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HEADER HYDROLASE 07-FEB-21 7E30
TITLE CRYSTAL STRUCTURE OF A NOVEL ALPHA/BETA HYDROLASE IN APO FORM IN
TITLE 2 COMPLEX WITH CITRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS ALPHA/BETA DEHYDROGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GAO,X.HAN,Y.Y.ZHENG,W.D.LIU
REVDAT 1 09-FEB-22 7E30 0
JRNL AUTH J.GAO,X.HAN,Y.Y.ZHENG,W.D.LIU
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL ALPHA/BETA HYDROLASE IN APO
JRNL TITL 2 FORM IN COMPLEX WITH CITRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 77449
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3866
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.5500 - 3.3600 1.00 7700 401 0.1429 0.1463
REMARK 3 2 3.3600 - 2.6700 1.00 7438 391 0.1488 0.1655
REMARK 3 3 2.6700 - 2.3300 1.00 7395 385 0.1498 0.1888
REMARK 3 4 2.3300 - 2.1200 1.00 7354 387 0.1411 0.1793
REMARK 3 5 2.1200 - 1.9700 1.00 7320 390 0.1416 0.1743
REMARK 3 6 1.9700 - 1.8500 1.00 7322 379 0.1481 0.1729
REMARK 3 7 1.8500 - 1.7600 1.00 7261 383 0.1522 0.1790
REMARK 3 8 1.7600 - 1.6800 1.00 7289 386 0.1644 0.2048
REMARK 3 9 1.6800 - 1.6200 1.00 7296 391 0.1801 0.2160
REMARK 3 10 1.6200 - 1.5600 1.00 7208 373 0.1996 0.2232
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 1 THROUGH 258 OR
REMARK 3 RESID 401))
REMARK 3 SELECTION : (CHAIN B AND (RESID 1 THROUGH 258 OR
REMARK 3 RESID 401))
REMARK 3 ATOM PAIRS NUMBER : 1582
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7E30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-21.
REMARK 100 THE DEPOSITION ID IS D_1300020689.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77551
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5ZRQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PEG 1500, NAAC, PH 8.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 27.98700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.55600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.54300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.55600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.98700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.54300
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 THR A 63 -3.86 72.32
REMARK 500 SER A 130 -115.75 54.28
REMARK 500 ASN A 143 89.46 -160.21
REMARK 500 HIS A 184 -93.73 -120.90
REMARK 500 PRO A 242 -157.71 -81.72
REMARK 500 SER B 130 -117.98 59.39
REMARK 500 ASN B 143 92.40 -161.40
REMARK 500 HIS B 184 -92.71 -120.84
REMARK 500 PRO B 242 -148.64 -82.54
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 B 672 DISTANCE = 5.97 ANGSTROMS
DBREF 7E30 A 1 258 PDB 7E30 7E30 1 258
DBREF 7E30 B 1 258 PDB 7E30 7E30 1 258
SEQRES 1 A 258 ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 A 258 SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA GLN
SEQRES 3 A 258 THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY GLY
SEQRES 4 A 258 GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY THR
SEQRES 5 A 258 PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA GLY
SEQRES 6 A 258 GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER
SEQRES 7 A 258 GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR ARG
SEQRES 8 A 258 LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN ALA
SEQRES 9 A 258 ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG ASN
SEQRES 10 A 258 ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS SER
SEQRES 11 A 258 MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN ASN
SEQRES 12 A 258 THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP HIS
SEQRES 13 A 258 THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR LEU
SEQRES 14 A 258 VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL SER
SEQRES 15 A 258 SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER ASP
SEQRES 16 A 258 LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER HIS
SEQRES 17 A 258 LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS TYR
SEQRES 18 A 258 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP LEU
SEQRES 19 A 258 ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP PHE
SEQRES 20 A 258 ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE
SEQRES 1 B 258 ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 B 258 SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA GLN
SEQRES 3 B 258 THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY GLY
SEQRES 4 B 258 GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY THR
SEQRES 5 B 258 PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA GLY
SEQRES 6 B 258 GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER
SEQRES 7 B 258 GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR ARG
SEQRES 8 B 258 LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN ALA
SEQRES 9 B 258 ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG ASN
SEQRES 10 B 258 ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS SER
SEQRES 11 B 258 MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN ASN
SEQRES 12 B 258 THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP HIS
SEQRES 13 B 258 THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR LEU
SEQRES 14 B 258 VAL VAL GLY ALA GLN LEU ASP THR ILE ALA PRO VAL SER
SEQRES 15 B 258 SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER ASP
SEQRES 16 B 258 LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER HIS
SEQRES 17 B 258 LEU VAL SER ASN THR PRO ASP THR THR THR ALA LYS TYR
SEQRES 18 B 258 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP ASP ASP LEU
SEQRES 19 B 258 ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP PHE
SEQRES 20 B 258 ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE
HET CIT A 301 13
HET MPD A 302 8
HET SO4 A 303 5
HET MPD B 301 8
HET MPD B 302 8
HET SO4 B 303 5
HETNAM CIT CITRIC ACID
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM SO4 SULFATE ION
FORMUL 3 CIT C6 H8 O7
FORMUL 4 MPD 3(C6 H14 O2)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 9 HOH *555(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 GLY A 65 ALA A 70 5 6
HELIX 3 AA3 TRP A 71 SER A 78 1 8
HELIX 4 AA4 GLN A 94 ARG A 110 1 17
HELIX 5 AA5 VAL A 115 ASN A 117 5 3
HELIX 6 AA6 SER A 130 ASN A 142 1 13
HELIX 7 AA7 HIS A 184 LEU A 192 1 9
HELIX 8 AA8 LEU A 209 THR A 213 5 5
HELIX 9 AA9 ASP A 215 ASP A 231 1 17
HELIX 10 AB1 ASP A 233 LEU A 240 5 8
HELIX 11 AB2 THR B 11 ALA B 17 1 7
HELIX 12 AB3 GLY B 65 ALA B 70 5 6
HELIX 13 AB4 TRP B 71 SER B 78 1 8
HELIX 14 AB5 GLN B 94 ARG B 110 1 17
HELIX 15 AB6 VAL B 115 ASN B 117 5 3
HELIX 16 AB7 SER B 130 ASN B 142 1 13
HELIX 17 AB8 HIS B 184 LEU B 192 1 9
HELIX 18 AB9 SER B 207 THR B 213 5 7
HELIX 19 AC1 ASP B 215 ASP B 231 1 17
HELIX 20 AC2 ASP B 233 ARG B 235 5 3
HELIX 21 AC3 TYR B 236 CYS B 241 1 6
SHEET 1 AA1 6 VAL A 24 VAL A 29 0
SHEET 2 AA1 6 GLY A 40 PRO A 45 -1 O GLY A 40 N VAL A 29
SHEET 3 AA1 6 VAL A 82 ILE A 86 -1 O VAL A 83 N TYR A 43
SHEET 4 AA1 6 PHE A 53 SER A 59 1 N VAL A 56 O ILE A 84
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O MET A 127 N ALA A 57
SHEET 6 AA1 6 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 ALA A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O ALA A 199 N VAL A 170
SHEET 3 AA2 3 ILE A 249 SER A 254 -1 O ARG A 253 N TYR A 200
SHEET 1 AA3 6 VAL B 24 VAL B 29 0
SHEET 2 AA3 6 GLY B 40 PRO B 45 -1 O GLY B 40 N VAL B 29
SHEET 3 AA3 6 VAL B 82 ILE B 86 -1 O VAL B 83 N TYR B 43
SHEET 4 AA3 6 PHE B 53 SER B 59 1 N VAL B 56 O ILE B 84
SHEET 5 AA3 6 ILE B 119 HIS B 129 1 O HIS B 129 N SER B 59
SHEET 6 AA3 6 ALA B 148 LEU B 152 1 O LEU B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 ALA B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O ALA B 199 N VAL B 170
SHEET 3 AA4 3 ILE B 249 SER B 254 -1 O ARG B 253 N TYR B 200
SSBOND 1 CYS A 241 CYS A 256 1555 1555 2.03
SSBOND 2 CYS B 241 CYS B 256 1555 1555 2.03
CISPEP 1 CYS A 241 PRO A 242 0 -6.83
CISPEP 2 CYS A 256 PRO A 257 0 -5.48
CISPEP 3 CYS B 241 PRO B 242 0 -9.67
CISPEP 4 CYS B 256 PRO B 257 0 -6.08
CRYST1 55.974 97.086 99.112 90.00 90.00 90.00 P 21 21 21 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 0.017865 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010300 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010090 0.00000
TER 1963 PHE A 258
TER 3926 PHE B 258
MASTER 248 0 6 21 18 0 0 6 4526 2 51 40
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