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HEADER HYDROLASE 04-AUG-21 7PCW
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7-M175W LABELED
TITLE 2 WITH A CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D;
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 FLUOROPHORE, TETRAMETHYLRHODAMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
REVDAT 1 15-DEC-21 7PCW 0
JRNL AUTH M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE
JRNL TITL 2 HALOTAG7-M175W LABELED WITH A
JRNL TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 43471
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2174
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 40.3600 - 5.7900 0.95 2559 135 0.1533 0.1718
REMARK 3 2 5.7900 - 4.6000 0.94 2550 135 0.1694 0.1837
REMARK 3 3 4.6000 - 4.0200 0.95 2544 134 0.1535 0.1861
REMARK 3 4 4.0200 - 3.6500 0.96 2593 136 0.1690 0.2098
REMARK 3 5 3.6500 - 3.3900 0.97 2608 137 0.1764 0.2437
REMARK 3 6 3.3900 - 3.1900 0.95 2531 134 0.2013 0.2662
REMARK 3 7 3.1900 - 3.0300 0.95 2612 137 0.2147 0.2751
REMARK 3 8 3.0300 - 2.9000 0.96 2569 135 0.2067 0.2853
REMARK 3 9 2.9000 - 2.7900 0.96 2552 134 0.2213 0.3070
REMARK 3 10 2.7900 - 2.6900 0.96 2610 138 0.2256 0.2987
REMARK 3 11 2.6900 - 2.6100 0.97 2577 136 0.2337 0.3398
REMARK 3 12 2.6100 - 2.5300 0.95 2612 137 0.2292 0.3266
REMARK 3 13 2.5300 - 2.4600 0.97 2580 136 0.2341 0.2730
REMARK 3 14 2.4600 - 2.4000 0.95 2624 138 0.2313 0.3034
REMARK 3 15 2.4000 - 2.3500 0.97 2562 135 0.2247 0.2800
REMARK 3 16 2.3500 - 2.3000 0.96 2614 137 0.2218 0.2751
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) : 0.277
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.14
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.57
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 9918
REMARK 3 ANGLE : 0.576 13570
REMARK 3 CHIRALITY : 0.045 1408
REMARK 3 PLANARITY : 0.005 1904
REMARK 3 DIHEDRAL : 13.496 3700
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 7PCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-21.
REMARK 100 THE DEPOSITION ID IS D_1292117490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-21
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) : 1.00000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43477
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 95.6
REMARK 200 DATA REDUNDANCY : 2.670
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.58
REMARK 200 R MERGE FOR SHELL (I) : 0.46700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
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: 6Y7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 1.0 M LITHIUM
REMARK 280 CHLORIDE, 22% (M/V) PEG 6000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 ILE A 295
REMARK 465 ILE D 295
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 PRO A 42 41.68 -105.34
REMARK 500 THR A 43 -158.86 -97.28
REMARK 500 ASP A 106 -122.74 53.43
REMARK 500 ARG A 153 37.19 -81.47
REMARK 500 ASP A 156 -67.18 -92.32
REMARK 500 PRO A 210 90.61 -68.71
REMARK 500 VAL A 245 -67.81 -124.90
REMARK 500 LEU A 271 -96.34 -119.22
REMARK 500 ASN A 278 67.61 -157.98
REMARK 500 PRO B 42 42.71 -105.05
REMARK 500 ASP B 106 -120.20 52.47
REMARK 500 GLU B 130 59.20 39.33
REMARK 500 ARG B 153 44.42 -84.60
REMARK 500 ASP B 156 -63.34 -93.19
REMARK 500 VAL B 245 -61.72 -128.57
REMARK 500 LEU B 271 -95.82 -117.62
REMARK 500 ASN B 278 66.42 -160.21
REMARK 500 GLU B 294 79.69 -101.05
REMARK 500 PRO C 42 44.92 -103.54
REMARK 500 GLU C 98 -83.86 -95.54
REMARK 500 ASP C 106 -124.17 52.94
REMARK 500 ARG C 153 46.89 -88.53
REMARK 500 ASP C 156 -69.45 -99.71
REMARK 500 VAL C 245 -65.33 -130.72
REMARK 500 LEU C 271 -90.61 -123.33
REMARK 500 ASN C 278 66.78 -153.20
REMARK 500 PRO D 42 51.30 -104.03
REMARK 500 THR D 43 -165.36 -107.35
REMARK 500 SER D 44 -159.38 -150.54
REMARK 500 GLU D 98 -85.67 -100.30
REMARK 500 ASP D 106 -122.88 56.71
REMARK 500 ARG D 153 48.90 -88.49
REMARK 500 ASP D 156 -67.04 -97.01
REMARK 500 VAL D 245 -65.25 -129.67
REMARK 500 LEU D 271 -99.24 -114.43
REMARK 500 ASN D 278 69.26 -158.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZVU RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVV RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVW RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVX RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVY RELATED DB: PDB
REMARK 900 RELATED ID: 7PCX RELATED DB: PDB
DBREF 7PCW A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCW B 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCW C 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 7PCW D 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 7PCW GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCW THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCW GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCW PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCW MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCW PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCW THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCW LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCW VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCW THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCW TRP A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCW GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCW ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCW GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCW ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCW LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCW ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCW ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCW LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCW SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCW THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCW GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW GLY B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCW THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCW GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCW PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCW MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCW PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCW THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCW LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCW VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCW THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCW TRP B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCW GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCW ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCW GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCW ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCW LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCW ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCW ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCW LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCW SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCW THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCW GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW GLY C 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW VAL C 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCW THR C 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCW GLY C 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCW PHE C 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCW MET C 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCW PHE C 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCW THR C 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCW LYS C 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCW VAL C 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCW THR C 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCW TRP C 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCW GLY C 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCW ASN C 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCW GLU C 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCW ASP C 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCW LYS C 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCW ALA C 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCW ASN C 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCW LEU C 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCW SER C 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCW THR C 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCW GLU C 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW ILE C 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW GLY D 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW VAL D 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7PCW THR D 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7PCW GLY D 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7PCW PHE D 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7PCW MET D 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7PCW PHE D 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7PCW THR D 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7PCW LYS D 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7PCW VAL D 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7PCW THR D 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7PCW TRP D 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7PCW GLY D 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7PCW ASN D 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7PCW GLU D 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7PCW ASP D 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7PCW LYS D 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7PCW ALA D 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7PCW ASN D 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7PCW LEU D 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7PCW SER D 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 7PCW THR D 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 7PCW GLU D 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7PCW ILE D 295 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 A 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 A 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 A 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 A 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 A 293 THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 A 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 A 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 A 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 A 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 B 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 B 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 B 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 B 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 B 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 B 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 B 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 B 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 B 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 B 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 B 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 B 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 B 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 B 293 THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 B 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 B 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 B 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 B 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 B 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 B 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 B 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 B 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 B 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 C 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 C 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 C 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 C 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 C 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 C 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 C 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 C 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 C 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 C 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 C 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 C 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 C 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 C 293 THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 C 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 C 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 C 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 C 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 C 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 C 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 C 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 C 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 C 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 D 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 D 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 D 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 D 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 D 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 D 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 D 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 D 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 D 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 D 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 D 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 D 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 D 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 D 293 THR LEU PRO TRP GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 D 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 D 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 D 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 D 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 D 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 D 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 D 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 D 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 D 293 TRP LEU SER THR LEU GLU ILE
HET OEH A 301 44
HET CL A 302 1
HET OEH B 301 44
HET CL B 302 1
HET OEH C 301 44
HET CL C 302 1
HET OEH D 301 44
HET CL D 302 1
HETNAM OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM 2 OEH ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM 3 OEH XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM CL CHLORIDE ION
FORMUL 5 OEH 4(C35 H43 CL N3 O6 1+)
FORMUL 6 CL 4(CL 1-)
FORMUL 13 HOH *125(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 LEU A 173 VAL A 177 5 5
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 ASN A 195 ASP A 198 5 4
HELIX 13 AB4 ARG A 199 GLU A 208 1 10
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 LEU A 273 ASN A 278 1 6
HELIX 17 AB8 ASN A 278 THR A 292 1 15
HELIX 18 AB9 SER B 44 ARG B 49 5 6
HELIX 19 AC1 ILE B 51 ALA B 56 1 6
HELIX 20 AC2 PHE B 80 LEU B 95 1 16
HELIX 21 AC3 ASP B 106 ASN B 119 1 14
HELIX 22 AC4 PRO B 142 PHE B 144 5 3
HELIX 23 AC5 ALA B 145 ARG B 153 1 9
HELIX 24 AC6 ASP B 156 ILE B 163 1 8
HELIX 25 AC7 ASN B 166 GLY B 171 1 6
HELIX 26 AC8 LEU B 173 VAL B 177 5 5
HELIX 27 AC9 THR B 182 GLU B 191 1 10
HELIX 28 AD1 PRO B 192 LEU B 194 5 3
HELIX 29 AD2 ASN B 195 ASP B 198 5 4
HELIX 30 AD3 ARG B 199 LEU B 209 1 11
HELIX 31 AD4 PRO B 215 SER B 232 1 18
HELIX 32 AD5 PRO B 248 LEU B 259 1 12
HELIX 33 AD6 LEU B 273 ASN B 278 1 6
HELIX 34 AD7 ASN B 278 SER B 291 1 14
HELIX 35 AD8 SER C 44 ARG C 49 5 6
HELIX 36 AD9 ILE C 51 ALA C 56 1 6
HELIX 37 AE1 PHE C 80 LEU C 95 1 16
HELIX 38 AE2 ASP C 106 ASN C 119 1 14
HELIX 39 AE3 THR C 137 TRP C 141 5 5
HELIX 40 AE4 PRO C 142 PHE C 144 5 3
HELIX 41 AE5 ALA C 145 ARG C 153 1 9
HELIX 42 AE6 ASP C 156 ILE C 163 1 8
HELIX 43 AE7 ASN C 166 GLY C 171 1 6
HELIX 44 AE8 LEU C 173 VAL C 177 5 5
HELIX 45 AE9 THR C 182 GLU C 191 1 10
HELIX 46 AF1 PRO C 192 LEU C 194 5 3
HELIX 47 AF2 ASN C 195 ASP C 198 5 4
HELIX 48 AF3 ARG C 199 LEU C 209 1 11
HELIX 49 AF4 PRO C 215 SER C 232 1 18
HELIX 50 AF5 PRO C 248 LEU C 259 1 12
HELIX 51 AF6 LEU C 273 ASP C 277 5 5
HELIX 52 AF7 ASN C 278 SER C 291 1 14
HELIX 53 AF8 SER D 44 ARG D 49 5 6
HELIX 54 AF9 ILE D 51 VAL D 55 5 5
HELIX 55 AG1 PHE D 80 LEU D 95 1 16
HELIX 56 AG2 ASP D 106 ASN D 119 1 14
HELIX 57 AG3 PRO D 142 ARG D 153 1 12
HELIX 58 AG4 ASP D 156 ILE D 163 1 8
HELIX 59 AG5 ASN D 166 GLY D 171 1 6
HELIX 60 AG6 LEU D 173 VAL D 177 5 5
HELIX 61 AG7 THR D 182 GLU D 191 1 10
HELIX 62 AG8 PRO D 192 LEU D 194 5 3
HELIX 63 AG9 ASN D 195 ASP D 198 5 4
HELIX 64 AH1 ARG D 199 GLU D 208 1 10
HELIX 65 AH2 PRO D 215 SER D 232 1 18
HELIX 66 AH3 PRO D 248 LEU D 259 1 12
HELIX 67 AH4 LEU D 273 ASN D 278 1 6
HELIX 68 AH5 ASN D 278 THR D 292 1 15
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O LYS A 263 N LEU A 238
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 GLU B 20 VAL B 27 -1 O GLU B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N PHE B 37 O ILE B 62
SHEET 5 AA2 8 VAL B 100 HIS B 105 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 1 O ALA B 127 N LEU B 102
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 CYS B 262 GLY B 270 1 O LYS B 263 N LEU B 238
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 GLU C 20 VAL C 27 -1 O GLU C 20 N VAL C 17
SHEET 3 AA3 8 CYS C 61 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 VAL C 35 LEU C 38 1 N VAL C 35 O ILE C 62
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 101 N LEU C 36
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O ALA C 127 N LEU C 102
SHEET 7 AA3 8 LYS C 236 PRO C 243 1 O LEU C 237 N PHE C 128
SHEET 8 AA3 8 CYS C 262 GLY C 270 1 O LYS C 263 N LEU C 238
SHEET 1 AA4 8 HIS D 13 VAL D 17 0
SHEET 2 AA4 8 GLU D 20 VAL D 27 -1 O GLU D 20 N VAL D 17
SHEET 3 AA4 8 CYS D 61 PRO D 64 -1 O CYS D 61 N VAL D 27
SHEET 4 AA4 8 VAL D 35 LEU D 38 1 N PHE D 37 O ILE D 62
SHEET 5 AA4 8 VAL D 100 HIS D 105 1 O VAL D 101 N LEU D 36
SHEET 6 AA4 8 VAL D 123 MET D 129 1 O ALA D 127 N LEU D 102
SHEET 7 AA4 8 LYS D 236 PRO D 243 1 O LEU D 237 N PHE D 128
SHEET 8 AA4 8 CYS D 262 GLY D 270 1 O LYS D 263 N LEU D 238
LINK OD2 ASP A 106 C20 OEH A 301 1555 1555 1.38
LINK OD2 ASP B 106 C20 OEH B 301 1555 1555 1.38
LINK OD2 ASP C 106 C20 OEH C 301 1555 1555 1.38
LINK OD2 ASP D 106 C20 OEH D 301 1555 1555 1.38
CISPEP 1 ASN A 41 PRO A 42 0 -0.88
CISPEP 2 GLU A 214 PRO A 215 0 -3.29
CISPEP 3 THR A 242 PRO A 243 0 3.49
CISPEP 4 ASN B 41 PRO B 42 0 -0.75
CISPEP 5 GLU B 214 PRO B 215 0 -6.81
CISPEP 6 THR B 242 PRO B 243 0 4.38
CISPEP 7 ASN C 41 PRO C 42 0 -1.78
CISPEP 8 GLU C 214 PRO C 215 0 -4.58
CISPEP 9 THR C 242 PRO C 243 0 2.32
CISPEP 10 ASN D 41 PRO D 42 0 -1.83
CISPEP 11 GLU D 214 PRO D 215 0 -2.83
CISPEP 12 THR D 242 PRO D 243 0 2.25
CRYST1 44.320 76.560 85.760 68.40 79.81 79.02 P 1 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 0.022563 -0.004377 -0.002710 0.00000
SCALE2 0.000000 0.013305 -0.004909 0.00000
SCALE3 0.000000 0.000000 0.012628 0.00000
TER 2348 GLU A 294
TER 4705 ILE B 295
TER 7062 ILE C 295
TER 9410 GLU D 294
MASTER 282 0 8 68 32 0 0 6 9711 4 180 92
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