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HEADER HYDROLASE 29-JUN-25 9VMW
TITLE THE CRYSTAL STRUCTURE OF THE PHTHALATE HYDROLASE ESTJ6 IN COMPLEX WITH
TITLE 2 PHTHALIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHTHALIC ACID ESTERS, PHTHALATE HYDROLASE, PHTHALIC ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.WANG,Y.B.CHEN,R.K.HU
REVDAT 1 08-JUL-26 9VMW 0
JRNL AUTH Y.B.CHEN,Y.H.WANG,R.K.HU
JRNL TITL CRYSTAL STRUCTURE OF THE PHTHALATE HYDROLASE ESTJ6 IN
JRNL TITL 2 COMPLEX WITH PHTHALIC ACID AT 1.9 ANGSTROMS RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30005
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) : 0.148
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.380
REMARK 3 FREE R VALUE TEST SET COUNT : 1013
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 37.6950 - 3.6337 1.00 4322 151 0.1336 0.1771
REMARK 3 2 3.6337 - 2.8845 1.00 4168 147 0.1509 0.1656
REMARK 3 3 2.8845 - 2.5199 1.00 4131 141 0.1581 0.2126
REMARK 3 4 2.5199 - 2.2896 1.00 4106 147 0.1557 0.1880
REMARK 3 5 2.2896 - 2.1255 1.00 4127 147 0.1497 0.1931
REMARK 3 6 2.1255 - 2.0002 1.00 4089 134 0.1619 0.1993
REMARK 3 7 2.0002 - 1.9000 1.00 4049 146 0.1786 0.2086
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) : 0.180
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 : 0.007 2235
REMARK 3 ANGLE : 1.004 3039
REMARK 3 CHIRALITY : 0.044 341
REMARK 3 PLANARITY : 0.006 397
REMARK 3 DIHEDRAL : 14.409 823
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 4 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0091 -11.6891 14.6145
REMARK 3 T TENSOR
REMARK 3 T11: 0.3368 T22: 0.5107
REMARK 3 T33: 0.4702 T12: 0.0861
REMARK 3 T13: 0.0908 T23: -0.0357
REMARK 3 L TENSOR
REMARK 3 L11: 3.0941 L22: 9.8297
REMARK 3 L33: 3.5404 L12: 2.1081
REMARK 3 L13: -1.0890 L23: -3.4873
REMARK 3 S TENSOR
REMARK 3 S11: 0.3713 S12: 0.4407 S13: 0.6760
REMARK 3 S21: 0.3573 S22: 0.1408 S23: 0.7503
REMARK 3 S31: -0.4712 S32: -0.5000 S33: -0.5145
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 46 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6565 -9.5636 18.3685
REMARK 3 T TENSOR
REMARK 3 T11: 0.4356 T22: 0.3987
REMARK 3 T33: 0.2950 T12: -0.0209
REMARK 3 T13: 0.0654 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 1.2506 L22: 8.0113
REMARK 3 L33: 6.3893 L12: -1.4629
REMARK 3 L13: 1.4958 L23: -7.1264
REMARK 3 S TENSOR
REMARK 3 S11: -0.0072 S12: -0.3109 S13: 0.0461
REMARK 3 S21: 0.8033 S22: 0.2705 S23: 0.5189
REMARK 3 S31: -0.5332 S32: -0.5346 S33: -0.2757
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 47 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5931 -18.6503 15.0681
REMARK 3 T TENSOR
REMARK 3 T11: 0.2127 T22: 0.2410
REMARK 3 T33: 0.2142 T12: -0.0178
REMARK 3 T13: -0.0299 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 2.1567 L22: 1.4735
REMARK 3 L33: 1.7653 L12: 0.5757
REMARK 3 L13: 0.0151 L23: -0.3952
REMARK 3 S TENSOR
REMARK 3 S11: 0.0767 S12: -0.3595 S13: -0.0431
REMARK 3 S21: 0.2552 S22: -0.1275 S23: -0.1012
REMARK 3 S31: -0.0412 S32: 0.0254 S33: 0.0614
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 183 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1497 -22.4692 3.7149
REMARK 3 T TENSOR
REMARK 3 T11: 0.1860 T22: 0.1943
REMARK 3 T33: 0.2216 T12: 0.0081
REMARK 3 T13: -0.0266 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.5728 L22: 1.8433
REMARK 3 L33: 0.8757 L12: 0.2071
REMARK 3 L13: -0.0777 L23: 0.2772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0219 S12: -0.0728 S13: -0.1102
REMARK 3 S21: -0.0087 S22: 0.0044 S23: -0.1331
REMARK 3 S31: 0.0675 S32: 0.0928 S33: -0.0351
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 230 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4161 -13.9442 -3.4999
REMARK 3 T TENSOR
REMARK 3 T11: 0.1938 T22: 0.1909
REMARK 3 T33: 0.2224 T12: 0.0256
REMARK 3 T13: -0.0254 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 1.2093 L22: 1.8840
REMARK 3 L33: 1.5542 L12: 0.2192
REMARK 3 L13: 0.3841 L23: 0.1543
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: 0.1833 S13: 0.0081
REMARK 3 S21: -0.2068 S22: -0.0510 S23: 0.2116
REMARK 3 S31: -0.1194 S32: -0.1684 S33: 0.0506
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 231 THROUGH 256 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.3547 -25.8567 -2.0834
REMARK 3 T TENSOR
REMARK 3 T11: 0.1903 T22: 0.2543
REMARK 3 T33: 0.2961 T12: -0.0175
REMARK 3 T13: -0.0488 T23: -0.0749
REMARK 3 L TENSOR
REMARK 3 L11: 3.3329 L22: 1.9500
REMARK 3 L33: 1.6548 L12: -1.9011
REMARK 3 L13: -1.0545 L23: -0.0684
REMARK 3 S TENSOR
REMARK 3 S11: 0.1039 S12: 0.3083 S13: -0.3903
REMARK 3 S21: -0.1368 S22: -0.1446 S23: 0.2856
REMARK 3 S31: 0.0560 S32: -0.2258 S33: 0.0955
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 257 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8446 -29.1290 11.0119
REMARK 3 T TENSOR
REMARK 3 T11: 0.2386 T22: 0.2400
REMARK 3 T33: 0.3110 T12: -0.0575
REMARK 3 T13: -0.0134 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.4201 L22: 0.6250
REMARK 3 L33: 1.8460 L12: 0.4526
REMARK 3 L13: -0.2273 L23: -0.1862
REMARK 3 S TENSOR
REMARK 3 S11: 0.0646 S12: -0.1149 S13: -0.2349
REMARK 3 S21: 0.1860 S22: -0.1322 S23: 0.1124
REMARK 3 S31: 0.2163 S32: -0.1669 S33: 0.0660
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 9VMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 30-JUN-25.
REMARK 100 THE DEPOSITION ID IS D_1300061063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-22
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35417
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 56.840
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 MOL/L CH2(CO2NA)2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.25400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.25400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 32.20850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.37900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.20850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.37900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.25400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.20850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.37900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.25400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.20850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.37900
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 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 554 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 721 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 ALA A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 HIS A 304
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 708 O HOH A 718 1.88
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 SER A 146 -113.64 58.17
REMARK 500 SER A 174 65.54 24.08
REMARK 500 ALA A 239 41.86 -98.78
REMARK 500 GLU A 267 -5.41 69.71
REMARK 500 VAL A 271 58.75 37.92
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9VMW A 1 298 UNP A0A4P8L7K3_9ZZZZ
DBREF2 9VMW A A0A4P8L7K3 1 298
SEQADV 9VMW GLN A 240 UNP A0A4P8L7K GLU 240 CONFLICT
SEQADV 9VMW HIS A 299 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMW HIS A 300 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMW HIS A 301 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMW HIS A 302 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMW HIS A 303 UNP A0A4P8L7K EXPRESSION TAG
SEQADV 9VMW HIS A 304 UNP A0A4P8L7K EXPRESSION TAG
SEQRES 1 A 304 MET ALA SER PRO GLN LEU GLN MET ALA LEU ASP ALA PHE
SEQRES 2 A 304 LYS THR MET GLY GLU LYS MET ALA GLN ALA GLY ASN ASP
SEQRES 3 A 304 VAL LYS ALA LEU ARG ALA VAL MET GLU GLU MET SER GLY
SEQRES 4 A 304 PHE PRO SER ALA GLY GLU THR LYS CYS THR PRO VAL ASN
SEQRES 5 A 304 ALA GLY GLY VAL PRO ALA GLU TRP ILE SER GLY PRO GLY
SEQRES 6 A 304 ALA ALA ASP ASP ARG VAL ILE LEU TYR VAL HIS GLY GLY
SEQRES 7 A 304 GLY TYR VAL MET GLY SER ILE ALA THR HIS ARG GLU THR
SEQRES 8 A 304 VAL ALA ARG LEU SER LYS ALA SER GLY ALA ARG GLY LEU
SEQRES 9 A 304 ALA LEU ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO
SEQRES 10 A 304 ALA ALA VAL ASP ASP ALA THR ALA ALA TYR ARG TRP LEU
SEQRES 11 A 304 LEU SER GLN ASN ILE LYS PRO ALA HIS ILE VAL ILE ALA
SEQRES 12 A 304 GLY ASP SER ALA GLY GLY GLY LEU THR LEU ALA THR LEU
SEQRES 13 A 304 ILE ALA LEU ARG ASP ALA LYS VAL PRO LEU PRO ALA ALA
SEQRES 14 A 304 GLY VAL CYS ILE SER PRO TRP THR ASP MET GLU GLY ALA
SEQRES 15 A 304 GLY GLU SER MET THR THR ARG ALA LYS ALA ASP PRO VAL
SEQRES 16 A 304 VAL GLN LYS GLN GLY LEU LEU GLY MET ALA GLN LEU TYR
SEQRES 17 A 304 LEU GLY GLY LYS ASP PRO LYS SER PRO LEU ALA ALA PRO
SEQRES 18 A 304 LEU HIS ALA ASN LEU ALA GLY LEU PRO PRO LEU LEU ILE
SEQRES 19 A 304 GLN VAL GLY ASP ALA GLN THR LEU LEU ASP ASP SER ILE
SEQRES 20 A 304 ARG VAL ALA GLU LYS ALA LYS LYS ALA GLY VAL LYS VAL
SEQRES 21 A 304 ASP LEU GLU VAL TRP PRO GLU MET PRO HIS VAL TRP HIS
SEQRES 22 A 304 LEU PHE ALA PRO PHE LEU PRO GLU GLY GLN GLN ALA ILE
SEQRES 23 A 304 ASP LYS ILE GLY LYS TYR VAL ARG GLN ILE THR ALA HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
HET PHT A 401 12
HETNAM PHT PHTHALIC ACID
FORMUL 2 PHT C8 H6 O4
FORMUL 3 HOH *246(H2 O)
HELIX 1 AA1 GLN A 5 GLY A 24 1 20
HELIX 2 AA2 ASP A 26 SER A 38 1 13
HELIX 3 AA3 SER A 42 THR A 46 5 5
HELIX 4 AA4 SER A 84 GLY A 100 1 17
HELIX 5 AA5 PRO A 117 GLN A 133 1 17
HELIX 6 AA6 LYS A 136 ALA A 138 5 3
HELIX 7 AA7 SER A 146 ALA A 162 1 17
HELIX 8 AA8 GLU A 184 ARG A 189 1 6
HELIX 9 AA9 GLN A 197 GLY A 210 1 14
HELIX 10 AB1 ALA A 220 ALA A 224 5 5
HELIX 11 AB2 LEU A 242 ALA A 256 1 15
HELIX 12 AB3 VAL A 271 ALA A 276 5 6
HELIX 13 AB4 LEU A 279 THR A 297 1 19
SHEET 1 AA1 8 LYS A 47 ALA A 53 0
SHEET 2 AA1 8 VAL A 56 SER A 62 -1 O TRP A 60 N THR A 49
SHEET 3 AA1 8 ALA A 101 LEU A 106 -1 O GLY A 103 N ILE A 61
SHEET 4 AA1 8 ALA A 67 VAL A 75 1 N ILE A 72 O LEU A 104
SHEET 5 AA1 8 ILE A 140 ASP A 145 1 O ALA A 143 N VAL A 75
SHEET 6 AA1 8 ALA A 169 ILE A 173 1 O ILE A 173 N GLY A 144
SHEET 7 AA1 8 LEU A 232 GLY A 237 1 O LEU A 233 N CYS A 172
SHEET 8 AA1 8 VAL A 260 TRP A 265 1 O TRP A 265 N VAL A 236
CISPEP 1 ALA A 111 PRO A 112 0 1.04
CISPEP 2 PHE A 116 PRO A 117 0 7.20
CRYST1 64.417 120.758 96.508 90.00 90.00 90.00 C 2 2 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 0.015524 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008281 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010362 0.00000
TER 2175 THR A 297
MASTER 372 0 1 13 8 0 0 6 2432 1 12 24
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