HEADER HYDROLASE 15-AUG-03 1Q74
TITLE THE CRYSTAL STRUCTURE OF 1D-MYO-INOSITYL 2-ACETAMIDO-2-
TITLE 2 DEOXY-ALPHA-D-GLUCOPYRANOSIDE DEACETYLASE (MSHB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1D-MYO-INOSITYL 2-ACETAMIDO-2-DEOXY-ALPHA-D-
COMPND 3 GLUCOPYRANOSIDE DEACETYLASE (MSHB);
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: RV1170;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS ROSSMANN FOLD, ZINC AMINOHYDROLASE, STRUCTURAL GENOMICS,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.MAYNES,C.GAREN,M.M.CHERNEY,G.NEWTON,D.ARAD,Y.AV-GAY,
AUTHOR 2 R.C.FAHEY,M.N.JAMES,TB STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (TBSGC)
REVDAT 2 01-FEB-05 1Q74 1 AUTHOR KEYWDS REMARK
REVDAT 1 02-DEC-03 1Q74 0
JRNL AUTH J.T.MAYNES,C.GAREN,M.M.CHERNEY,G.NEWTON,D.ARAD,
JRNL AUTH 2 Y.AV-GAY,R.C.FAHEY,M.N.JAMES
JRNL TITL THE CRYSTAL STRUCTURE OF 1-D-MYO-INOSITYL
JRNL TITL 2 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSIDE
JRNL TITL 3 DEACETYLASE (MSHB) FROM MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 4 REVEALS A ZINC HYDROLASE WITH A LACTATE
JRNL TITL 5 DEHYDROGENASE FOLD.
JRNL REF J.BIOL.CHEM. V. 278 47166 2003
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.800
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 127442
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6745
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9167
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 497
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 9152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.108
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.227
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8578 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 7783 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11714 ; 1.899 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17892 ; 1.468 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1106 ; 4.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1271 ;15.638 ;15.000
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): 1320 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9838 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1797 ; 0.017 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1652 ; 0.193 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7404 ; 0.133 ; 0.300
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): 1567 ; 0.149 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.100 ; 0.500
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): 16 ; 0.139 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 71 ; 0.152 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 59 ; 0.316 ; 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): 5526 ; 1.108 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8771 ; 1.907 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3052 ; 2.943 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2943 ; 4.694 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1Q74 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK 4
REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .
REMARK 100 THE RCSB ID CODE IS RCSB019999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-2001
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 517484
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.29600
REMARK 200 R SYM FOR SHELL (I) : 0.29600
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 50MM TRIS-HCL, 0.1M
REMARK 280 MG(NO3)2, 6% 1,6-HEXANEDIOL AND 10% ETHYLENEGLYCOL, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 3
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 BIOMOLECULE: 4
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 GLY A 100
REMARK 465 THR A 101
REMARK 465 ASP A 102
REMARK 465 GLN A 103
REMARK 465 GLY A 164
REMARK 465 SER A 165
REMARK 465 GLY A 166
REMARK 465 THR A 167
REMARK 465 ALA A 168
REMARK 465 ASP A 169
REMARK 465 ALA A 300
REMARK 465 SER A 301
REMARK 465 GLY A 302
REMARK 465 THR A 303
REMARK 465 MET B 1
REMARK 465 GLY B 97
REMARK 465 MET B 98
REMARK 465 ALA B 99
REMARK 465 GLY B 100
REMARK 465 THR B 101
REMARK 465 ASP B 102
REMARK 465 GLN B 103
REMARK 465 GLY B 164
REMARK 465 SER B 165
REMARK 465 GLY B 166
REMARK 465 THR B 167
REMARK 465 VAL B 207
REMARK 465 LEU B 208
REMARK 465 PRO B 209
REMARK 465 ARG B 210
REMARK 465 ALA B 211
REMARK 465 ASP B 212
REMARK 465 GLU B 213
REMARK 465 ILE B 214
REMARK 465 ALA B 215
REMARK 465 THR B 299
REMARK 465 ALA B 300
REMARK 465 SER B 301
REMARK 465 GLY B 302
REMARK 465 THR B 303
REMARK 465 MET C 1
REMARK 465 GLY C 97
REMARK 465 MET C 98
REMARK 465 ALA C 99
REMARK 465 GLY C 100
REMARK 465 THR C 101
REMARK 465 ASP C 102
REMARK 465 GLN C 103
REMARK 465 VAL C 163
REMARK 465 GLY C 164
REMARK 465 SER C 165
REMARK 465 GLY C 166
REMARK 465 THR C 167
REMARK 465 ALA C 211
REMARK 465 ASP C 212
REMARK 465 GLU C 213
REMARK 465 ILE C 214
REMARK 465 ALA C 215
REMARK 465 PHE C 216
REMARK 465 THR C 299
REMARK 465 ALA C 300
REMARK 465 SER C 301
REMARK 465 GLY C 302
REMARK 465 THR C 303
REMARK 465 MET D 1
REMARK 465 GLY D 100
REMARK 465 THR D 101
REMARK 465 ASP D 102
REMARK 465 GLY D 164
REMARK 465 SER D 165
REMARK 465 GLY D 166
REMARK 465 THR D 167
REMARK 465 GLU D 205
REMARK 465 TRP D 206
REMARK 465 VAL D 207
REMARK 465 LEU D 208
REMARK 465 PRO D 209
REMARK 465 ARG D 210
REMARK 465 ALA D 211
REMARK 465 ASP D 212
REMARK 465 GLU D 213
REMARK 465 ILE D 214
REMARK 465 ALA D 215
REMARK 465 PHE D 216
REMARK 465 THR D 299
REMARK 465 ALA D 300
REMARK 465 SER D 301
REMARK 465 GLY D 302
REMARK 465 THR D 303
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
REMARK 500 O HOH 201 O HOH 710 2.00
REMARK 500 O HOH 254 O HOH 763 2.06
REMARK 500 OD1 ASP A 200 O HOH 763 2.08
REMARK 500 O HOH 140 O HOH 763 2.11
REMARK 500 O HOH 133 O HOH 762 2.16
REMARK 500 O HOH 376 O HOH 762 2.17
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 445 O HOH 762 1655 2.00
REMARK 500 O HOH 204 O HOH 763 1556 2.01
REMARK 500 O HOH 89 O HOH 639 1554 2.02
REMARK 500 O HOH 256 O HOH 762 1655 2.02
REMARK 500 OE1 GLN B 106 O HOH 762 1655 2.06
REMARK 500 O HOH 255 O HOH 763 1556 2.14
REMARK 500 O HOH 281 O HOH 711 1554 2.18
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 252 CB PRO A 252 CG -0.131
REMARK 500 PRO B 252 CB PRO B 252 CG -0.153
REMARK 500 PRO C 252 CB PRO C 252 CG -0.130
REMARK 500 MET D 98 SD MET D 98 CE 0.116
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 107 CG - CD - NE ANGL. DEV. =-12.0 DEGREES
REMARK 500 ARG B 77 CB - CG - CD ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG D 203 N - CA - C ANGL. DEV. = 13.2 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ASP A 15 -33.89 122.97
REMARK 500 ASP B 15 -32.87 127.63
REMARK 500 ASP C 15 -30.76 124.72
REMARK 500 ASP D 15 -29.42 128.37
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 548 DISTANCE = 7.13 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1170 RELATED DB: TARGETDB
DBREF 1Q74 A 1 303 UNP O50426 O50426_MYCTU 1 303
DBREF 1Q74 B 1 303 UNP O50426 O50426_MYCTU 1 303
DBREF 1Q74 C 1 303 UNP O50426 O50426_MYCTU 1 303
DBREF 1Q74 D 1 303 UNP O50426 O50426_MYCTU 1 303
SEQRES 1 A 303 MET SER GLU THR PRO ARG LEU LEU PHE VAL HIS ALA HIS
SEQRES 2 A 303 PRO ASP ASP GLU SER LEU SER ASN GLY ALA THR ILE ALA
SEQRES 3 A 303 HIS TYR THR SER ARG GLY ALA GLN VAL HIS VAL VAL THR
SEQRES 4 A 303 CYS THR LEU GLY GLU GLU GLY GLU VAL ILE GLY ASP ARG
SEQRES 5 A 303 TRP ALA GLN LEU THR ALA ASP HIS ALA ASP GLN LEU GLY
SEQRES 6 A 303 GLY TYR ARG ILE GLY GLU LEU THR ALA ALA LEU ARG ALA
SEQRES 7 A 303 LEU GLY VAL SER ALA PRO ILE TYR LEU GLY GLY ALA GLY
SEQRES 8 A 303 ARG TRP ARG ASP SER GLY MET ALA GLY THR ASP GLN ARG
SEQRES 9 A 303 SER GLN ARG ARG PHE VAL ASP ALA ASP PRO ARG GLN THR
SEQRES 10 A 303 VAL GLY ALA LEU VAL ALA ILE ILE ARG GLU LEU ARG PRO
SEQRES 11 A 303 HIS VAL VAL VAL THR TYR ASP PRO ASN GLY GLY TYR GLY
SEQRES 12 A 303 HIS PRO ASP HIS VAL HIS THR HIS THR VAL THR THR ALA
SEQRES 13 A 303 ALA VAL ALA ALA ALA GLY VAL GLY SER GLY THR ALA ASP
SEQRES 14 A 303 HIS PRO GLY ASP PRO TRP THR VAL PRO LYS PHE TYR TRP
SEQRES 15 A 303 THR VAL LEU GLY LEU SER ALA LEU ILE SER GLY ALA ARG
SEQRES 16 A 303 ALA LEU VAL PRO ASP ASP LEU ARG PRO GLU TRP VAL LEU
SEQRES 17 A 303 PRO ARG ALA ASP GLU ILE ALA PHE GLY TYR SER ASP ASP
SEQRES 18 A 303 GLY ILE ASP ALA VAL VAL GLU ALA ASP GLU GLN ALA ARG
SEQRES 19 A 303 ALA ALA LYS VAL ALA ALA LEU ALA ALA HIS ALA THR GLN
SEQRES 20 A 303 VAL VAL VAL GLY PRO THR GLY ARG ALA ALA ALA LEU SER
SEQRES 21 A 303 ASN ASN LEU ALA LEU PRO ILE LEU ALA ASP GLU HIS TYR
SEQRES 22 A 303 VAL LEU ALA GLY GLY SER ALA GLY ALA ARG ASP GLU ARG
SEQRES 23 A 303 GLY TRP GLU THR ASP LEU LEU ALA GLY LEU GLY PHE THR
SEQRES 24 A 303 ALA SER GLY THR
SEQRES 1 B 303 MET SER GLU THR PRO ARG LEU LEU PHE VAL HIS ALA HIS
SEQRES 2 B 303 PRO ASP ASP GLU SER LEU SER ASN GLY ALA THR ILE ALA
SEQRES 3 B 303 HIS TYR THR SER ARG GLY ALA GLN VAL HIS VAL VAL THR
SEQRES 4 B 303 CYS THR LEU GLY GLU GLU GLY GLU VAL ILE GLY ASP ARG
SEQRES 5 B 303 TRP ALA GLN LEU THR ALA ASP HIS ALA ASP GLN LEU GLY
SEQRES 6 B 303 GLY TYR ARG ILE GLY GLU LEU THR ALA ALA LEU ARG ALA
SEQRES 7 B 303 LEU GLY VAL SER ALA PRO ILE TYR LEU GLY GLY ALA GLY
SEQRES 8 B 303 ARG TRP ARG ASP SER GLY MET ALA GLY THR ASP GLN ARG
SEQRES 9 B 303 SER GLN ARG ARG PHE VAL ASP ALA ASP PRO ARG GLN THR
SEQRES 10 B 303 VAL GLY ALA LEU VAL ALA ILE ILE ARG GLU LEU ARG PRO
SEQRES 11 B 303 HIS VAL VAL VAL THR TYR ASP PRO ASN GLY GLY TYR GLY
SEQRES 12 B 303 HIS PRO ASP HIS VAL HIS THR HIS THR VAL THR THR ALA
SEQRES 13 B 303 ALA VAL ALA ALA ALA GLY VAL GLY SER GLY THR ALA ASP
SEQRES 14 B 303 HIS PRO GLY ASP PRO TRP THR VAL PRO LYS PHE TYR TRP
SEQRES 15 B 303 THR VAL LEU GLY LEU SER ALA LEU ILE SER GLY ALA ARG
SEQRES 16 B 303 ALA LEU VAL PRO ASP ASP LEU ARG PRO GLU TRP VAL LEU
SEQRES 17 B 303 PRO ARG ALA ASP GLU ILE ALA PHE GLY TYR SER ASP ASP
SEQRES 18 B 303 GLY ILE ASP ALA VAL VAL GLU ALA ASP GLU GLN ALA ARG
SEQRES 19 B 303 ALA ALA LYS VAL ALA ALA LEU ALA ALA HIS ALA THR GLN
SEQRES 20 B 303 VAL VAL VAL GLY PRO THR GLY ARG ALA ALA ALA LEU SER
SEQRES 21 B 303 ASN ASN LEU ALA LEU PRO ILE LEU ALA ASP GLU HIS TYR
SEQRES 22 B 303 VAL LEU ALA GLY GLY SER ALA GLY ALA ARG ASP GLU ARG
SEQRES 23 B 303 GLY TRP GLU THR ASP LEU LEU ALA GLY LEU GLY PHE THR
SEQRES 24 B 303 ALA SER GLY THR
SEQRES 1 C 303 MET SER GLU THR PRO ARG LEU LEU PHE VAL HIS ALA HIS
SEQRES 2 C 303 PRO ASP ASP GLU SER LEU SER ASN GLY ALA THR ILE ALA
SEQRES 3 C 303 HIS TYR THR SER ARG GLY ALA GLN VAL HIS VAL VAL THR
SEQRES 4 C 303 CYS THR LEU GLY GLU GLU GLY GLU VAL ILE GLY ASP ARG
SEQRES 5 C 303 TRP ALA GLN LEU THR ALA ASP HIS ALA ASP GLN LEU GLY
SEQRES 6 C 303 GLY TYR ARG ILE GLY GLU LEU THR ALA ALA LEU ARG ALA
SEQRES 7 C 303 LEU GLY VAL SER ALA PRO ILE TYR LEU GLY GLY ALA GLY
SEQRES 8 C 303 ARG TRP ARG ASP SER GLY MET ALA GLY THR ASP GLN ARG
SEQRES 9 C 303 SER GLN ARG ARG PHE VAL ASP ALA ASP PRO ARG GLN THR
SEQRES 10 C 303 VAL GLY ALA LEU VAL ALA ILE ILE ARG GLU LEU ARG PRO
SEQRES 11 C 303 HIS VAL VAL VAL THR TYR ASP PRO ASN GLY GLY TYR GLY
SEQRES 12 C 303 HIS PRO ASP HIS VAL HIS THR HIS THR VAL THR THR ALA
SEQRES 13 C 303 ALA VAL ALA ALA ALA GLY VAL GLY SER GLY THR ALA ASP
SEQRES 14 C 303 HIS PRO GLY ASP PRO TRP THR VAL PRO LYS PHE TYR TRP
SEQRES 15 C 303 THR VAL LEU GLY LEU SER ALA LEU ILE SER GLY ALA ARG
SEQRES 16 C 303 ALA LEU VAL PRO ASP ASP LEU ARG PRO GLU TRP VAL LEU
SEQRES 17 C 303 PRO ARG ALA ASP GLU ILE ALA PHE GLY TYR SER ASP ASP
SEQRES 18 C 303 GLY ILE ASP ALA VAL VAL GLU ALA ASP GLU GLN ALA ARG
SEQRES 19 C 303 ALA ALA LYS VAL ALA ALA LEU ALA ALA HIS ALA THR GLN
SEQRES 20 C 303 VAL VAL VAL GLY PRO THR GLY ARG ALA ALA ALA LEU SER
SEQRES 21 C 303 ASN ASN LEU ALA LEU PRO ILE LEU ALA ASP GLU HIS TYR
SEQRES 22 C 303 VAL LEU ALA GLY GLY SER ALA GLY ALA ARG ASP GLU ARG
SEQRES 23 C 303 GLY TRP GLU THR ASP LEU LEU ALA GLY LEU GLY PHE THR
SEQRES 24 C 303 ALA SER GLY THR
SEQRES 1 D 303 MET SER GLU THR PRO ARG LEU LEU PHE VAL HIS ALA HIS
SEQRES 2 D 303 PRO ASP ASP GLU SER LEU SER ASN GLY ALA THR ILE ALA
SEQRES 3 D 303 HIS TYR THR SER ARG GLY ALA GLN VAL HIS VAL VAL THR
SEQRES 4 D 303 CYS THR LEU GLY GLU GLU GLY GLU VAL ILE GLY ASP ARG
SEQRES 5 D 303 TRP ALA GLN LEU THR ALA ASP HIS ALA ASP GLN LEU GLY
SEQRES 6 D 303 GLY TYR ARG ILE GLY GLU LEU THR ALA ALA LEU ARG ALA
SEQRES 7 D 303 LEU GLY VAL SER ALA PRO ILE TYR LEU GLY GLY ALA GLY
SEQRES 8 D 303 ARG TRP ARG ASP SER GLY MET ALA GLY THR ASP GLN ARG
SEQRES 9 D 303 SER GLN ARG ARG PHE VAL ASP ALA ASP PRO ARG GLN THR
SEQRES 10 D 303 VAL GLY ALA LEU VAL ALA ILE ILE ARG GLU LEU ARG PRO
SEQRES 11 D 303 HIS VAL VAL VAL THR TYR ASP PRO ASN GLY GLY TYR GLY
SEQRES 12 D 303 HIS PRO ASP HIS VAL HIS THR HIS THR VAL THR THR ALA
SEQRES 13 D 303 ALA VAL ALA ALA ALA GLY VAL GLY SER GLY THR ALA ASP
SEQRES 14 D 303 HIS PRO GLY ASP PRO TRP THR VAL PRO LYS PHE TYR TRP
SEQRES 15 D 303 THR VAL LEU GLY LEU SER ALA LEU ILE SER GLY ALA ARG
SEQRES 16 D 303 ALA LEU VAL PRO ASP ASP LEU ARG PRO GLU TRP VAL LEU
SEQRES 17 D 303 PRO ARG ALA ASP GLU ILE ALA PHE GLY TYR SER ASP ASP
SEQRES 18 D 303 GLY ILE ASP ALA VAL VAL GLU ALA ASP GLU GLN ALA ARG
SEQRES 19 D 303 ALA ALA LYS VAL ALA ALA LEU ALA ALA HIS ALA THR GLN
SEQRES 20 D 303 VAL VAL VAL GLY PRO THR GLY ARG ALA ALA ALA LEU SER
SEQRES 21 D 303 ASN ASN LEU ALA LEU PRO ILE LEU ALA ASP GLU HIS TYR
SEQRES 22 D 303 VAL LEU ALA GLY GLY SER ALA GLY ALA ARG ASP GLU ARG
SEQRES 23 D 303 GLY TRP GLU THR ASP LEU LEU ALA GLY LEU GLY PHE THR
SEQRES 24 D 303 ALA SER GLY THR
HET ZN A 300 1
HET ZN B 300 1
HET ZN C 300 1
HET ZN D 300 1
HET PE4 800 24
HETNAM ZN ZINC ION
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 5 ZN 4(ZN 2+)
FORMUL 9 PE4 C16 H34 O8
FORMUL 10 HOH *760(H2 O)
HELIX 1 1 ASP A 15 ARG A 31 1 17
HELIX 2 2 TRP A 53 THR A 57 5 5
HELIX 3 3 GLN A 63 LEU A 79 1 17
HELIX 4 4 ARG A 108 ALA A 112 5 5
HELIX 5 5 ASP A 113 ARG A 129 1 17
HELIX 6 6 HIS A 144 VAL A 163 1 20
HELIX 7 7 GLY A 186 LEU A 197 1 12
HELIX 8 8 VAL A 198 LEU A 202 5 5
HELIX 9 9 ARG A 210 ILE A 214 5 5
HELIX 10 10 SER A 219 ILE A 223 5 5
HELIX 11 11 ASP A 230 HIS A 244 1 15
HELIX 12 12 ASP B 15 ARG B 31 1 17
HELIX 13 13 TRP B 53 THR B 57 5 5
HELIX 14 14 GLN B 63 LEU B 79 1 17
HELIX 15 15 ARG B 108 ALA B 112 5 5
HELIX 16 16 ASP B 113 ARG B 129 1 17
HELIX 17 17 HIS B 144 GLY B 162 1 19
HELIX 18 18 GLY B 186 ALA B 196 1 11
HELIX 19 19 VAL B 198 LEU B 202 5 5
HELIX 20 20 SER B 219 ILE B 223 5 5
HELIX 21 21 ASP B 230 HIS B 244 1 15
HELIX 22 22 ASP C 15 ARG C 31 1 17
HELIX 23 23 TRP C 53 THR C 57 5 5
HELIX 24 24 GLN C 63 LEU C 79 1 17
HELIX 25 25 ARG C 108 ALA C 112 5 5
HELIX 26 26 ASP C 113 ARG C 129 1 17
HELIX 27 27 HIS C 144 GLY C 162 1 19
HELIX 28 28 GLY C 186 ALA C 196 1 11
HELIX 29 29 VAL C 198 LEU C 202 5 5
HELIX 30 30 SER C 219 ILE C 223 5 5
HELIX 31 31 ASP C 230 HIS C 244 1 15
HELIX 32 32 ASP D 15 ARG D 31 1 17
HELIX 33 33 TRP D 53 THR D 57 5 5
HELIX 34 34 GLN D 63 LEU D 79 1 17
HELIX 35 35 ARG D 108 ALA D 112 5 5
HELIX 36 36 ASP D 113 ARG D 129 1 17
HELIX 37 37 HIS D 144 GLY D 162 1 19
HELIX 38 38 GLY D 186 ALA D 196 1 11
HELIX 39 39 VAL D 198 LEU D 202 5 5
HELIX 40 40 SER D 219 ILE D 223 5 5
HELIX 41 41 ASP D 230 HIS D 244 1 15
SHEET 1 A 7 ILE A 85 TYR A 86 0
SHEET 2 A 7 GLN A 34 THR A 39 1 N THR A 39 O ILE A 85
SHEET 3 A 7 ARG A 6 HIS A 11 1 N HIS A 11 O VAL A 38
SHEET 4 A 7 VAL A 132 TYR A 136 1 O VAL A 132 N LEU A 8
SHEET 5 A 7 LYS A 179 VAL A 184 1 O TYR A 181 N VAL A 133
SHEET 6 A 7 ASP A 270 GLY A 277 -1 O VAL A 274 N TRP A 182
SHEET 7 A 7 ALA A 225 GLU A 228 -1 N VAL A 227 O GLU A 271
SHEET 1 B 3 VAL A 249 VAL A 250 0
SHEET 2 B 3 ALA A 256 ALA A 258 -1 O ALA A 258 N VAL A 249
SHEET 3 B 3 ALA A 264 PRO A 266 -1 O LEU A 265 N ALA A 257
SHEET 1 C 7 ILE B 85 TYR B 86 0
SHEET 2 C 7 GLN B 34 THR B 39 1 N THR B 39 O ILE B 85
SHEET 3 C 7 ARG B 6 HIS B 11 1 N HIS B 11 O VAL B 38
SHEET 4 C 7 VAL B 132 TYR B 136 1 O VAL B 134 N LEU B 8
SHEET 5 C 7 LYS B 179 VAL B 184 1 O TYR B 181 N VAL B 133
SHEET 6 C 7 ASP B 270 GLY B 277 -1 O VAL B 274 N TRP B 182
SHEET 7 C 7 ALA B 225 GLU B 228 -1 N ALA B 225 O TYR B 273
SHEET 1 D 3 VAL B 249 VAL B 250 0
SHEET 2 D 3 ALA B 256 ALA B 258 -1 O ALA B 258 N VAL B 249
SHEET 3 D 3 ALA B 264 PRO B 266 -1 O LEU B 265 N ALA B 257
SHEET 1 E 7 ILE C 85 TYR C 86 0
SHEET 2 E 7 GLN C 34 THR C 39 1 N THR C 39 O ILE C 85
SHEET 3 E 7 ARG C 6 HIS C 11 1 N HIS C 11 O VAL C 38
SHEET 4 E 7 VAL C 132 TYR C 136 1 O VAL C 134 N LEU C 8
SHEET 5 E 7 LYS C 179 VAL C 184 1 O TYR C 181 N VAL C 133
SHEET 6 E 7 ASP C 270 GLY C 277 -1 O VAL C 274 N TRP C 182
SHEET 7 E 7 ALA C 225 GLU C 228 -1 N VAL C 227 O GLU C 271
SHEET 1 F 3 VAL C 249 VAL C 250 0
SHEET 2 F 3 ALA C 256 ALA C 258 -1 O ALA C 258 N VAL C 249
SHEET 3 F 3 ALA C 264 PRO C 266 -1 O LEU C 265 N ALA C 257
SHEET 1 G 7 ILE D 85 TYR D 86 0
SHEET 2 G 7 GLN D 34 THR D 39 1 N THR D 39 O ILE D 85
SHEET 3 G 7 ARG D 6 HIS D 11 1 N HIS D 11 O VAL D 38
SHEET 4 G 7 VAL D 132 TYR D 136 1 O VAL D 132 N LEU D 8
SHEET 5 G 7 LYS D 179 VAL D 184 1 O THR D 183 N THR D 135
SHEET 6 G 7 ASP D 270 GLY D 277 -1 O VAL D 274 N TRP D 182
SHEET 7 G 7 ALA D 225 GLU D 228 -1 N ALA D 225 O TYR D 273
SHEET 1 H 3 VAL D 249 VAL D 250 0
SHEET 2 H 3 ALA D 256 ALA D 258 -1 O ALA D 258 N VAL D 249
SHEET 3 H 3 ALA D 264 PRO D 266 -1 O LEU D 265 N ALA D 257
LINK ZN ZN A 300 ND1 HIS A 13
LINK ZN ZN A 300 OD2 ASP A 16
LINK ZN ZN A 300 NE2 HIS A 147
LINK ZN ZN B 300 ND1 HIS B 13
LINK ZN ZN B 300 OD2 ASP B 16
LINK ZN ZN B 300 NE2 HIS B 147
LINK ZN ZN C 300 ND1 HIS C 13
LINK ZN ZN C 300 OD2 ASP C 16
LINK ZN ZN C 300 NE2 HIS C 147
LINK ZN ZN D 300 ND1 HIS D 13
LINK ZN ZN D 300 OD2 ASP D 16
LINK ZN ZN D 300 NE2 HIS D 147
CISPEP 1 ALA B 168 ASP B 169 0 -4.29
CISPEP 2 ALA C 168 ASP C 169 0 -3.06
CISPEP 3 ALA D 168 ASP D 169 0 -0.17
CISPEP 4 ARG D 203 PRO D 204 0 4.77
CRYST1 56.794 73.964 85.587 102.09 108.16 97.18 P 1 4
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 0.017608 0.002219 0.006593 0.00000
SCALE2 0.000000 0.013627 0.003723 0.00000
SCALE3 0.000000 0.000000 0.012747 0.00000