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HEADER HYDROLASE 12-APR-18 5ZOA
TITLE THE CRYSTAL STRUCTURE OF A THERMOBIFIDA FUSCA CUTINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BTA-HYDROLASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_COMMON: THERMOMONOSPORA FUSCA;
SOURCE 4 ORGANISM_TAXID: 2021;
SOURCE 5 GENE: BTA1, CUT_2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS CUTIN, THERMOBIFIDA FUSCA CUTINASE HYDROLYSIS ACTIVITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.L.DONG,L.WU,J.WU,J.H.ZHOU
REVDAT 1 17-APR-19 5ZOA 0
JRNL AUTH Q.L.DONG,L.WU,J.WU,J.H.ZHOU
JRNL TITL THE CRYSTAL STRUCTURE OF A CUTINASE FROM THERMOBIFIDA FUSCA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 43229
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.830
REMARK 3 FREE R VALUE TEST SET COUNT : 2089
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 28.5473 - 3.7887 0.99 2968 143 0.1640 0.1797
REMARK 3 2 3.7887 - 3.0083 1.00 2840 133 0.1668 0.1628
REMARK 3 3 3.0083 - 2.6283 1.00 2765 151 0.1842 0.2016
REMARK 3 4 2.6283 - 2.3881 1.00 2747 143 0.1732 0.1985
REMARK 3 5 2.3881 - 2.2170 1.00 2749 144 0.1626 0.1692
REMARK 3 6 2.2170 - 2.0864 1.00 2738 154 0.1546 0.1595
REMARK 3 7 2.0864 - 1.9819 1.00 2710 150 0.1513 0.1658
REMARK 3 8 1.9819 - 1.8956 1.00 2766 104 0.1568 0.1829
REMARK 3 9 1.8956 - 1.8227 1.00 2683 140 0.1567 0.1639
REMARK 3 10 1.8227 - 1.7598 1.00 2704 162 0.1498 0.2056
REMARK 3 11 1.7598 - 1.7048 1.00 2737 131 0.1546 0.1833
REMARK 3 12 1.7048 - 1.6561 1.00 2702 119 0.1561 0.1843
REMARK 3 13 1.6561 - 1.6125 1.00 2695 144 0.1696 0.1667
REMARK 3 14 1.6125 - 1.5731 1.00 2684 139 0.1841 0.2258
REMARK 3 15 1.5731 - 1.5374 0.98 2652 132 0.2111 0.2387
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.010 2069
REMARK 3 ANGLE : 1.147 2834
REMARK 3 CHIRALITY : 0.074 318
REMARK 3 PLANARITY : 0.008 372
REMARK 3 DIHEDRAL : 2.791 1685
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0740 31.7331 17.1818
REMARK 3 T TENSOR
REMARK 3 T11: 0.0614 T22: 0.0815
REMARK 3 T33: 0.0583 T12: 0.0007
REMARK 3 T13: 0.0134 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 1.8747 L22: 1.8214
REMARK 3 L33: 1.5125 L12: 0.7580
REMARK 3 L13: -0.2088 L23: -0.1433
REMARK 3 S TENSOR
REMARK 3 S11: -0.0907 S12: -0.0371 S13: -0.0604
REMARK 3 S21: -0.0455 S22: 0.0439 S23: -0.0109
REMARK 3 S31: 0.0040 S32: 0.1548 S33: -0.0111
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5ZOA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1300007387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43283
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.537
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 18.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 2.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0M NACL, 4.0%(V/V) POLYPROPYLENE
REMARK 280 GLYCEL P400, 0.1M HEPES PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 2 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-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 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 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 TOTAL BURIED SURFACE AREA: 140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 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 O HOH A 514 O HOH A 517 2.05
REMARK 500 OE1 GLU A 64 O HOH A 401 2.13
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 LEU A 14 CA - CB - CG ANGL. DEV. = 17.1 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 THR A 61 -0.66 70.43
REMARK 500 SER A 130 -119.90 65.74
REMARK 500 THR A 153 59.32 35.39
REMARK 500 HIS A 184 -84.64 -124.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
DBREF 5ZOA A 1 261 UNP Q6A0I4 Q6A0I4_THEFU 41 301
SEQRES 1 A 261 ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR ASP ALA
SEQRES 2 A 261 LEU LEU GLU ALA SER SER GLY PRO PHE SER VAL SER GLU
SEQRES 3 A 261 GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE GLY GLY
SEQRES 4 A 261 GLY THR ILE TYR TYR PRO ARG GLU ASN ASN THR TYR GLY
SEQRES 5 A 261 ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR GLU ALA
SEQRES 6 A 261 SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER HIS GLY
SEQRES 7 A 261 PHE VAL VAL ILE THR ILE ASP THR ILE THR THR LEU ASP
SEQRES 8 A 261 GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA ALA LEU
SEQRES 9 A 261 ASN HIS MET ILE ASN ARG ALA SER SER THR VAL ARG SER
SEQRES 10 A 261 ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY HIS SER
SEQRES 11 A 261 MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER GLN ARG
SEQRES 12 A 261 PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO TRP HIS
SEQRES 13 A 261 LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO THR LEU
SEQRES 14 A 261 ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO VAL ALA
SEQRES 15 A 261 THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO SER SER
SEQRES 16 A 261 ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA THR HIS
SEQRES 17 A 261 PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY LYS TYR
SEQRES 18 A 261 SER VAL ALA TRP LEU LYS ARG PHE VAL ASP ASN ASP THR
SEQRES 19 A 261 ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG ASP GLY
SEQRES 20 A 261 LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR CYS PRO
SEQRES 21 A 261 PHE
HET CL A 301 1
HET CL A 302 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL 2(CL 1-)
FORMUL 4 HOH *158(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 THR A 63 SER A 66 5 4
HELIX 3 AA3 ILE A 67 SER A 76 1 10
HELIX 4 AA4 GLN A 92 ARG A 110 1 19
HELIX 5 AA5 SER A 112 SER A 117 1 6
HELIX 6 AA6 SER A 130 ARG A 143 1 14
HELIX 7 AA7 HIS A 184 LEU A 192 1 9
HELIX 8 AA8 PHE A 209 ILE A 213 5 5
HELIX 9 AA9 ASN A 215 ASP A 231 1 17
HELIX 10 AB1 ASP A 233 ARG A 235 5 3
HELIX 11 AB2 TYR A 236 CYS A 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 ILE A 42 N GLU A 27
SHEET 3 AA1 6 VAL A 80 ILE A 84 -1 O VAL A 81 N TYR A 43
SHEET 4 AA1 6 TYR A 51 SER A 57 1 N VAL A 54 O ILE A 82
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O ASP A 120 N TYR A 51
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 LEU A 203 N GLY A 172
SHEET 3 AA2 3 GLU A 254 SER A 257 -1 O GLU A 254 N GLU A 202
CISPEP 1 CYS A 241 PRO A 242 0 9.30
CISPEP 2 CYS A 259 PRO A 260 0 15.86
SITE 1 AC1 1 ASN A 215
SITE 1 AC2 3 ASN A 215 LYS A 216 HOH A 532
CRYST1 86.298 86.298 76.117 90.00 90.00 90.00 P 4 2 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 0.011588 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011588 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013138 0.00000
TER 2013 PHE A 261
MASTER 298 0 2 11 9 0 2 6 2148 1 0 21
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