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HEADER LYASE 07-SEP-24 9DK4
TITLE ANCESTRAL HYDROXYNITRILE LYASE WITH FIFTEEN SUBSTITUTIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIFTEEN-SUBSTITUTION VARIANT OF AN ANCESTRAL HYDROXYNITRILE
COMPND 3 LYASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENGINEERED PROTEIN, ESTERASE, HYDROXYNITRILE LYASE, HYDROLASE FOLD,
KEYWDS 2 LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.C.SARAK,P.TAN,R.L.EVANS III,K.SHI,R.J.KAZLAUSKAS,H.AIHARA,
AUTHOR 2 C.T.PIERCE,M.E.WALSH,L.R.GREENBERG
REVDAT 1 02-OCT-24 9DK4 0
JRNL AUTH P.TAN,S.SARAK
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.88 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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 3 NUMBER OF REFLECTIONS : 73431
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.710
REMARK 3 FREE R VALUE TEST SET COUNT : 1993
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 46.4100 - 4.5300 0.99 5654 155 0.1784 0.1831
REMARK 3 2 4.5300 - 3.5900 0.82 4628 128 0.1564 0.2267
REMARK 3 3 3.5900 - 3.1400 0.86 4869 137 0.1858 0.2110
REMARK 3 4 3.1400 - 2.8500 0.99 5504 154 0.1934 0.2215
REMARK 3 5 2.8500 - 2.6500 0.98 5518 156 0.1858 0.2225
REMARK 3 6 2.6500 - 2.4900 0.98 5489 148 0.1824 0.1961
REMARK 3 7 2.4900 - 2.3700 0.97 5465 158 0.1847 0.2442
REMARK 3 8 2.3700 - 2.2600 0.98 5445 151 0.1889 0.2530
REMARK 3 9 2.2600 - 2.1800 0.98 5448 149 0.1930 0.2682
REMARK 3 10 2.1800 - 2.1000 0.97 5421 154 0.2030 0.2372
REMARK 3 11 2.1000 - 2.0400 0.96 5347 149 0.1992 0.2642
REMARK 3 12 2.0400 - 1.9800 0.94 5217 145 0.2086 0.2762
REMARK 3 13 1.9800 - 1.9300 0.80 4495 123 0.2206 0.2553
REMARK 3 14 1.9300 - 1.8800 0.53 2938 86 0.2771 0.3554
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) : 0.191
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.407
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.79
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 8000
REMARK 3 ANGLE : 0.876 10872
REMARK 3 CHIRALITY : 0.054 1165
REMARK 3 PLANARITY : 0.007 1397
REMARK 3 DIHEDRAL : 6.125 1057
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 9DK4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-24.
REMARK 100 THE DEPOSITION ID IS D_1000284998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-24
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 : NSLS
REMARK 200 BEAMLINE : X17B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73445
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 46.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : 0.13700
REMARK 200 FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40800
REMARK 200 R SYM FOR SHELL (I) : 0.40800
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 (%): 39.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: J000843, C8 5%(W/V) PEG 20K, 25%(W/V)
REMARK 280 1,1,1-TRIS(HYDROXYMETHYL)PROPANE, 1%(W/V) NDSB 195
REMARK 280 (DIMETHYLETHYLAMMONIUM PROPANE SULFONATE), 1 MM OF EACH ALKALI
REMARK 280 (BARIUM ACETATE, CESIUM ACETATE, RUBIDIUM CHLORIDE, STRONTIUM
REMARK 280 ACETATE) AND 0.1 M N,N-BIS(2-HYDROXYETHYL)-2-AMINOETHANESULFONIC
REMARK 280 ACID/TRIETHYLAMINE PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 40.19250
REMARK 290 SMTRY3 2 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 MET A 1
REMARK 465 GLN A 70
REMARK 465 GLY A 71
REMARK 465 GLU A 72
REMARK 465 SER A 138
REMARK 465 ASN A 139
REMARK 465 ASN A 140
REMARK 465 GLU A 141
REMARK 465 THR A 142
REMARK 465 ASP A 258
REMARK 465 LEU A 259
REMARK 465 LEU A 260
REMARK 465 ALA A 261
REMARK 465 VAL A 262
REMARK 465 ALA A 263
REMARK 465 GLY A 264
REMARK 465 LEU A 265
REMARK 465 GLU A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 465 MET B 1
REMARK 465 GLN B 70
REMARK 465 GLY B 71
REMARK 465 ASN B 139
REMARK 465 ASN B 140
REMARK 465 GLU B 141
REMARK 465 ASP B 258
REMARK 465 LEU B 259
REMARK 465 LEU B 260
REMARK 465 ALA B 261
REMARK 465 VAL B 262
REMARK 465 ALA B 263
REMARK 465 GLY B 264
REMARK 465 LEU B 265
REMARK 465 GLU B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 HIS B 272
REMARK 465 MET C 1
REMARK 465 GLN C 70
REMARK 465 GLY C 71
REMARK 465 GLU C 72
REMARK 465 THR C 137
REMARK 465 SER C 138
REMARK 465 ASN C 139
REMARK 465 ASN C 140
REMARK 465 GLU C 141
REMARK 465 THR C 142
REMARK 465 ASP C 258
REMARK 465 LEU C 259
REMARK 465 LEU C 260
REMARK 465 ALA C 261
REMARK 465 VAL C 262
REMARK 465 ALA C 263
REMARK 465 GLY C 264
REMARK 465 LEU C 265
REMARK 465 GLU C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
REMARK 465 HIS C 272
REMARK 465 MET D 1
REMARK 465 GLN D 70
REMARK 465 GLY D 71
REMARK 465 GLU D 72
REMARK 465 THR D 137
REMARK 465 SER D 138
REMARK 465 ASN D 139
REMARK 465 ASN D 140
REMARK 465 GLU D 141
REMARK 465 ASP D 258
REMARK 465 LEU D 259
REMARK 465 LEU D 260
REMARK 465 ALA D 261
REMARK 465 VAL D 262
REMARK 465 ALA D 263
REMARK 465 GLY D 264
REMARK 465 LEU D 265
REMARK 465 GLU D 266
REMARK 465 HIS D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 HIS D 271
REMARK 465 HIS D 272
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 32 CE NZ
REMARK 470 GLN A 50 NE2
REMARK 470 ILE A 51 CG2
REMARK 470 GLU A 66 CG CD OE1 OE2
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 LYS A 92 CD CE NZ
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 THR A 135 CB OG1 CG2
REMARK 470 TYR A 136 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 136 OH
REMARK 470 THR A 137 CB OG1 CG2
REMARK 470 ILE A 143 CG1 CG2 CD1
REMARK 470 THR A 144 CG2
REMARK 470 ILE A 180 CG1 CG2 CD1
REMARK 470 GLN A 185 CG CD OE1 NE2
REMARK 470 LYS A 188 NZ
REMARK 470 THR A 190 CG2
REMARK 470 GLU A 191 CB CG CD OE1 OE2
REMARK 470 GLU A 192 CG CD OE1 OE2
REMARK 470 LYS A 198 CE NZ
REMARK 470 LYS A 208 CE NZ
REMARK 470 GLU A 213 CG CD OE1 OE2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 226 CE NZ
REMARK 470 GLU A 244 CD OE1 OE2
REMARK 470 GLU A 247 CD OE1 OE2
REMARK 470 LYS B 32 CD CE NZ
REMARK 470 LEU B 36 CD1 CD2
REMARK 470 GLN B 50 CG CD OE1 NE2
REMARK 470 THR B 53 CG2
REMARK 470 GLU B 56 CG CD OE1 OE2
REMARK 470 SER B 67 CB OG
REMARK 470 GLU B 72 N CB CG CD OE1 OE2
REMARK 470 LYS B 73 CD CE NZ
REMARK 470 LYS B 92 CE NZ
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 VAL B 124 CB CG1 CG2
REMARK 470 ASP B 127 OD1 OD2
REMARK 470 GLU B 132 CD OE1 OE2
REMARK 470 THR B 135 CG2
REMARK 470 THR B 137 CG2
REMARK 470 SER B 138 CB OG
REMARK 470 THR B 142 CG2
REMARK 470 ILE B 143 CB CG1 CG2 CD1
REMARK 470 LYS B 156 NZ
REMARK 470 ILE B 180 CG2
REMARK 470 GLN B 185 CG CD OE1 NE2
REMARK 470 LYS B 188 CE NZ
REMARK 470 GLU B 191 CD OE1 OE2
REMARK 470 LYS B 198 CE NZ
REMARK 470 LYS B 223 CD CE NZ
REMARK 470 LEU C 36 CD1
REMARK 470 THR C 53 CG2
REMARK 470 GLU C 66 CG CD OE1 OE2
REMARK 470 LEU C 68 CD1 CD2
REMARK 470 LYS C 73 NZ
REMARK 470 LYS C 92 CE NZ
REMARK 470 GLU C 111 CG CD OE1 OE2
REMARK 470 THR C 135 CG2
REMARK 470 ILE C 143 CG1 CG2 CD1
REMARK 470 THR C 144 CG2
REMARK 470 ILE C 180 CG2
REMARK 470 GLN C 185 CD OE1 NE2
REMARK 470 GLU C 191 CG CD OE1 OE2
REMARK 470 LYS C 208 CE NZ
REMARK 470 LYS C 223 CD CE NZ
REMARK 470 LYS C 226 CG CD CE NZ
REMARK 470 GLU C 244 CD OE1 OE2
REMARK 470 GLU C 247 CD OE1 OE2
REMARK 470 LYS D 32 CE NZ
REMARK 470 LEU D 36 CD1
REMARK 470 GLN D 50 NE2
REMARK 470 THR D 53 CG2
REMARK 470 LYS D 92 CD CE NZ
REMARK 470 GLU D 111 CG CD OE1 OE2
REMARK 470 VAL D 124 CB CG1 CG2
REMARK 470 LYS D 129 CE NZ
REMARK 470 GLU D 132 CG CD OE1 OE2
REMARK 470 SER D 134 CB OG
REMARK 470 THR D 135 OG1 CG2
REMARK 470 THR D 142 OG1 CG2
REMARK 470 ILE D 143 CG2
REMARK 470 LYS D 151 CD CE NZ
REMARK 470 LYS D 156 NZ
REMARK 470 ILE D 163 CD1
REMARK 470 ILE D 180 CG1 CG2 CD1
REMARK 470 ASN D 181 OD1 ND2
REMARK 470 GLN D 185 CB CG CD OE1 NE2
REMARK 470 LYS D 188 CE NZ
REMARK 470 LYS D 198 CE NZ
REMARK 470 LYS D 208 NZ
REMARK 470 LYS D 223 CD CE NZ
REMARK 470 LYS D 226 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 CYS A 13 -0.10 75.20
REMARK 500 SER A 80 -127.67 54.97
REMARK 500 THR A 104 55.41 33.28
REMARK 500 ASP A 109 -167.14 -129.34
REMARK 500 SER A 113 150.25 -48.40
REMARK 500 LYS A 129 -119.01 44.24
REMARK 500 TYR A 222 79.04 -153.38
REMARK 500 ASP A 234 -156.68 -85.99
REMARK 500 MET A 236 58.60 -119.07
REMARK 500 HIS B 14 -167.71 -114.98
REMARK 500 SER B 80 -130.60 56.93
REMARK 500 THR B 104 55.55 31.90
REMARK 500 ASP B 109 -169.42 -126.65
REMARK 500 PHE B 125 75.40 35.97
REMARK 500 LYS B 129 -125.95 46.93
REMARK 500 ASP B 234 -155.74 -85.74
REMARK 500 SER C 80 -127.81 60.99
REMARK 500 THR C 104 56.15 31.51
REMARK 500 LYS C 129 -123.33 52.61
REMARK 500 ASP C 234 -153.53 -86.72
REMARK 500 MET C 236 66.51 -119.50
REMARK 500 LYS C 241 47.90 -142.54
REMARK 500 SER D 80 -126.47 56.46
REMARK 500 THR D 104 56.49 36.47
REMARK 500 ASP D 109 -165.88 -129.94
REMARK 500 PHE D 125 71.04 43.54
REMARK 500 LYS D 129 -121.85 46.67
REMARK 500 ASP D 234 -153.14 -90.75
REMARK 500 MET D 236 62.60 -112.19
REMARK 500 LYS D 241 44.28 -142.27
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 37 OD2
REMARK 620 2 HOH A 445 O 72.7
REMARK 620 3 HOH A 457 O 122.8 126.3
REMARK 620 4 MET B 171 O 125.6 90.9 108.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 240 O
REMARK 620 2 HOH A 424 O 123.3
REMARK 620 3 GLU D 206 OE2 83.0 123.0
REMARK 620 4 HOH D 440 O 137.9 88.8 102.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 461 O
REMARK 620 2 GLU B 167 OE1 117.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 206 OE2
REMARK 620 2 SER C 240 O 58.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 110 OG1
REMARK 620 2 TYR C 222 OH 97.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 116 OH
REMARK 620 2 ASN C 221 OD1 102.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 109 OD1
REMARK 620 2 SER D 113 O 119.7
REMARK 620 3 HOH D 435 O 143.2 86.0
REMARK 620 N 1 2
DBREF 9DK4 A 1 272 PDB 9DK4 9DK4 1 272
DBREF 9DK4 B 1 272 PDB 9DK4 9DK4 1 272
DBREF 9DK4 C 1 272 PDB 9DK4 9DK4 1 272
DBREF 9DK4 D 1 272 PDB 9DK4 9DK4 1 272
SEQRES 1 A 272 MET ALA THR ALA HIS PHE VAL LEU VAL HIS GLY ALA CYS
SEQRES 2 A 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 A 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 A 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 A 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 272 HIS SER PHE GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 A 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE LEU THR
SEQRES 9 A 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 A 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 A 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 A 272 THR GLY MET LEU LEU GLY PHE LYS PHE MET ARG GLU LYS
SEQRES 13 A 272 LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 A 272 LYS MET LEU THR ARG PRO GLY SER PHE PHE ILE ASN ASP
SEQRES 15 A 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 A 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 A 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 A 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 A 272 HIS MET PRO GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 A 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 A 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 272 MET ALA THR ALA HIS PHE VAL LEU VAL HIS GLY ALA CYS
SEQRES 2 B 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 B 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 B 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 B 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 B 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 B 272 HIS SER PHE GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 B 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE LEU THR
SEQRES 9 B 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 B 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 B 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 B 272 THR GLY MET LEU LEU GLY PHE LYS PHE MET ARG GLU LYS
SEQRES 13 B 272 LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 B 272 LYS MET LEU THR ARG PRO GLY SER PHE PHE ILE ASN ASP
SEQRES 15 B 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 B 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 B 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 B 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 B 272 HIS MET PRO GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 B 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 B 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 272 MET ALA THR ALA HIS PHE VAL LEU VAL HIS GLY ALA CYS
SEQRES 2 C 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 C 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 C 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 C 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 C 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 C 272 HIS SER PHE GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 C 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE LEU THR
SEQRES 9 C 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 C 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 C 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 C 272 THR GLY MET LEU LEU GLY PHE LYS PHE MET ARG GLU LYS
SEQRES 13 C 272 LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 C 272 LYS MET LEU THR ARG PRO GLY SER PHE PHE ILE ASN ASP
SEQRES 15 C 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 C 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 C 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 C 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 C 272 HIS MET PRO GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 C 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 C 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 272 MET ALA THR ALA HIS PHE VAL LEU VAL HIS GLY ALA CYS
SEQRES 2 D 272 HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU LEU
SEQRES 3 D 272 GLU ALA ALA GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 D 272 ALA SER GLY ILE ASP PRO ARG GLN ILE GLU GLN ILE ASN
SEQRES 5 D 272 THR PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE MET
SEQRES 6 D 272 GLU SER LEU PRO GLN GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 D 272 HIS SER PHE GLY GLY LEU ASN ILE ALA LEU ALA ALA ASP
SEQRES 8 D 272 LYS TYR PRO GLU LYS ILE SER ALA ALA VAL PHE LEU THR
SEQRES 9 D 272 ALA LEU MET PRO ASP THR GLU HIS SER PRO SER TYR VAL
SEQRES 10 D 272 VAL ASP LYS PHE MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 D 272 THR GLU PHE SER THR TYR THR SER ASN ASN GLU THR ILE
SEQRES 12 D 272 THR GLY MET LEU LEU GLY PHE LYS PHE MET ARG GLU LYS
SEQRES 13 D 272 LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU ALA
SEQRES 14 D 272 LYS MET LEU THR ARG PRO GLY SER PHE PHE ILE ASN ASP
SEQRES 15 D 272 LEU ALA GLN ARG PRO LYS PHE THR GLU GLU GLY TYR GLY
SEQRES 16 D 272 SER ILE LYS ARG VAL TYR VAL TRP THR ASP GLU ASP LYS
SEQRES 17 D 272 ILE PHE PRO PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 D 272 TYR LYS PRO ASP LYS VAL TYR ARG VAL GLN GLY GLY ASP
SEQRES 19 D 272 HIS MET PRO GLN LEU SER LYS THR ASN GLU LEU ALA GLU
SEQRES 20 D 272 ILE LEU GLN GLU VAL ALA ASP THR TYR ALA ASP LEU LEU
SEQRES 21 D 272 ALA VAL ALA GLY LEU GLU HIS HIS HIS HIS HIS HIS
HET NA A 301 1
HET NA B 301 1
HET NA B 302 1
HET NA C 301 1
HET NA C 302 1
HET NA D 301 1
HET NA D 302 1
HETNAM NA SODIUM ION
FORMUL 5 NA 7(NA 1+)
FORMUL 12 HOH *261(H2 O)
HELIX 1 AA1 GLY A 15 TYR A 20 5 6
HELIX 2 AA2 LYS A 21 ALA A 29 1 9
HELIX 3 AA3 GLN A 47 ILE A 51 5 5
HELIX 4 AA4 THR A 53 SER A 67 1 15
HELIX 5 AA5 PHE A 81 TYR A 93 1 13
HELIX 6 AA6 SER A 115 VAL A 124 1 10
HELIX 7 AA7 GLY A 149 LEU A 157 1 9
HELIX 8 AA8 PRO A 162 THR A 173 1 12
HELIX 9 AA9 PHE A 179 ARG A 186 1 8
HELIX 10 AB1 GLY A 193 ILE A 197 5 5
HELIX 11 AB2 PRO A 211 TYR A 222 1 12
HELIX 12 AB3 MET A 236 LYS A 241 1 6
HELIX 13 AB4 LYS A 241 ALA A 257 1 17
HELIX 14 AB5 GLY B 15 TYR B 20 5 6
HELIX 15 AB6 LYS B 21 ALA B 29 1 9
HELIX 16 AB7 GLN B 47 ILE B 51 5 5
HELIX 17 AB8 THR B 53 SER B 58 1 6
HELIX 18 AB9 SER B 58 LEU B 68 1 11
HELIX 19 AC1 PHE B 81 TYR B 93 1 13
HELIX 20 AC2 SER B 115 VAL B 124 1 10
HELIX 21 AC3 GLY B 149 LEU B 157 1 9
HELIX 22 AC4 PRO B 162 THR B 173 1 12
HELIX 23 AC5 PHE B 179 ARG B 186 1 8
HELIX 24 AC6 GLY B 193 ILE B 197 5 5
HELIX 25 AC7 PRO B 211 TYR B 222 1 12
HELIX 26 AC8 MET B 236 LYS B 241 1 6
HELIX 27 AC9 LYS B 241 ALA B 257 1 17
HELIX 28 AD1 GLY C 15 TYR C 20 5 6
HELIX 29 AD2 LYS C 21 ALA C 29 1 9
HELIX 30 AD3 GLN C 47 ILE C 51 5 5
HELIX 31 AD4 THR C 53 LEU C 68 1 16
HELIX 32 AD5 PHE C 81 TYR C 93 1 13
HELIX 33 AD6 SER C 115 VAL C 124 1 10
HELIX 34 AD7 GLY C 149 LEU C 157 1 9
HELIX 35 AD8 PRO C 162 THR C 173 1 12
HELIX 36 AD9 PHE C 179 ARG C 186 1 8
HELIX 37 AE1 GLY C 193 ILE C 197 5 5
HELIX 38 AE2 PRO C 211 TYR C 222 1 12
HELIX 39 AE3 MET C 236 LYS C 241 1 6
HELIX 40 AE4 LYS C 241 ALA C 257 1 17
HELIX 41 AE5 GLY D 15 TYR D 20 5 6
HELIX 42 AE6 LYS D 21 ALA D 28 1 8
HELIX 43 AE7 GLN D 47 ILE D 51 5 5
HELIX 44 AE8 THR D 53 SER D 58 1 6
HELIX 45 AE9 SER D 58 LEU D 68 1 11
HELIX 46 AF1 PHE D 81 TYR D 93 1 13
HELIX 47 AF2 SER D 115 VAL D 124 1 10
HELIX 48 AF3 GLY D 149 LEU D 157 1 9
HELIX 49 AF4 PRO D 162 THR D 173 1 12
HELIX 50 AF5 PHE D 179 ARG D 186 1 8
HELIX 51 AF6 GLY D 193 ILE D 197 5 5
HELIX 52 AF7 PRO D 211 TYR D 222 1 12
HELIX 53 AF8 MET D 236 LYS D 241 1 6
HELIX 54 AF9 LYS D 241 ALA D 257 1 17
SHEET 1 AA1 6 LYS A 32 LEU A 36 0
SHEET 2 AA1 6 HIS A 5 VAL A 9 1 N LEU A 8 O THR A 34
SHEET 3 AA1 6 VAL A 74 HIS A 79 1 O VAL A 77 N VAL A 9
SHEET 4 AA1 6 ILE A 97 LEU A 103 1 O VAL A 101 N LEU A 76
SHEET 5 AA1 6 ARG A 199 THR A 204 1 O VAL A 200 N PHE A 102
SHEET 6 AA1 6 LYS A 226 VAL A 230 1 O VAL A 230 N TRP A 203
SHEET 1 AA2 2 GLU A 132 THR A 135 0
SHEET 2 AA2 2 THR A 144 LEU A 147 -1 O GLY A 145 N SER A 134
SHEET 1 AA3 6 LYS B 32 LEU B 36 0
SHEET 2 AA3 6 HIS B 5 VAL B 9 1 N LEU B 8 O THR B 34
SHEET 3 AA3 6 VAL B 74 HIS B 79 1 O VAL B 77 N VAL B 9
SHEET 4 AA3 6 ILE B 97 LEU B 103 1 O VAL B 101 N LEU B 76
SHEET 5 AA3 6 ARG B 199 THR B 204 1 O VAL B 200 N PHE B 102
SHEET 6 AA3 6 LYS B 226 VAL B 230 1 O VAL B 230 N TRP B 203
SHEET 1 AA4 2 GLU B 132 TYR B 136 0
SHEET 2 AA4 2 ILE B 143 LEU B 147 -1 O GLY B 145 N SER B 134
SHEET 1 AA5 6 LYS C 32 LEU C 36 0
SHEET 2 AA5 6 HIS C 5 VAL C 9 1 N LEU C 8 O THR C 34
SHEET 3 AA5 6 VAL C 74 HIS C 79 1 O VAL C 77 N VAL C 9
SHEET 4 AA5 6 ILE C 97 LEU C 103 1 O VAL C 101 N LEU C 76
SHEET 5 AA5 6 ARG C 199 THR C 204 1 O VAL C 200 N PHE C 102
SHEET 6 AA5 6 LYS C 226 VAL C 230 1 O VAL C 230 N TRP C 203
SHEET 1 AA6 3 GLU C 132 SER C 134 0
SHEET 2 AA6 3 GLY C 145 LEU C 147 -1 O GLY C 145 N SER C 134
SHEET 3 AA6 3 GLY C 176 SER C 177 -1 O GLY C 176 N MET C 146
SHEET 1 AA7 6 LYS D 32 ALA D 35 0
SHEET 2 AA7 6 HIS D 5 VAL D 9 1 N LEU D 8 O THR D 34
SHEET 3 AA7 6 VAL D 74 HIS D 79 1 O VAL D 77 N VAL D 9
SHEET 4 AA7 6 ILE D 97 LEU D 103 1 O VAL D 101 N LEU D 76
SHEET 5 AA7 6 ARG D 199 THR D 204 1 O VAL D 200 N PHE D 102
SHEET 6 AA7 6 LYS D 226 VAL D 230 1 O VAL D 230 N TRP D 203
SHEET 1 AA8 2 GLU D 132 THR D 135 0
SHEET 2 AA8 2 THR D 144 LEU D 147 -1 O GLY D 145 N SER D 134
LINK OD2 ASP A 37 NA NA A 301 1555 1555 2.66
LINK O SER A 240 NA NA D 302 1555 1555 2.87
LINK NA NA A 301 O HOH A 445 1555 1555 3.11
LINK NA NA A 301 O HOH A 457 1555 1555 2.93
LINK NA NA A 301 O MET B 171 1555 1555 2.56
LINK O HOH A 424 NA NA D 302 1555 1555 2.85
LINK O HOH A 461 NA NA B 301 1555 1555 2.76
LINK OE1 GLU B 167 NA NA B 301 1555 1555 2.41
LINK OE2 GLU B 206 NA NA B 302 1555 1555 2.45
LINK NA NA B 302 O SER C 240 2746 1555 2.93
LINK OG1 THR C 110 NA NA C 301 1555 1555 2.51
LINK OH TYR C 116 NA NA C 302 1555 1555 2.91
LINK OD1 ASN C 221 NA NA C 302 1555 1555 2.49
LINK OH TYR C 222 NA NA C 301 1555 1555 3.15
LINK OD1 ASP D 109 NA NA D 301 1555 1555 2.75
LINK O SER D 113 NA NA D 301 1555 1555 2.76
LINK OE2 GLU D 206 NA NA D 302 1555 1555 2.42
LINK NA NA D 301 O HOH D 435 1555 1555 2.59
LINK NA NA D 302 O HOH D 440 1555 1555 3.18
CRYST1 67.244 80.385 92.823 90.00 90.62 90.00 P 1 21 1 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 0.014871 0.000000 0.000161 0.00000
SCALE2 0.000000 0.012440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010774 0.00000
TER 1922 ALA A 257
TER 3880 ALA B 257
TER 5830 ALA C 257
TER 7777 ALA D 257
MASTER 524 0 7 54 33 0 0 6 8041 4 25 84
END |