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HEADER HYDROLASE 27-SEP-22 8B6P
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7 CIRCULAR
TITLE 2 PERMUTATED AT POSITIONS 154-156 (CPHALOTAG7_154-156)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALOTAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
REVDAT 1 11-OCT-23 8B6P 0
JRNL AUTH M.TARNAWSKI,K.JOHNSSON,J.HIBLOT
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7
JRNL TITL 2 CIRCULAR PERMUTATED AT POSITIONS 154-156
JRNL TITL 3 (CPHALOTAG7_154-156)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.10 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 251832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.149
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 12591
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 42.7900 - 3.4200 0.97 8603 453 0.1581 0.1571
REMARK 3 2 3.4200 - 2.7100 0.98 8398 441 0.1707 0.1748
REMARK 3 3 2.7100 - 2.3700 0.97 8227 433 0.1623 0.1781
REMARK 3 4 2.3700 - 2.1500 0.97 8227 433 0.1487 0.1478
REMARK 3 5 2.1500 - 2.0000 0.97 8210 433 0.1428 0.1457
REMARK 3 6 2.0000 - 1.8800 0.98 8216 432 0.1428 0.1533
REMARK 3 7 1.8800 - 1.7900 0.98 8184 431 0.1389 0.1465
REMARK 3 8 1.7900 - 1.7100 0.96 8101 426 0.1269 0.1332
REMARK 3 9 1.7100 - 1.6400 0.97 8112 427 0.1226 0.1441
REMARK 3 10 1.6400 - 1.5900 0.97 8138 428 0.1140 0.1311
REMARK 3 11 1.5900 - 1.5400 0.97 8110 427 0.1126 0.1290
REMARK 3 12 1.5400 - 1.4900 0.97 8110 427 0.1113 0.1341
REMARK 3 13 1.4900 - 1.4500 0.97 8073 425 0.1143 0.1353
REMARK 3 14 1.4500 - 1.4200 0.97 8064 424 0.1174 0.1411
REMARK 3 15 1.4200 - 1.3900 0.96 7995 421 0.1136 0.1400
REMARK 3 16 1.3900 - 1.3600 0.96 8012 422 0.1155 0.1459
REMARK 3 17 1.3600 - 1.3300 0.96 8001 421 0.1135 0.1340
REMARK 3 18 1.3300 - 1.3000 0.96 7990 420 0.1094 0.1287
REMARK 3 19 1.3000 - 1.2800 0.96 8027 423 0.1121 0.1311
REMARK 3 20 1.2800 - 1.2600 0.96 7957 419 0.1101 0.1292
REMARK 3 21 1.2600 - 1.2400 0.96 7980 420 0.1105 0.1318
REMARK 3 22 1.2400 - 1.2200 0.95 7864 414 0.1119 0.1365
REMARK 3 23 1.2200 - 1.2000 0.95 7895 415 0.1122 0.1378
REMARK 3 24 1.2000 - 1.1800 0.95 7904 416 0.1136 0.1367
REMARK 3 25 1.1800 - 1.1700 0.95 7845 413 0.1105 0.1406
REMARK 3 26 1.1700 - 1.1500 0.94 7861 414 0.1126 0.1499
REMARK 3 27 1.1500 - 1.1400 0.94 7808 411 0.1088 0.1348
REMARK 3 28 1.1400 - 1.1300 0.93 7656 403 0.1115 0.1299
REMARK 3 29 1.1300 - 1.1100 0.88 7277 383 0.1150 0.1370
REMARK 3 30 1.1100 - 1.1000 0.77 6396 336 0.1251 0.1421
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) : 0.065
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.647
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.99
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 4897
REMARK 3 ANGLE : 1.165 6696
REMARK 3 CHIRALITY : 0.098 707
REMARK 3 PLANARITY : 0.013 883
REMARK 3 DIHEDRAL : 5.611 644
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 8B6P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1292125779.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99986
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 251839
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
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 (%) : 95.4
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.17400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 8.490
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: 5Y2X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE PH 9.0, 1.6 M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, 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 34.43500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.05500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.05500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.43500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.33000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 142
REMARK 465 GLY A 143
REMARK 465 THR A 144
REMARK 465 GLY A 145
REMARK 465 GLY A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
REMARK 465 GLY A 149
REMARK 465 THR A 150
REMARK 465 GLY A 151
REMARK 465 GLY A 152
REMARK 465 SER A 153
REMARK 465 GLY A 154
REMARK 465 GLY A 155
REMARK 465 SER A 156
REMARK 465 THR B 144
REMARK 465 GLY B 145
REMARK 465 GLY B 146
REMARK 465 SER B 147
REMARK 465 GLY B 148
REMARK 465 GLY B 149
REMARK 465 THR B 150
REMARK 465 GLY B 151
REMARK 465 GLY B 152
REMARK 465 SER B 153
REMARK 465 GLY B 154
REMARK 465 GLY B 155
REMARK 465 SER B 156
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 VAL A 91 -66.75 -130.80
REMARK 500 LEU A 117 -101.27 -117.50
REMARK 500 PRO A 162 49.62 -88.86
REMARK 500 GLU A 251 -95.76 -106.97
REMARK 500 ASP A 259 -136.63 60.13
REMARK 500 VAL B 91 -69.43 -130.47
REMARK 500 LEU B 117 -100.74 -117.69
REMARK 500 GLU B 251 -93.79 -108.80
REMARK 500 ASP B 259 -136.75 59.12
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 B 848 DISTANCE = 6.39 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8B6N RELATED DB: PDB
REMARK 900 RELATED ID: 8B6O RELATED DB: PDB
REMARK 900 RELATED ID: 8B6Q RELATED DB: PDB
DBREF 8B6P A 2 139 UNP P0A3G3 DHAA_RHOSO 156 293
DBREF 8B6P A 157 307 UNP P0A3G3 DHAA_RHOSO 4 154
DBREF 8B6P B 2 139 UNP P0A3G3 DHAA_RHOSO 156 293
DBREF 8B6P B 157 307 UNP P0A3G3 DHAA_RHOSO 4 154
SEQADV 8B6P GLY A -1 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6P GLY A 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6P GLY A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6P LYS A 6 UNP P0A3G3 GLU 160 CONFLICT
SEQADV 8B6P VAL A 13 UNP P0A3G3 ALA 167 CONFLICT
SEQADV 8B6P THR A 18 UNP P0A3G3 ALA 172 CONFLICT
SEQADV 8B6P MET A 21 UNP P0A3G3 LYS 175 CONFLICT
SEQADV 8B6P GLY A 22 UNP P0A3G3 CYS 176 CONFLICT
SEQADV 8B6P ASN A 41 UNP P0A3G3 LYS 195 CONFLICT
SEQADV 8B6P GLU A 70 UNP P0A3G3 ALA 224 CONFLICT
SEQADV 8B6P ASP A 73 UNP P0A3G3 ASN 227 CONFLICT
SEQADV 8B6P LYS A 103 UNP P0A3G3 GLU 257 CONFLICT
SEQADV 8B6P ALA A 110 UNP P0A3G3 THR 264 CONFLICT
SEQADV 8B6P ASN A 118 UNP P0A3G3 HIS 272 CONFLICT
SEQADV 8B6P LEU A 119 UNP P0A3G3 TYR 273 CONFLICT
SEQADV 8B6P SER A 137 UNP P0A3G3 PRO 291 CONFLICT
SEQADV 8B6P THR A 138 UNP P0A3G3 ALA 292 CONFLICT
SEQADV 8B6P GLU A 140 UNP P0A3G3 LINKER
SEQADV 8B6P ILE A 141 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 142 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 143 UNP P0A3G3 LINKER
SEQADV 8B6P THR A 144 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 145 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 146 UNP P0A3G3 LINKER
SEQADV 8B6P SER A 147 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 148 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 149 UNP P0A3G3 LINKER
SEQADV 8B6P THR A 150 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 151 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 152 UNP P0A3G3 LINKER
SEQADV 8B6P SER A 153 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 154 UNP P0A3G3 LINKER
SEQADV 8B6P GLY A 155 UNP P0A3G3 LINKER
SEQADV 8B6P SER A 156 UNP P0A3G3 LINKER
SEQADV 8B6P VAL A 200 UNP P0A3G3 LEU 47 CONFLICT
SEQADV 8B6P THR A 211 UNP P0A3G3 SER 58 CONFLICT
SEQADV 8B6P GLY A 231 UNP P0A3G3 ASP 78 CONFLICT
SEQADV 8B6P PHE A 240 UNP P0A3G3 TYR 87 CONFLICT
SEQADV 8B6P MET A 241 UNP P0A3G3 LEU 88 CONFLICT
SEQADV 8B6P PHE A 281 UNP P0A3G3 CYS 128 CONFLICT
SEQADV 8B6P GLY B -1 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6P GLY B 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6P GLY B 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 8B6P LYS B 6 UNP P0A3G3 GLU 160 CONFLICT
SEQADV 8B6P VAL B 13 UNP P0A3G3 ALA 167 CONFLICT
SEQADV 8B6P THR B 18 UNP P0A3G3 ALA 172 CONFLICT
SEQADV 8B6P MET B 21 UNP P0A3G3 LYS 175 CONFLICT
SEQADV 8B6P GLY B 22 UNP P0A3G3 CYS 176 CONFLICT
SEQADV 8B6P ASN B 41 UNP P0A3G3 LYS 195 CONFLICT
SEQADV 8B6P GLU B 70 UNP P0A3G3 ALA 224 CONFLICT
SEQADV 8B6P ASP B 73 UNP P0A3G3 ASN 227 CONFLICT
SEQADV 8B6P LYS B 103 UNP P0A3G3 GLU 257 CONFLICT
SEQADV 8B6P ALA B 110 UNP P0A3G3 THR 264 CONFLICT
SEQADV 8B6P ASN B 118 UNP P0A3G3 HIS 272 CONFLICT
SEQADV 8B6P LEU B 119 UNP P0A3G3 TYR 273 CONFLICT
SEQADV 8B6P SER B 137 UNP P0A3G3 PRO 291 CONFLICT
SEQADV 8B6P THR B 138 UNP P0A3G3 ALA 292 CONFLICT
SEQADV 8B6P GLU B 140 UNP P0A3G3 LINKER
SEQADV 8B6P ILE B 141 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 142 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 143 UNP P0A3G3 LINKER
SEQADV 8B6P THR B 144 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 145 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 146 UNP P0A3G3 LINKER
SEQADV 8B6P SER B 147 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 148 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 149 UNP P0A3G3 LINKER
SEQADV 8B6P THR B 150 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 151 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 152 UNP P0A3G3 LINKER
SEQADV 8B6P SER B 153 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 154 UNP P0A3G3 LINKER
SEQADV 8B6P GLY B 155 UNP P0A3G3 LINKER
SEQADV 8B6P SER B 156 UNP P0A3G3 LINKER
SEQADV 8B6P VAL B 200 UNP P0A3G3 LEU 47 CONFLICT
SEQADV 8B6P THR B 211 UNP P0A3G3 SER 58 CONFLICT
SEQADV 8B6P GLY B 231 UNP P0A3G3 ASP 78 CONFLICT
SEQADV 8B6P PHE B 240 UNP P0A3G3 TYR 87 CONFLICT
SEQADV 8B6P MET B 241 UNP P0A3G3 LEU 88 CONFLICT
SEQADV 8B6P PHE B 281 UNP P0A3G3 CYS 128 CONFLICT
SEQRES 1 A 309 GLY GLY GLY ASP VAL GLY ARG LYS LEU ILE ILE ASP GLN
SEQRES 2 A 309 ASN VAL PHE ILE GLU GLY THR LEU PRO MET GLY VAL VAL
SEQRES 3 A 309 ARG PRO LEU THR GLU VAL GLU MET ASP HIS TYR ARG GLU
SEQRES 4 A 309 PRO PHE LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP ARG
SEQRES 5 A 309 PHE PRO ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA ASN
SEQRES 6 A 309 ILE VAL ALA LEU VAL GLU GLU TYR MET ASP TRP LEU HIS
SEQRES 7 A 309 GLN SER PRO VAL PRO LYS LEU LEU PHE TRP GLY THR PRO
SEQRES 8 A 309 GLY VAL LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU ALA
SEQRES 9 A 309 LYS SER LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY PRO
SEQRES 10 A 309 GLY LEU ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU ILE
SEQRES 11 A 309 GLY SER GLU ILE ALA ARG TRP LEU SER THR LEU GLU ILE
SEQRES 12 A 309 GLY GLY THR GLY GLY SER GLY GLY THR GLY GLY SER GLY
SEQRES 13 A 309 GLY SER ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR
SEQRES 14 A 309 VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL
SEQRES 15 A 309 GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY
SEQRES 16 A 309 ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO
SEQRES 17 A 309 HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU
SEQRES 18 A 309 ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR
SEQRES 19 A 309 PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE
SEQRES 20 A 309 GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS
SEQRES 21 A 309 ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG
SEQRES 22 A 309 ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE
SEQRES 23 A 309 ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE
SEQRES 24 A 309 ALA ARG GLU THR PHE GLN ALA PHE ARG THR
SEQRES 1 B 309 GLY GLY GLY ASP VAL GLY ARG LYS LEU ILE ILE ASP GLN
SEQRES 2 B 309 ASN VAL PHE ILE GLU GLY THR LEU PRO MET GLY VAL VAL
SEQRES 3 B 309 ARG PRO LEU THR GLU VAL GLU MET ASP HIS TYR ARG GLU
SEQRES 4 B 309 PRO PHE LEU ASN PRO VAL ASP ARG GLU PRO LEU TRP ARG
SEQRES 5 B 309 PHE PRO ASN GLU LEU PRO ILE ALA GLY GLU PRO ALA ASN
SEQRES 6 B 309 ILE VAL ALA LEU VAL GLU GLU TYR MET ASP TRP LEU HIS
SEQRES 7 B 309 GLN SER PRO VAL PRO LYS LEU LEU PHE TRP GLY THR PRO
SEQRES 8 B 309 GLY VAL LEU ILE PRO PRO ALA GLU ALA ALA ARG LEU ALA
SEQRES 9 B 309 LYS SER LEU PRO ASN CYS LYS ALA VAL ASP ILE GLY PRO
SEQRES 10 B 309 GLY LEU ASN LEU LEU GLN GLU ASP ASN PRO ASP LEU ILE
SEQRES 11 B 309 GLY SER GLU ILE ALA ARG TRP LEU SER THR LEU GLU ILE
SEQRES 12 B 309 GLY GLY THR GLY GLY SER GLY GLY THR GLY GLY SER GLY
SEQRES 13 B 309 GLY SER ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR
SEQRES 14 B 309 VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL
SEQRES 15 B 309 GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY
SEQRES 16 B 309 ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO
SEQRES 17 B 309 HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU
SEQRES 18 B 309 ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR
SEQRES 19 B 309 PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE
SEQRES 20 B 309 GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS
SEQRES 21 B 309 ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG
SEQRES 22 B 309 ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE
SEQRES 23 B 309 ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE
SEQRES 24 B 309 ALA ARG GLU THR PHE GLN ALA PHE ARG THR
HET CL A 400 1
HET CL B 400 1
HETNAM CL CHLORIDE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *680(H2 O)
HELIX 1 AA1 GLY A 1 ILE A 9 1 9
HELIX 2 AA2 ASN A 12 GLY A 17 1 6
HELIX 3 AA3 GLY A 17 GLY A 22 1 6
HELIX 4 AA4 THR A 28 GLU A 37 1 10
HELIX 5 AA5 PRO A 38 LEU A 40 5 3
HELIX 6 AA6 ASN A 41 ASP A 44 5 4
HELIX 7 AA7 ARG A 45 LEU A 55 1 11
HELIX 8 AA8 PRO A 61 SER A 78 1 18
HELIX 9 AA9 PRO A 94 LEU A 105 1 12
HELIX 10 AB1 LEU A 119 ASN A 124 1 6
HELIX 11 AB2 ASN A 124 LEU A 139 1 16
HELIX 12 AB3 SER A 197 ARG A 202 5 6
HELIX 13 AB4 ILE A 204 ALA A 209 1 6
HELIX 14 AB5 PHE A 233 LEU A 248 1 16
HELIX 15 AB6 ASP A 259 ASN A 272 1 14
HELIX 16 AB7 THR A 290 TRP A 294 5 5
HELIX 17 AB8 PRO A 295 ARG A 306 1 12
HELIX 18 AB9 GLY B 1 ILE B 9 1 9
HELIX 19 AC1 ASN B 12 GLY B 17 1 6
HELIX 20 AC2 GLY B 17 GLY B 22 1 6
HELIX 21 AC3 THR B 28 GLU B 37 1 10
HELIX 22 AC4 PRO B 38 LEU B 40 5 3
HELIX 23 AC5 ASN B 41 ASP B 44 5 4
HELIX 24 AC6 ARG B 45 LEU B 55 1 11
HELIX 25 AC7 PRO B 61 SER B 78 1 18
HELIX 26 AC8 PRO B 94 LEU B 105 1 12
HELIX 27 AC9 LEU B 119 ASN B 124 1 6
HELIX 28 AD1 ASN B 124 SER B 137 1 14
HELIX 29 AD2 SER B 197 ARG B 202 5 6
HELIX 30 AD3 ILE B 204 ALA B 209 1 6
HELIX 31 AD4 PHE B 233 LEU B 248 1 16
HELIX 32 AD5 ASP B 259 ASN B 272 1 14
HELIX 33 AD6 THR B 290 TRP B 294 5 5
HELIX 34 AD7 PRO B 295 PHE B 297 5 3
HELIX 35 AD8 ALA B 298 ARG B 306 1 9
SHEET 1 AA1 8 CYS A 108 GLY A 116 0
SHEET 2 AA1 8 LYS A 82 PRO A 89 1 N TRP A 86 O ILE A 113
SHEET 3 AA1 8 VAL A 276 MET A 282 1 O PHE A 281 N LEU A 83
SHEET 4 AA1 8 VAL A 253 HIS A 258 1 N LEU A 255 O ALA A 280
SHEET 5 AA1 8 VAL A 188 LEU A 191 1 N LEU A 189 O VAL A 254
SHEET 6 AA1 8 CYS A 214 PRO A 217 1 O ILE A 215 N PHE A 190
SHEET 7 AA1 8 GLU A 173 VAL A 180 -1 N VAL A 180 O CYS A 214
SHEET 8 AA1 8 HIS A 166 VAL A 170 -1 N VAL A 170 O GLU A 173
SHEET 1 AA2 8 CYS B 108 GLY B 116 0
SHEET 2 AA2 8 LYS B 82 PRO B 89 1 N LEU B 84 O VAL B 111
SHEET 3 AA2 8 VAL B 276 MET B 282 1 O PHE B 281 N LEU B 83
SHEET 4 AA2 8 VAL B 253 HIS B 258 1 N LEU B 255 O ALA B 280
SHEET 5 AA2 8 VAL B 188 LEU B 191 1 N LEU B 189 O VAL B 254
SHEET 6 AA2 8 CYS B 214 PRO B 217 1 O ILE B 215 N PHE B 190
SHEET 7 AA2 8 GLU B 173 VAL B 180 -1 N VAL B 180 O CYS B 214
SHEET 8 AA2 8 HIS B 166 VAL B 170 -1 N VAL B 170 O GLU B 173
CISPEP 1 GLU A 60 PRO A 61 0 -5.76
CISPEP 2 THR A 88 PRO A 89 0 4.13
CISPEP 3 ASN A 194 PRO A 195 0 5.76
CISPEP 4 GLU B 60 PRO B 61 0 -6.43
CISPEP 5 THR B 88 PRO B 89 0 3.82
CISPEP 6 ASN B 194 PRO B 195 0 5.43
CRYST1 68.870 94.660 100.110 90.00 90.00 90.00 P 21 21 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 0.014520 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010564 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009989 0.00000
TER 2362 THR A 307
TER 4738 THR B 307
MASTER 302 0 2 35 16 0 0 6 5392 2 0 48
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