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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 01-OCT-03 1R3D
TITLE CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN VC1974 FROM
TITLE 2 VIBRIO CHOLERAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN VC1974;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 GENE: VC1974;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A DERIVED CUSTOM VECTOR
KEYWDS STRUCTURAL GENOMICS, HYDROLASE, NYSGRC, NEW YORK STRUCTURAL
KEYWDS 2 GENOMICS RESEARCH CONSORTIUM, PSI, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GORMAN,L.SHAPIRO
REVDAT 1 30-NOV-04 1R3D 0
JRNL AUTH J.GORMAN,L.SHAPIRO
JRNL TITL STRUCTURAL GENOMICS TARGET NYSGRC-T920 RELATED TO
JRNL TITL 2 A/B HYDROLASE FOLD.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 20222
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1089
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1481
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.1790
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2149
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.49000
REMARK 3 B22 (A**2) : 0.49000
REMARK 3 B33 (A**2) : -0.98000
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): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2030 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1822 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2759 ; 1.439 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4240 ; 0.829 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 255 ; 5.820 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 95 ;39.752 ;24.737
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 329 ;14.429 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;20.881 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 310 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2282 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 387 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 413 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1770 ; 0.190 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 977 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1145 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 119 ; 0.141 ; 0.200
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): 7 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.249 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.136 ; 0.200
REMARK 3 SYMMETRY H-BOND 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): 1541 ; 1.385 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 523 ; 0.276 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2038 ; 1.740 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 825 ; 3.061 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 721 ; 4.480 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1R3D COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020386.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-AUG-2003
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 : APS
REMARK 200 BEAMLINE : 8BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .978
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21381
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, .1M TRIS PH 8.0, 10%
REMARK 280 ISOPROPANOL, .24M NA ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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 1/2-Y,1/2+X,1/2+Z
REMARK 290 4555 1/2+Y,1/2-X,1/2+Z
REMARK 290 5555 1/2-X,1/2+Y,1/2-Z
REMARK 290 6555 1/2+X,1/2-Y,1/2-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 49.73500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.73500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.74600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.73500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.73500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.74600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.73500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.73500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.74600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.73500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.73500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.74600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 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 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 23 LIES ON A SPECIAL POSITION.
REMARK 375 HOH 70 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 GLU A 58
REMARK 465 ARG A 59
REMARK 465 HIS A 60
REMARK 465 CYS A 61
REMARK 465 ASP A 62
REMARK 465 ASN A 63
REMARK 465 PHE A 64
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 PHE A 8 -59.19 79.89
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: T920 RELATED DB: TARGETDB
DBREF 1R3D A 2 263 GB 15641976 NP_231608 2 263
SEQADV 1R3D SER A 0 GB 15641976 CLONING ARTIFACT
SEQADV 1R3D LEU A 1 GB 15641976 CLONING ARTIFACT
SEQADV 1R3D MSE A 70 GB 15641976 MET 70 MODIFIED RESIDUE
SEQADV 1R3D MSE A 98 GB 15641976 MET 98 MODIFIED RESIDUE
SEQADV 1R3D MSE A 187 GB 15641976 MET 187 MODIFIED RESIDUE
SEQADV 1R3D MSE A 257 GB 15641976 MET 257 MODIFIED RESIDUE
SEQRES 1 A 264 SER LEU LEU SER ASN GLN LEU HIS PHE ALA LYS PRO THR
SEQRES 2 A 264 ALA ARG THR PRO LEU VAL VAL LEU VAL HIS GLY LEU LEU
SEQRES 3 A 264 GLY SER GLY ALA ASP TRP GLN PRO VAL LEU SER HIS LEU
SEQRES 4 A 264 ALA ARG THR GLN CYS ALA ALA LEU THR LEU ASP LEU PRO
SEQRES 5 A 264 GLY HIS GLY THR ASN PRO GLU ARG HIS CYS ASP ASN PHE
SEQRES 6 A 264 ALA GLU ALA VAL GLU MSE ILE GLU GLN THR VAL GLN ALA
SEQRES 7 A 264 HIS VAL THR SER GLU VAL PRO VAL ILE LEU VAL GLY TYR
SEQRES 8 A 264 SER LEU GLY GLY ARG LEU ILE MSE HIS GLY LEU ALA GLN
SEQRES 9 A 264 GLY ALA PHE SER ARG LEU ASN LEU ARG GLY ALA ILE ILE
SEQRES 10 A 264 GLU GLY GLY HIS PHE GLY LEU GLN GLU ASN GLU GLU LYS
SEQRES 11 A 264 ALA ALA ARG TRP GLN HIS ASP GLN GLN TRP ALA GLN ARG
SEQRES 12 A 264 PHE SER GLN GLN PRO ILE GLU HIS VAL LEU SER ASP TRP
SEQRES 13 A 264 TYR GLN GLN ALA VAL PHE SER SER LEU ASN HIS GLU GLN
SEQRES 14 A 264 ARG GLN THR LEU ILE ALA GLN ARG SER ALA ASN LEU GLY
SEQRES 15 A 264 SER SER VAL ALA HIS MSE LEU LEU ALA THR SER LEU ALA
SEQRES 16 A 264 LYS GLN PRO TYR LEU LEU PRO ALA LEU GLN ALA LEU LYS
SEQRES 17 A 264 LEU PRO ILE HIS TYR VAL CYS GLY GLU GLN ASP SER LYS
SEQRES 18 A 264 PHE GLN GLN LEU ALA GLU SER SER GLY LEU SER TYR SER
SEQRES 19 A 264 GLN VAL ALA GLN ALA GLY HIS ASN VAL HIS HIS GLU GLN
SEQRES 20 A 264 PRO GLN ALA PHE ALA LYS ILE VAL GLN ALA MSE ILE HIS
SEQRES 21 A 264 SER ILE ILE ASP
MODRES 1R3D MSE A 70 MET SELENOMETHIONINE
MODRES 1R3D MSE A 98 MET SELENOMETHIONINE
MODRES 1R3D MSE A 187 MET SELENOMETHIONINE
MODRES 1R3D MSE A 257 MET SELENOMETHIONINE
HET MSE A 70 8
HET MSE A 98 8
HET MSE A 187 8
HET MSE A 257 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N1 O2 SE1)
FORMUL 2 HOH *164(H2 O1)
HELIX 1 1 SER A 27 ASP A 30 5 4
HELIX 2 2 TRP A 31 ALA A 39 1 9
HELIX 3 3 ALA A 65 ALA A 77 1 13
HELIX 4 4 SER A 91 GLY A 104 1 14
HELIX 5 5 GLU A 125 GLN A 146 1 22
HELIX 6 6 PRO A 147 TYR A 156 1 10
HELIX 7 7 GLN A 157 SER A 162 5 6
HELIX 8 8 ASN A 165 SER A 177 1 13
HELIX 9 9 LEU A 180 THR A 191 1 12
HELIX 10 10 SER A 192 GLN A 196 5 5
HELIX 11 11 LEU A 199 ALA A 205 1 7
HELIX 12 12 ASP A 218 GLY A 229 1 12
HELIX 13 13 ASN A 241 GLN A 246 1 6
HELIX 14 14 GLN A 246 ILE A 262 1 17
SHEET 1 A 7 ASN A 4 HIS A 7 0
SHEET 2 A 7 ALA A 44 LEU A 48 -1 O ALA A 45 N HIS A 7
SHEET 3 A 7 LEU A 17 VAL A 21 1 N LEU A 20 O LEU A 46
SHEET 4 A 7 PRO A 84 TYR A 90 1 O ILE A 86 N VAL A 19
SHEET 5 A 7 ASN A 110 GLU A 117 1 O ARG A 112 N VAL A 85
SHEET 6 A 7 ILE A 210 GLY A 215 1 O VAL A 213 N ILE A 116
SHEET 7 A 7 SER A 231 VAL A 235 1 O VAL A 235 N CYS A 214
CRYST1 99.470 99.470 53.492 90.00 90.00 90.00 P 42 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 0.010053 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010053 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018694 0.00000
TER 1986 ASP A 263
MASTER 278 0 4 14 7 0 0 6 2149 1 32 21
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