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HEADER TRANSFERASE 19-APR-07 2PL5
TITLE CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE FROM
TITLE 2 LEPTOSPIRA INTERROGANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HOMOSERINE O-TRANS-ACETYLASE, HOMOSERINE
COMPND 5 TRANSACETYLASE, HTA;
COMPND 6 EC: 2.3.1.31;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEPTOSPIRA INTERROGANS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: METX;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS HOMOSERINE O-ACETYLTRANSFERASE, ALPHA/BETA HYDROLASE
KEYWDS 2 SUPERFAMILY
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LIU,M.WANG,Y.WANG,Z.WEI,H.XU,W.GONG
REVDAT 1 20-NOV-07 2PL5 0
JRNL AUTH M.WANG,L.LIU,Y.WANG,Z.WEI,P.ZHANG,Y.LI,X.JIANG,
JRNL AUTH 2 H.XU,W.GONG
JRNL TITL CRYSTAL STRUCTURE OF HOMOSERINE
JRNL TITL 2 O-ACETYLTRANSFERASE FROM LEPTOSPIRA INTERROGANS
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 363 1050 2007
JRNL REFN ASTM BBRCA9 US ISSN 0006-291X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 21656
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1108
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2410
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3043
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : 0.27000
REMARK 3 B33 (A**2) : -0.54000
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): 0.290
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.205
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2917 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3963 ; 1.059 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 378 ; 5.371 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;34.398 ;24.567
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 476 ;14.843 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;17.390 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 426 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2244 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1382 ; 0.183 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1977 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 234 ; 0.145 ; 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): 106 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.165 ; 0.200
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): 1881 ; 0.498 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2938 ; 0.882 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1194 ; 1.065 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1019 ; 1.559 ; 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 2PL5 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB042498.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21812
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 58.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000, 0.1M MES, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 3555 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,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 107.57150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.56200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.56200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 161.35725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.56200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.56200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 53.78575
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.56200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.56200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 161.35725
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.56200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.56200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 53.78575
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 107.57150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: DIMER
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 215.14300
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
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 70 CG CD CE NZ
REMARK 480 LYS A 71 CG CD CE NZ
REMARK 480 LYS A 290 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 CE1 TYR A 228 OD1 ASP A 345 1.53
REMARK 500 CE1 TYR A 228 CG ASP A 345 2.19
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 PRO A 72 -162.68 -78.01
REMARK 500 SER A 153 -118.48 65.02
REMARK 500 ASN A 205 18.39 53.66
REMARK 500 LEU A 207 30.38 -99.39
REMARK 500 ASP A 209 -54.10 -151.72
REMARK 500 VAL A 254 54.71 -91.82
REMARK 500 ASP A 267 96.33 -60.86
REMARK 500 TYR A 314 77.74 -118.55
REMARK 500 HIS A 344 -38.97 -166.69
REMARK 500 ASP A 345 40.00 -97.38
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2PL5 A 1 366 UNP Q8F4I0 METX_LEPIN 1 366
SEQRES 1 A 366 MET ASN GLU THR GLY SER ILE GLY ILE ILE GLU THR LYS
SEQRES 2 A 366 TYR ALA GLU PHE LYS GLU LEU ILE LEU ASN ASN GLY SER
SEQRES 3 A 366 VAL LEU SER PRO VAL VAL ILE ALA TYR GLU THR TYR GLY
SEQRES 4 A 366 THR LEU SER SER SER LYS ASN ASN ALA ILE LEU ILE CYS
SEQRES 5 A 366 HIS ALA LEU SER GLY ASP ALA HIS ALA ALA GLY TYR HIS
SEQRES 6 A 366 SER GLY SER ASP LYS LYS PRO GLY TRP TRP ASP ASP TYR
SEQRES 7 A 366 ILE GLY PRO GLY LYS SER PHE ASP THR ASN GLN TYR PHE
SEQRES 8 A 366 ILE ILE CYS SER ASN VAL ILE GLY GLY CYS LYS GLY SER
SEQRES 9 A 366 SER GLY PRO LEU SER ILE HIS PRO GLU THR SER THR PRO
SEQRES 10 A 366 TYR GLY SER ARG PHE PRO PHE VAL SER ILE GLN ASP MET
SEQRES 11 A 366 VAL LYS ALA GLN LYS LEU LEU VAL GLU SER LEU GLY ILE
SEQRES 12 A 366 GLU LYS LEU PHE CYS VAL ALA GLY GLY SER MET GLY GLY
SEQRES 13 A 366 MET GLN ALA LEU GLU TRP SER ILE ALA TYR PRO ASN SER
SEQRES 14 A 366 LEU SER ASN CYS ILE VAL MET ALA SER THR ALA GLU HIS
SEQRES 15 A 366 SER ALA MET GLN ILE ALA PHE ASN GLU VAL GLY ARG GLN
SEQRES 16 A 366 ALA ILE LEU SER ASP PRO ASN TRP LYS ASN GLY LEU TYR
SEQRES 17 A 366 ASP GLU ASN SER PRO ARG LYS GLY LEU ALA LEU ALA ARG
SEQRES 18 A 366 MET VAL GLY HIS ILE THR TYR LEU SER ASP ASP LYS MET
SEQRES 19 A 366 ARG GLU LYS PHE GLY ARG ASN PRO PRO ARG GLY ASN ILE
SEQRES 20 A 366 LEU SER THR ASP PHE ALA VAL GLY SER TYR LEU ILE TYR
SEQRES 21 A 366 GLN GLY GLU SER PHE VAL ASP ARG PHE ASP ALA ASN SER
SEQRES 22 A 366 TYR ILE TYR VAL THR LYS ALA LEU ASP HIS TYR SER LEU
SEQRES 23 A 366 GLY LYS GLY LYS GLU LEU THR ALA ALA LEU SER ASN ALA
SEQRES 24 A 366 THR CYS ARG PHE LEU VAL VAL SER TYR SER SER ASP TRP
SEQRES 25 A 366 LEU TYR PRO PRO ALA GLN SER ARG GLU ILE VAL LYS SER
SEQRES 26 A 366 LEU GLU ALA ALA ASP LYS ARG VAL PHE TYR VAL GLU LEU
SEQRES 27 A 366 GLN SER GLY GLU GLY HIS ASP SER PHE LEU LEU LYS ASN
SEQRES 28 A 366 PRO LYS GLN ILE GLU ILE LEU LYS GLY PHE LEU GLU ASN
SEQRES 29 A 366 PRO ASN
HET GOL A 400 6
HET GOL A 500 6
HETNAM GOL GLYCEROL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 HOH *188(H2 O)
HELIX 1 1 TYR A 118 PHE A 122 5 5
HELIX 2 2 SER A 126 LEU A 141 1 16
HELIX 3 3 SER A 153 TYR A 166 1 14
HELIX 4 4 SER A 183 SER A 199 1 17
HELIX 5 5 TRP A 203 LEU A 207 5 5
HELIX 6 6 PRO A 213 THR A 227 1 15
HELIX 7 7 SER A 230 GLY A 239 1 10
HELIX 8 8 GLY A 255 TYR A 260 5 6
HELIX 9 9 ASP A 270 TYR A 284 1 15
HELIX 10 10 LYS A 288 SER A 297 1 10
HELIX 11 11 PRO A 315 ALA A 329 1 15
HELIX 12 12 HIS A 344 LEU A 349 5 6
HELIX 13 13 ASN A 351 ASN A 364 1 14
SHEET 1 A 8 LYS A 13 PHE A 17 0
SHEET 2 A 8 VAL A 31 GLY A 39 -1 O TYR A 35 N LYS A 13
SHEET 3 A 8 PHE A 91 SER A 95 -1 O ILE A 92 N TYR A 38
SHEET 4 A 8 ALA A 48 CYS A 52 1 N ILE A 51 O ILE A 93
SHEET 5 A 8 LEU A 146 GLY A 152 1 O ALA A 150 N CYS A 52
SHEET 6 A 8 LEU A 170 MET A 176 1 O ILE A 174 N VAL A 149
SHEET 7 A 8 ARG A 302 TYR A 308 1 O LEU A 304 N VAL A 175
SHEET 8 A 8 VAL A 333 LEU A 338 1 O LEU A 338 N SER A 307
SHEET 1 B 2 LEU A 20 ILE A 21 0
SHEET 2 B 2 VAL A 27 LEU A 28 -1 O LEU A 28 N LEU A 20
SHEET 1 C 2 ILE A 79 GLY A 80 0
SHEET 2 C 2 PHE A 85 ASP A 86 1 O PHE A 85 N GLY A 80
CISPEP 1 SER A 29 PRO A 30 0 -1.61
CRYST1 61.124 61.124 215.143 90.00 90.00 90.00 P 43 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 0.016360 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016360 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004648 0.00000
TER 2844 ASN A 366
MASTER 304 0 2 13 12 0 0 6 3043 1 12 29
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