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HEADER HYDROLASE 10-MAR-19 6QZ1
TITLE STRUCTURE OF MHETASE FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN NBRC 110686 /
SOURCE 3 TISTR 2288 / 201-F6);
SOURCE 4 ORGANISM_TAXID: 1547922;
SOURCE 5 GENE: ISF6_0224;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCJ136
KEYWDS PLASTIC-BINDING PROTEIN, MHETASE, PET DEGRADATION, STRUCTURAL
KEYWDS 2 GENOMICS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 30-SEP-20 6QZ1 0
JRNL AUTH M.D.ALLEN,C.W.JOHNSON,B.C.KNOTT,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL STRUCTURE OF FROM MHETASE FROM IDEONELLA SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.620
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 70749
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) : 0.165
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6747
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 45.9980 - 5.2797 0.98 4227 222 0.1439 0.1427
REMARK 3 2 5.2797 - 4.1916 0.98 4189 255 0.1190 0.1371
REMARK 3 3 4.1916 - 3.6620 0.98 4261 171 0.1355 0.1713
REMARK 3 4 3.6620 - 3.3273 0.98 4179 249 0.1521 0.1787
REMARK 3 5 3.3273 - 3.0889 0.98 4287 174 0.1645 0.1831
REMARK 3 6 3.0889 - 2.9068 0.98 4231 246 0.1605 0.2061
REMARK 3 7 2.9068 - 2.7612 0.99 4226 233 0.1658 0.1851
REMARK 3 8 2.7612 - 2.6410 0.99 4301 186 0.1713 0.1760
REMARK 3 9 2.6410 - 2.5394 0.99 4313 222 0.1725 0.2131
REMARK 3 10 2.5394 - 2.4517 1.00 4264 258 0.1771 0.2123
REMARK 3 11 2.4517 - 2.3751 1.00 4298 184 0.1749 0.2077
REMARK 3 12 2.3751 - 2.3072 1.00 4274 238 0.1765 0.2031
REMARK 3 13 2.3072 - 2.2465 0.99 4275 231 0.1797 0.2165
REMARK 3 14 2.2465 - 2.1917 0.99 4268 222 0.1850 0.2187
REMARK 3 15 2.1917 - 2.1418 1.00 4276 210 0.1826 0.2332
REMARK 3 16 2.1418 - 2.0963 1.00 4353 244 0.1841 0.2143
REMARK 3 17 2.0963 - 2.0543 1.00 4296 206 0.1931 0.2277
REMARK 3 18 2.0543 - 2.0156 1.00 4338 211 0.1929 0.2183
REMARK 3 19 2.0156 - 1.9796 1.00 4244 257 0.1954 0.2746
REMARK 3 20 1.9796 - 1.9460 1.00 4275 224 0.2051 0.2460
REMARK 3 21 1.9460 - 1.9146 1.00 4292 206 0.2186 0.2714
REMARK 3 22 1.9146 - 1.8852 1.00 4313 217 0.2305 0.2484
REMARK 3 23 1.8852 - 1.8574 1.00 4323 244 0.2364 0.2750
REMARK 3 24 1.8574 - 1.8313 1.00 4228 272 0.2425 0.3020
REMARK 3 25 1.8313 - 1.8065 1.00 4336 210 0.2226 0.2643
REMARK 3 26 1.8065 - 1.7831 1.00 4280 277 0.2274 0.2639
REMARK 3 27 1.7831 - 1.7608 1.00 4252 232 0.2293 0.2238
REMARK 3 28 1.7608 - 1.7395 1.00 4288 235 0.2308 0.2650
REMARK 3 29 1.7395 - 1.7193 1.00 4301 225 0.2490 0.2976
REMARK 3 30 1.7193 - 1.7000 0.94 4088 186 0.2662 0.2575
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.870
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 : 0.008 4269
REMARK 3 ANGLE : 0.900 5820
REMARK 3 CHIRALITY : 0.055 610
REMARK 3 PLANARITY : 0.006 778
REMARK 3 DIHEDRAL : 3.956 3368
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 6QZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAR-20.
REMARK 100 THE DEPOSITION ID IS D_1292101164.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70855
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.58400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
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: 6QZ3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE (PH 5.5), 24% PEG
REMARK 280 5000 MME, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.93750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.99750
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.93750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.99750
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: 360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 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 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 A 875 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1324 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 ASP A 56
REMARK 465 GLY A 57
REMARK 465 ASN A 58
REMARK 465 GLY A 59
REMARK 465 ASP A 60
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 1297 O HOH A 1314 1.87
REMARK 500 O HOH A 1146 O HOH A 1225 1.88
REMARK 500 NZ LYS A 442 O HOH A 801 1.93
REMARK 500 O HOH A 1231 O HOH A 1246 1.98
REMARK 500 O HOH A 1091 O HOH A 1249 2.00
REMARK 500 OE2 GLU A 71 O HOH A 802 2.01
REMARK 500 O HOH A 1266 O HOH A 1296 2.05
REMARK 500 O HOH A 1195 O HOH A 1214 2.07
REMARK 500 O HOH A 1229 O HOH A 1304 2.09
REMARK 500 OD2 ASP A 465 O HOH A 803 2.11
REMARK 500 O HOH A 1213 O HOH A 1284 2.13
REMARK 500 NH1 ARG A 214 O HOH A 804 2.13
REMARK 500 O HOH A 1214 O HOH A 1248 2.14
REMARK 500 O HOH A 816 O HOH A 1310 2.15
REMARK 500 OD1 ASP A 77 O HOH A 805 2.16
REMARK 500 O PRO A 40 O HOH A 806 2.18
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 ASN A 134 -143.27 55.85
REMARK 500 LEU A 177 30.60 71.02
REMARK 500 TYR A 194 -29.34 -153.12
REMARK 500 SER A 225 -122.80 74.28
REMARK 500 ALA A 249 58.91 33.41
REMARK 500 ASP A 311 14.95 -146.61
REMARK 500 TYR A 373 -93.48 -141.76
REMARK 500 SER A 383 -144.32 -138.38
REMARK 500 SER A 491 32.63 -99.24
REMARK 500 ASN A 527 -154.18 -86.07
REMARK 500 CYS A 529 -22.25 68.23
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 A1352 DISTANCE = 6.53 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 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 71.5
REMARK 620 3 ASP A 307 OD1 70.2 135.7
REMARK 620 4 ASP A 307 OD2 74.3 135.6 49.1
REMARK 620 5 LEU A 309 O 84.0 80.6 74.0 122.9
REMARK 620 6 ASP A 311 OD1 145.7 74.6 137.0 137.2 85.7
REMARK 620 7 ILE A 313 O 97.3 80.4 125.8 76.7 159.5 81.9
REMARK 620 8 HOH A 829 O 141.5 146.8 73.2 73.0 97.2 72.3 94.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 702
DBREF1 6QZ1 A 40 603 UNP MHETH_IDESA
DBREF2 6QZ1 A A0A0K8P8E7 40 603
SEQRES 1 A 564 PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA CYS GLU
SEQRES 2 A 564 ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP PRO ASN
SEQRES 3 A 564 ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA
SEQRES 4 A 564 ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO GLU HIS
SEQRES 5 A 564 CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR GLY ILE
SEQRES 6 A 564 ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU ARG MET
SEQRES 7 A 564 PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU GLY GLY
SEQRES 8 A 564 SER GLY THR ASN GLY SER LEU SER ALA ALA THR GLY SER
SEQRES 9 A 564 ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER ARG ASN
SEQRES 10 A 564 PHE ALA THR ILE ALA THR ASP GLY GLY HIS ASP ASN ALA
SEQRES 11 A 564 VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL ALA PHE
SEQRES 12 A 564 GLY LEU ASP PRO GLN ALA ARG LEU ASP MET GLY TYR ASN
SEQRES 13 A 564 SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA ALA VAL
SEQRES 14 A 564 ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER TYR PHE
SEQRES 15 A 564 ILE GLY CYS SER GLU GLY GLY ARG GLU GLY MET MET LEU
SEQRES 16 A 564 SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE VAL ALA
SEQRES 17 A 564 GLY ALA PRO GLY TYR GLN LEU PRO LYS ALA GLY ILE SER
SEQRES 18 A 564 GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA ALA VAL
SEQRES 19 A 564 GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN LYS SER
SEQRES 20 A 564 PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN ALA ILE
SEQRES 21 A 564 LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY
SEQRES 22 A 564 ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP
SEQRES 23 A 564 PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU
SEQRES 24 A 564 GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU SER PRO
SEQRES 25 A 564 VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA GLY PRO
SEQRES 26 A 564 VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG TRP ALA
SEQRES 27 A 564 TRP ASP ALA GLY MET SER GLY LEU SER GLY THR THR TYR
SEQRES 28 A 564 ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER PHE ASN
SEQRES 29 A 564 SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY PHE SER
SEQRES 30 A 564 ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO PRO GLU
SEQRES 31 A 564 PRO MET PRO MET THR GLN VAL ALA ALA ARG MET MET LYS
SEQRES 32 A 564 PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP ALA THR
SEQRES 33 A 564 SER GLY GLN PHE THR GLN SER SER MET ASP TRP HIS GLY
SEQRES 34 A 564 ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP ARG GLY
SEQRES 35 A 564 GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP ALA ALA
SEQRES 36 A 564 PHE SER ALA LEU ASP THR ALA ASP TYR TYR GLU ARG LEU
SEQRES 37 A 564 GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA ARG LEU
SEQRES 38 A 564 PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY GLY PRO
SEQRES 39 A 564 GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU VAL ALA
SEQRES 40 A 564 TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE SER ALA
SEQRES 41 A 564 TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA ALA ARG
SEQRES 42 A 564 THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR
SEQRES 43 A 564 LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN PHE ALA
SEQRES 44 A 564 CYS ALA ALA PRO PRO
HET BEZ A 701 9
HET CA A 702 1
HETNAM BEZ BENZOIC ACID
HETNAM CA CALCIUM ION
FORMUL 2 BEZ C7 H6 O2
FORMUL 3 CA CA 2+
FORMUL 4 HOH *552(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SER A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 PHE A 287 5 6
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 GLY A 414 PHE A 424 1 11
HELIX 17 AB8 PRO A 432 THR A 434 5 3
HELIX 18 AB9 GLN A 435 LYS A 442 1 8
HELIX 19 AC1 ILE A 447 TRP A 453 5 7
HELIX 20 AC2 SER A 462 GLY A 468 1 7
HELIX 21 AC3 LEU A 474 ARG A 480 1 7
HELIX 22 AC4 SER A 496 MET A 511 1 16
HELIX 23 AC5 GLY A 513 GLY A 516 5 4
HELIX 24 AC6 MET A 540 GLY A 551 1 12
HELIX 25 AC7 THR A 563 GLY A 568 5 6
HELIX 26 AC8 THR A 593 ALA A 595 5 3
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O HIS A 91 N ARG A 76
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N ARG A 124 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O ARG A 519 N LEU A 486
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 2 ILE A 557 TRP A 560 0
SHEET 2 AA3 2 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 600 N ILE A 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.09
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.12
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.11
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.02
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.08
LINK O ASP A 304 CA CA A 702 1555 1555 2.49
LINK OD1 ASP A 304 CA CA A 702 1555 1555 2.42
LINK OD1 ASP A 307 CA CA A 702 1555 1555 2.72
LINK OD2 ASP A 307 CA CA A 702 1555 1555 2.56
LINK O LEU A 309 CA CA A 702 1555 1555 2.31
LINK OD1 ASP A 311 CA CA A 702 1555 1555 2.40
LINK O ILE A 313 CA CA A 702 1555 1555 2.39
LINK CA CA A 702 O HOH A 829 1555 1555 2.48
CISPEP 1 THR A 426 PRO A 427 0 -1.43
CISPEP 2 TYR A 579 PRO A 580 0 3.32
SITE 1 AC1 10 GLY A 132 SER A 225 LEU A 254 TRP A 397
SITE 2 AC1 10 ARG A 411 PHE A 415 SER A 416 PHE A 495
SITE 3 AC1 10 HOH A 814 HOH A 880
SITE 1 AC2 6 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC2 6 ILE A 313 HOH A 829
CRYST1 77.195 89.875 91.995 90.00 90.00 90.00 P 2 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 0.012954 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011127 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010870 0.00000
TER 4143 PRO A 603
MASTER 334 0 2 26 15 0 5 6 4691 1 29 44
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