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HEADER PLANT PROTEIN 02-JUL-23 8JY1
TITLE STRUCTURE OF MANGIFERA INDICA EPOXIDE HYDROLASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MANGIFERA INDICA;
SOURCE 3 ORGANISM_COMMON: MANGO;
SOURCE 4 ORGANISM_TAXID: 29780;
SOURCE 5 GENE: EH2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEXP5-CT/TOPO
KEYWDS ALPHA-BETA HYDROLASE EPOXIDE HYDROLASE, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.BHOITE,V.S.GUPTA,K.A.KULKARNI
REVDAT 1 07-AUG-24 8JY1 0
JRNL AUTH A.S.BHOITE,V.S.GUPTA,K.A.KULKARNI
JRNL TITL STRUCTURE OF MANGIFERA INDICA EPOXIDE HYDROLASE 2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.19.2_4158: ???)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34350
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1654
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 47.6000 - 5.4900 1.00 2926 158 0.2020 0.2277
REMARK 3 2 5.4900 - 4.3600 1.00 2823 116 0.1542 0.1796
REMARK 3 3 4.3600 - 3.8100 1.00 2743 139 0.1458 0.1744
REMARK 3 4 3.8100 - 3.4600 1.00 2730 138 0.1568 0.1849
REMARK 3 5 3.4600 - 3.2100 1.00 2705 138 0.1619 0.1955
REMARK 3 6 3.2100 - 3.0200 1.00 2714 131 0.1712 0.2099
REMARK 3 7 3.0200 - 2.8700 1.00 2704 130 0.1782 0.1829
REMARK 3 8 2.8700 - 2.7500 1.00 2652 156 0.1870 0.2101
REMARK 3 9 2.7500 - 2.6400 1.00 2699 133 0.2006 0.2877
REMARK 3 10 2.6400 - 2.5500 1.00 2645 153 0.2092 0.2640
REMARK 3 11 2.5500 - 2.4700 1.00 2687 127 0.2185 0.2638
REMARK 3 12 2.4700 - 2.4000 1.00 2668 135 0.2243 0.2596
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.710
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 : 0.002 4496
REMARK 3 ANGLE : 0.459 6118
REMARK 3 CHIRALITY : 0.045 647
REMARK 3 PLANARITY : 0.004 784
REMARK 3 DIHEDRAL : 10.896 1584
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): 16.8600 40.1446 59.7091
REMARK 3 T TENSOR
REMARK 3 T11: 0.1041 T22: 0.0330
REMARK 3 T33: 0.1311 T12: -0.0213
REMARK 3 T13: -0.0071 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.8212 L22: 1.0002
REMARK 3 L33: 2.0364 L12: -0.4764
REMARK 3 L13: 0.5659 L23: -1.3185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0641 S12: 0.1503 S13: -0.0254
REMARK 3 S21: -0.0850 S22: -0.0270 S23: 0.0511
REMARK 3 S31: 0.0780 S32: 0.2272 S33: 0.0433
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 8JY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-23.
REMARK 100 THE DEPOSITION ID IS D_1300038954.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 11.2C
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34442
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 47.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 13.20
REMARK 200 R MERGE FOR SHELL (I) : 0.90700
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 (%): 56.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE, 0.2M AMMONIUM
REMARK 280 ACETATE, 30%W/V PEG 4000, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 86.39200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.52000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.52000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 129.58800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.52000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.52000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.19600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.52000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.52000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 129.58800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.52000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.52000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.19600
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 86.39200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 ASP B 3
REMARK 465 PRO B 139
REMARK 465 LEU B 140
REMARK 465 GLU B 141
REMARK 465 GLY B 142
REMARK 465 LEU B 143
REMARK 465 LYS B 144
REMARK 465 ALA B 145
REMARK 465 VAL B 146
REMARK 465 TYR B 147
REMARK 465 GLY B 148
REMARK 465 ASP B 149
REMARK 465 ASP B 150
REMARK 465 TYR B 151
REMARK 465 TYR B 152
REMARK 465 MET B 153
REMARK 465 ILE B 154
REMARK 465 ARG B 155
REMARK 465 PHE B 156
REMARK 465 GLN B 157
REMARK 465 GLU B 158
REMARK 465 PRO B 159
REMARK 465 GLY B 160
REMARK 465 GLU B 161
REMARK 465 ILE B 162
REMARK 465 GLU B 163
REMARK 465 ALA B 164
REMARK 465 GLU B 165
REMARK 465 PHE B 166
REMARK 465 ALA B 167
REMARK 465 GLN B 168
REMARK 465 ILE B 169
REMARK 465 GLY B 170
REMARK 465 THR B 171
REMARK 465 GLU B 172
REMARK 465 THR B 173
REMARK 465 VAL B 174
REMARK 465 VAL B 175
REMARK 465 LYS B 176
REMARK 465 GLU B 177
REMARK 465 PHE B 178
REMARK 465 PHE B 179
REMARK 465 THR B 180
REMARK 465 TYR B 181
REMARK 465 ARG B 182
REMARK 465 THR B 183
REMARK 465 PRO B 184
REMARK 465 GLY B 185
REMARK 465 PRO B 186
REMARK 465 LEU B 187
REMARK 465 PHE B 188
REMARK 465 LEU B 189
REMARK 465 PRO B 190
REMARK 465 THR B 191
REMARK 465 GLY B 192
REMARK 465 LYS B 193
REMARK 465 GLY B 194
REMARK 465 PHE B 195
REMARK 465 GLY B 196
REMARK 465 HIS B 197
REMARK 465 PRO B 198
REMARK 465 PRO B 199
REMARK 465 ASN B 200
REMARK 465 ALA B 201
REMARK 465 GLU B 202
REMARK 465 ILE B 203
REMARK 465 VAL B 204
REMARK 465 LEU B 205
REMARK 465 PRO B 206
REMARK 465 SER B 207
REMARK 465 TRP B 208
REMARK 465 LEU B 209
REMARK 465 SER B 210
REMARK 465 GLU B 211
REMARK 465 ASP B 212
REMARK 465 ASP B 213
REMARK 465 VAL B 214
REMARK 465 LYS B 215
REMARK 465 ASN B 216
REMARK 465 TYR B 217
REMARK 465 THR B 218
REMARK 465 SER B 219
REMARK 465 LYS B 220
REMARK 465 PHE B 221
REMARK 465 GLU B 222
REMARK 465 LYS B 223
REMARK 465 GLY B 224
REMARK 465 PHE B 225
REMARK 465 GLY B 320
REMARK 465 HIS B 321
REMARK 465 HIS B 322
REMARK 465 HIS B 323
REMARK 465 HIS B 324
REMARK 465 HIS B 325
REMARK 465 HIS B 326
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 LYS A 215 CD CE NZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 TYR B 38 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 94 CZ NH1 NH2
REMARK 470 LYS B 136 CG CD CE NZ
REMARK 470 ARG B 137 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 138 CG CD CE NZ
REMARK 470 LEU B 263 CG CD1 CD2
REMARK 470 LYS B 319 CG CD CE NZ
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 46 13.87 -68.11
REMARK 500 ALA A 91 47.78 -148.70
REMARK 500 ASP A 103 -130.59 62.72
REMARK 500 SER A 127 -60.78 74.35
REMARK 500 ALA B 91 52.06 -151.87
REMARK 500 ASP B 103 -125.35 58.51
REMARK 500 SER B 127 -45.62 73.93
REMARK 500 LYS B 303 61.56 -117.32
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 708 DISTANCE = 6.06 ANGSTROMS
DBREF1 8JY1 A 3 318 UNP A0A1U9ZCB5_MANIN
DBREF2 8JY1 A A0A1U9ZCB5 3 318
DBREF1 8JY1 B 3 318 UNP A0A1U9ZCB5_MANIN
DBREF2 8JY1 B A0A1U9ZCB5 3 318
SEQADV 8JY1 LYS A 319 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 GLY A 320 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS A 321 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS A 322 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS A 323 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS A 324 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS A 325 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS A 326 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 LYS B 319 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 GLY B 320 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS B 321 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS B 322 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS B 323 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS B 324 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS B 325 UNP A0A1U9ZCB EXPRESSION TAG
SEQADV 8JY1 HIS B 326 UNP A0A1U9ZCB EXPRESSION TAG
SEQRES 1 A 324 ASP ILE GLN HIS ARG ILE VAL ASN VAL ASN GLY LEU ASN
SEQRES 2 A 324 MET HIS VAL ALA GLU LYS GLY GLU GLY PRO VAL ILE LEU
SEQRES 3 A 324 PHE ILE HIS GLY PHE PRO GLU LEU TRP TYR SER TRP ARG
SEQRES 4 A 324 HIS GLN ILE ILE ALA LEU ALA SER LEU GLY TYR ARG ALA
SEQRES 5 A 324 ILE ALA PRO ASP LEU ARG GLY PHE GLY ASP THR ASP ALA
SEQRES 6 A 324 PRO PRO SER VAL SER SER TYR THR CYS PHE HIS VAL VAL
SEQRES 7 A 324 GLY ASP LEU ILE GLY LEU LEU ASP VAL VAL ALA SER ASP
SEQRES 8 A 324 ARG ASP LYS VAL PHE VAL VAL GLY HIS ASP TRP GLY ALA
SEQRES 9 A 324 LEU ILE ALA TRP TYR LEU CYS LEU PHE ARG PRO ASP LYS
SEQRES 10 A 324 VAL LYS ALA LEU VAL ASN LEU SER VAL ALA PHE ASN PRO
SEQRES 11 A 324 TRP ASN PRO LYS ARG LYS PRO LEU GLU GLY LEU LYS ALA
SEQRES 12 A 324 VAL TYR GLY ASP ASP TYR TYR MET ILE ARG PHE GLN GLU
SEQRES 13 A 324 PRO GLY GLU ILE GLU ALA GLU PHE ALA GLN ILE GLY THR
SEQRES 14 A 324 GLU THR VAL VAL LYS GLU PHE PHE THR TYR ARG THR PRO
SEQRES 15 A 324 GLY PRO LEU PHE LEU PRO THR GLY LYS GLY PHE GLY HIS
SEQRES 16 A 324 PRO PRO ASN ALA GLU ILE VAL LEU PRO SER TRP LEU SER
SEQRES 17 A 324 GLU ASP ASP VAL LYS ASN TYR THR SER LYS PHE GLU LYS
SEQRES 18 A 324 GLY PHE THR GLY GLY VAL ASN TYR TYR ARG ASN ILE ASN
SEQRES 19 A 324 VAL ASN TRP GLU LEU THR ALA PRO TRP ALA GLY SER GLN
SEQRES 20 A 324 ILE LYS VAL PRO VAL LYS PHE ILE VAL GLY ASP LEU ASP
SEQRES 21 A 324 LEU THR TYR TYR MET PRO GLY VAL LYS ASP TYR ILE HIS
SEQRES 22 A 324 LYS GLY GLY PHE LYS ARG ASP VAL PRO LEU LEU GLU GLU
SEQRES 23 A 324 VAL ILE VAL MET GLU GLY VAL GLY HIS PHE ILE ASN GLY
SEQRES 24 A 324 GLU LYS ALA ASP ALA ILE SER GLU HIS ILE TYR ASN PHE
SEQRES 25 A 324 PHE GLN LYS PHE LYS GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 324 ASP ILE GLN HIS ARG ILE VAL ASN VAL ASN GLY LEU ASN
SEQRES 2 B 324 MET HIS VAL ALA GLU LYS GLY GLU GLY PRO VAL ILE LEU
SEQRES 3 B 324 PHE ILE HIS GLY PHE PRO GLU LEU TRP TYR SER TRP ARG
SEQRES 4 B 324 HIS GLN ILE ILE ALA LEU ALA SER LEU GLY TYR ARG ALA
SEQRES 5 B 324 ILE ALA PRO ASP LEU ARG GLY PHE GLY ASP THR ASP ALA
SEQRES 6 B 324 PRO PRO SER VAL SER SER TYR THR CYS PHE HIS VAL VAL
SEQRES 7 B 324 GLY ASP LEU ILE GLY LEU LEU ASP VAL VAL ALA SER ASP
SEQRES 8 B 324 ARG ASP LYS VAL PHE VAL VAL GLY HIS ASP TRP GLY ALA
SEQRES 9 B 324 LEU ILE ALA TRP TYR LEU CYS LEU PHE ARG PRO ASP LYS
SEQRES 10 B 324 VAL LYS ALA LEU VAL ASN LEU SER VAL ALA PHE ASN PRO
SEQRES 11 B 324 TRP ASN PRO LYS ARG LYS PRO LEU GLU GLY LEU LYS ALA
SEQRES 12 B 324 VAL TYR GLY ASP ASP TYR TYR MET ILE ARG PHE GLN GLU
SEQRES 13 B 324 PRO GLY GLU ILE GLU ALA GLU PHE ALA GLN ILE GLY THR
SEQRES 14 B 324 GLU THR VAL VAL LYS GLU PHE PHE THR TYR ARG THR PRO
SEQRES 15 B 324 GLY PRO LEU PHE LEU PRO THR GLY LYS GLY PHE GLY HIS
SEQRES 16 B 324 PRO PRO ASN ALA GLU ILE VAL LEU PRO SER TRP LEU SER
SEQRES 17 B 324 GLU ASP ASP VAL LYS ASN TYR THR SER LYS PHE GLU LYS
SEQRES 18 B 324 GLY PHE THR GLY GLY VAL ASN TYR TYR ARG ASN ILE ASN
SEQRES 19 B 324 VAL ASN TRP GLU LEU THR ALA PRO TRP ALA GLY SER GLN
SEQRES 20 B 324 ILE LYS VAL PRO VAL LYS PHE ILE VAL GLY ASP LEU ASP
SEQRES 21 B 324 LEU THR TYR TYR MET PRO GLY VAL LYS ASP TYR ILE HIS
SEQRES 22 B 324 LYS GLY GLY PHE LYS ARG ASP VAL PRO LEU LEU GLU GLU
SEQRES 23 B 324 VAL ILE VAL MET GLU GLY VAL GLY HIS PHE ILE ASN GLY
SEQRES 24 B 324 GLU LYS ALA ASP ALA ILE SER GLU HIS ILE TYR ASN PHE
SEQRES 25 B 324 PHE GLN LYS PHE LYS GLY HIS HIS HIS HIS HIS HIS
HET PG4 A 401 13
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *286(H2 O)
HELIX 1 AA1 LEU A 36 SER A 39 5 4
HELIX 2 AA2 TRP A 40 SER A 49 1 10
HELIX 3 AA3 SER A 70 TYR A 74 5 5
HELIX 4 AA4 THR A 75 ALA A 91 1 17
HELIX 5 AA5 ASP A 103 ARG A 116 1 14
HELIX 6 AA6 LYS A 138 GLY A 148 1 11
HELIX 7 AA7 TYR A 151 PHE A 156 1 6
HELIX 8 AA8 GLY A 160 GLY A 170 1 11
HELIX 9 AA9 GLY A 170 THR A 180 1 11
HELIX 10 AB1 SER A 210 GLU A 222 1 13
HELIX 11 AB2 PHE A 225 ASN A 234 1 10
HELIX 12 AB3 ASN A 234 THR A 242 1 9
HELIX 13 AB4 ALA A 243 ALA A 246 5 4
HELIX 14 AB5 ASP A 262 MET A 267 5 6
HELIX 15 AB6 GLY A 269 LYS A 276 1 8
HELIX 16 AB7 GLY A 277 VAL A 283 1 7
HELIX 17 AB8 PHE A 298 LYS A 303 1 6
HELIX 18 AB9 LYS A 303 GLN A 316 1 14
HELIX 19 AC1 LYS A 317 LYS A 319 5 3
HELIX 20 AC2 LEU B 36 SER B 39 5 4
HELIX 21 AC3 TRP B 40 LEU B 50 1 11
HELIX 22 AC4 SER B 70 TYR B 74 5 5
HELIX 23 AC5 THR B 75 ALA B 91 1 17
HELIX 24 AC6 ASP B 103 ARG B 116 1 14
HELIX 25 AC7 GLY B 227 ARG B 233 1 7
HELIX 26 AC8 ASN B 234 THR B 242 1 9
HELIX 27 AC9 ALA B 243 ALA B 246 5 4
HELIX 28 AD1 LEU B 263 MET B 267 5 5
HELIX 29 AD2 GLY B 269 LYS B 276 1 8
HELIX 30 AD3 GLY B 277 VAL B 283 1 7
HELIX 31 AD4 PHE B 298 LYS B 303 1 6
HELIX 32 AD5 LYS B 303 LYS B 317 1 15
SHEET 1 AA1 8 GLN A 5 VAL A 11 0
SHEET 2 AA1 8 LEU A 14 LYS A 21 -1 O MET A 16 N VAL A 9
SHEET 3 AA1 8 ARG A 53 PRO A 57 -1 O ALA A 56 N ALA A 19
SHEET 4 AA1 8 VAL A 26 ILE A 30 1 N ILE A 27 O ILE A 55
SHEET 5 AA1 8 VAL A 97 HIS A 102 1 O PHE A 98 N LEU A 28
SHEET 6 AA1 8 VAL A 120 LEU A 126 1 O LYS A 121 N VAL A 97
SHEET 7 AA1 8 VAL A 254 GLY A 259 1 O LYS A 255 N LEU A 123
SHEET 8 AA1 8 LEU A 286 MET A 292 1 O ILE A 290 N PHE A 256
SHEET 1 AA2 8 GLN B 5 VAL B 11 0
SHEET 2 AA2 8 LEU B 14 GLY B 22 -1 O MET B 16 N VAL B 9
SHEET 3 AA2 8 ARG B 53 PRO B 57 -1 O ALA B 56 N ALA B 19
SHEET 4 AA2 8 VAL B 26 ILE B 30 1 N ILE B 27 O ILE B 55
SHEET 5 AA2 8 VAL B 97 HIS B 102 1 O PHE B 98 N LEU B 28
SHEET 6 AA2 8 VAL B 120 LEU B 126 1 O LYS B 121 N VAL B 97
SHEET 7 AA2 8 VAL B 254 GLY B 259 1 O LYS B 255 N LEU B 123
SHEET 8 AA2 8 LEU B 286 MET B 292 1 O ILE B 290 N PHE B 256
CISPEP 1 PHE A 33 PRO A 34 0 -7.57
CISPEP 2 PHE B 33 PRO B 34 0 -4.09
CRYST1 99.040 99.040 172.784 90.00 90.00 90.00 P 43 21 2 16
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 0.010097 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010097 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005788 0.00000
TER 2534 LYS A 319
TER 4337 LYS B 319
MASTER 399 0 1 32 16 0 0 6 4633 2 13 50
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