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HEADER HYDROLASE 23-JUN-20 7CEH
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S176A/S226P/R228S/
TITLE 2 MUTANT WITH THE C-TERMINAL THREE RESIDUES DELETION IN LIGAND EJECTING
TITLE 3 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CUTINASE;
COMPND 5 EC: 3.1.1.74;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 GENE: CUT190, SAMN02982918_2340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN ENGINEERING, THERMOSTABILITY, POLYESTERASE, MULTIPLE
KEYWDS 2 CONFORMATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SENGA,N.NUMOTO,N.ITO,F.KAWAI,M.ODA
REVDAT 1 26-AUG-20 7CEH 0
JRNL AUTH A.SENGA,N.NUMOTO,M.YAMASHITA,A.IIDA,N.ITO,F.KAWAI,M.ODA
JRNL TITL MULTIPLE STRUCTURAL STATES OF CA2+ REGULATED PET HYDROLASE,
JRNL TITL 2 CUT190, AND ITS CORRELATION WITH ACTIVITY AND STABILITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 87540
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.131
REMARK 3 FREE R VALUE : 0.153
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4378
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 45.6000 - 3.3900 1.00 3186 168 0.1513 0.1557
REMARK 3 2 3.3900 - 2.6900 1.00 3030 161 0.1488 0.1419
REMARK 3 3 2.6900 - 2.3500 1.00 2992 157 0.1485 0.1624
REMARK 3 4 2.3500 - 2.1400 1.00 2947 155 0.1306 0.1350
REMARK 3 5 2.1400 - 1.9800 1.00 2989 157 0.1327 0.1660
REMARK 3 6 1.9800 - 1.8700 1.00 2939 155 0.1294 0.1582
REMARK 3 7 1.8700 - 1.7700 1.00 2954 155 0.1259 0.1481
REMARK 3 8 1.7700 - 1.7000 1.00 2909 154 0.1204 0.1624
REMARK 3 9 1.7000 - 1.6300 1.00 2941 154 0.1126 0.1327
REMARK 3 10 1.6300 - 1.5700 1.00 2912 154 0.1057 0.1474
REMARK 3 11 1.5700 - 1.5300 1.00 2908 153 0.1043 0.1436
REMARK 3 12 1.5300 - 1.4800 1.00 2951 154 0.1012 0.1355
REMARK 3 13 1.4800 - 1.4400 1.00 2882 152 0.1032 0.1379
REMARK 3 14 1.4400 - 1.4100 1.00 2918 154 0.1040 0.1396
REMARK 3 15 1.4100 - 1.3800 1.00 2934 154 0.1040 0.1451
REMARK 3 16 1.3800 - 1.3500 1.00 2877 152 0.1055 0.1389
REMARK 3 17 1.3500 - 1.3200 1.00 2924 154 0.1026 0.1370
REMARK 3 18 1.3200 - 1.2900 1.00 2869 151 0.1013 0.1303
REMARK 3 19 1.2900 - 1.2700 1.00 2922 154 0.1039 0.1549
REMARK 3 20 1.2700 - 1.2500 1.00 2893 152 0.1063 0.1364
REMARK 3 21 1.2500 - 1.2300 1.00 2901 153 0.1079 0.1337
REMARK 3 22 1.2300 - 1.2100 1.00 2894 152 0.1155 0.1499
REMARK 3 23 1.2100 - 1.1900 0.99 2884 152 0.1360 0.1670
REMARK 3 24 1.1900 - 1.1800 0.99 2829 146 0.1421 0.1678
REMARK 3 25 1.1800 - 1.1600 0.94 2738 140 0.1493 0.1673
REMARK 3 26 1.1600 - 1.1500 0.89 2555 134 0.1514 0.1824
REMARK 3 27 1.1500 - 1.1300 0.80 2295 120 0.1763 0.2221
REMARK 3 28 1.1300 - 1.1200 0.71 2050 116 0.1995 0.2650
REMARK 3 29 1.1200 - 1.1000 0.60 1722 100 0.2599 0.2581
REMARK 3 30 1.1000 - 1.0900 0.49 1417 65 0.3085 0.3205
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) : 0.078
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.746
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.35
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 : 0.004 2131
REMARK 3 ANGLE : 0.828 2921
REMARK 3 CHIRALITY : 0.081 315
REMARK 3 PLANARITY : 0.007 390
REMARK 3 DIHEDRAL : 18.060 814
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7CEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1300017480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-19
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 : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87545
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.090
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 (%) : 94.7
REMARK 200 DATA REDUNDANCY : 20.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10800
REMARK 200 FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.13
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) : 0.75500
REMARK 200 FOR SHELL : 2.000
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: 4WFI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL, 22% W/V PEG 8000, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 18.21000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.47500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.55050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.47500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.21000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.55050
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 GLY A 43
REMARK 465 PRO A 44
REMARK 465 GLN A 45
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 106 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 135 CG CD NE CZ NH1 NH2
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 ALA A 176 -120.80 64.38
REMARK 500 THR A 199 59.36 30.78
REMARK 500 HIS A 230 -82.91 -117.97
REMARK 500 THR A 301 30.70 -99.24
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 A 839 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 6.02 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 204 OD1
REMARK 620 2 ASP A 204 OD2 52.7
REMARK 620 3 THR A 206 O 84.7 108.8
REMARK 620 4 THR A 206 OG1 74.7 126.3 71.9
REMARK 620 5 HOH A 624 O 112.4 77.8 69.8 139.9
REMARK 620 6 HOH A 719 O 77.6 83.6 145.5 74.9 144.6
REMARK 620 7 HOH A 723 O 151.8 155.0 85.3 77.1 88.6 96.4
REMARK 620 8 HOH A 742 O 127.6 80.8 138.4 135.3 73.3 74.2 75.2
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 220 OE1
REMARK 620 2 GLU A 220 OE2 52.6
REMARK 620 3 ASP A 250 OD1 80.1 132.4
REMARK 620 4 GLU A 296 OE1 90.7 88.7 86.0
REMARK 620 5 HOH A 518 O 120.2 68.5 159.0 98.2
REMARK 620 6 HOH A 734 O 81.3 91.9 85.8 169.5 91.8
REMARK 620 7 HOH A 741 O 161.3 145.9 81.7 92.2 77.6 93.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7CEF RELATED DB: PDB
DBREF 7CEH A 45 304 UNP W0TJ64 W0TJ64_9PSEU 45 304
SEQADV 7CEH GLY A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CEH PRO A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 7CEH ALA A 176 UNP W0TJ64 SER 176 ENGINEERED MUTATION
SEQADV 7CEH PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 7CEH SER A 228 UNP W0TJ64 ARG 228 ENGINEERED MUTATION
SEQRES 1 A 262 GLY PRO GLN ASP ASN PRO TYR GLU ARG GLY PRO ASP PRO
SEQRES 2 A 262 THR GLU ASP SER ILE GLU ALA ILE ARG GLY PRO PHE SER
SEQRES 3 A 262 VAL ALA THR GLU ARG VAL SER SER PHE ALA SER GLY PHE
SEQRES 4 A 262 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU THR ASP GLU
SEQRES 5 A 262 GLY THR PHE GLY ALA VAL ALA VAL ALA PRO GLY PHE THR
SEQRES 6 A 262 ALA SER GLN GLY SER MET SER TRP TYR GLY GLU ARG VAL
SEQRES 7 A 262 ALA SER GLN GLY PHE ILE VAL PHE THR ILE ASP THR ASN
SEQRES 8 A 262 THR ARG LEU ASP GLN PRO GLY GLN ARG GLY ARG GLN LEU
SEQRES 9 A 262 LEU ALA ALA LEU ASP TYR LEU VAL GLU ARG SER ASP ARG
SEQRES 10 A 262 LYS VAL ARG GLU ARG LEU ASP PRO ASN ARG LEU ALA VAL
SEQRES 11 A 262 MET GLY HIS ALA MET GLY GLY GLY GLY SER LEU GLU ALA
SEQRES 12 A 262 THR VAL MET ARG PRO SER LEU LYS ALA SER ILE PRO LEU
SEQRES 13 A 262 THR PRO TRP ASN LEU ASP LYS THR TRP GLY GLN VAL GLN
SEQRES 14 A 262 VAL PRO THR PHE ILE ILE GLY ALA GLU LEU ASP THR ILE
SEQRES 15 A 262 ALA PRO VAL SER THR HIS ALA LYS PRO PHE TYR GLU SER
SEQRES 16 A 262 LEU PRO SER SER LEU PRO LYS ALA TYR MET GLU LEU ASP
SEQRES 17 A 262 GLY ALA THR HIS PHE ALA PRO ASN ILE PRO ASN THR THR
SEQRES 18 A 262 ILE ALA LYS TYR VAL ILE SER TRP LEU LYS ARG PHE VAL
SEQRES 19 A 262 ASP GLU ASP THR ARG TYR SER GLN PHE LEU CYS PRO ASN
SEQRES 20 A 262 PRO THR ASP ARG ALA ILE GLU GLU TYR ARG SER THR CYS
SEQRES 21 A 262 PRO TYR
HET CA A 401 1
HET CA A 402 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
FORMUL 4 HOH *341(H2 O)
HELIX 1 AA1 THR A 56 ALA A 62 1 7
HELIX 2 AA2 THR A 107 GLY A 111 5 5
HELIX 3 AA3 TRP A 115 SER A 122 1 8
HELIX 4 AA4 GLN A 138 ARG A 156 1 19
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 ALA A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O ILE A 86 N GLU A 72
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N VAL A 102 O PHE A 128
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O ASP A 166 N PHE A 97
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O LEU A 249 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O GLU A 297 N GLU A 248
SSBOND 1 CYS A 287 CYS A 302 1555 1555 2.04
LINK OD1 ASP A 204 CA CA A 401 1555 1555 2.44
LINK OD2 ASP A 204 CA CA A 401 1555 1555 2.49
LINK O THR A 206 CA CA A 401 1555 1555 2.42
LINK OG1 THR A 206 CA CA A 401 1555 1555 2.53
LINK OE1 GLU A 220 CA CA A 402 1555 1555 2.41
LINK OE2 GLU A 220 CA CA A 402 1555 1555 2.52
LINK OD1 ASP A 250 CA CA A 402 1555 1555 2.30
LINK OE1 GLU A 296 CA CA A 402 1555 1555 2.37
LINK CA CA A 401 O HOH A 624 1555 1555 2.49
LINK CA CA A 401 O HOH A 719 1555 1555 2.45
LINK CA CA A 401 O HOH A 723 1555 1555 2.38
LINK CA CA A 401 O HOH A 742 1555 1555 2.45
LINK CA CA A 402 O HOH A 518 1555 1545 2.41
LINK CA CA A 402 O HOH A 734 1555 1555 2.38
LINK CA CA A 402 O HOH A 741 1555 1545 2.37
CISPEP 1 CYS A 287 PRO A 288 0 0.27
CISPEP 2 CYS A 302 PRO A 303 0 -0.09
SITE 1 AC1 6 ASP A 204 THR A 206 HOH A 624 HOH A 719
SITE 2 AC1 6 HOH A 723 HOH A 742
SITE 1 AC2 6 GLU A 220 ASP A 250 GLU A 296 HOH A 518
SITE 2 AC2 6 HOH A 734 HOH A 741
CRYST1 36.420 49.101 122.950 90.00 90.00 90.00 P 21 21 21 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 0.027457 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008133 0.00000
TER 2066 TYR A 304
MASTER 316 0 2 11 9 0 4 6 2344 1 19 21
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