SHEET 1 C 3 TRP A 127 LYS A 128 0
SHEET 2 C 3 GLN A 157 LEU A 160 -1 O TYR A 158 N LYS A 128
SHEET 3 C 3 TRP A 149 ASP A 152 -1 N ASP A 152 O GLN A 157
SHEET 1 D 5 GLN A 486 LEU A 488 0
SHEET 2 D 5 VAL A 495 TYR A 502 -1 O SER A 497 N LEU A 488
SHEET 3 D 5 GLU A 505 ASN A 512 -1 O VAL A 511 N PHE A 496
SHEET 4 D 5 ALA A 555 SER A 560 -1 O VAL A 556 N VAL A 510
SHEET 5 D 5 TRP A 531 SER A 536 -1 N LYS A 532 O ILE A 559
SHEET 1 E 2 ALA A 518 GLU A 521 0
SHEET 2 E 2 SER A 547 LEU A 550 -1 O ILE A 548 N PHE A 520
LINK OD1 ASP A 20 CA CA A 602 1555 1555 2.27
LINK OD1 ASN A 22 CA CA A 602 1555 1555 2.32
LINK OD1 ASP A 24 CA CA A 602 1555 1555 2.38
LINK O PHE A 26 CA CA A 602 1555 1555 2.27
LINK OD2 ASP A 28 CA CA A 602 1555 1555 2.31
LINK CA CA A 602 O HOH A 822 1555 1555 2.31
SITE 1 AC1 11 ASP A 59 TYR A 62 HIS A 102 PHE A 144
SITE 2 AC1 11 PHE A 163 ASP A 199 GLU A 255 ARG A 418
SITE 3 AC1 11 HOH A 717 HOH A 719 HOH A1179
SITE 1 AC2 6 ASP A 20 ASN A 22 ASP A 24 PHE A 26
SITE 2 AC2 6 ASP A 28 HOH A 822
CRYST1 48.500 101.070 61.850 90.00 112.86 90.00 P 1 21 1 2
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 0.020619 0.000000 0.008693 0.00000
SCALE2 0.000000 0.009894 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017546 0.00000
(ATOM LINES ARE NOT SHOWN.)
END