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HEADER HYDROLASE 21-JUL-16 5LKA
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB 140A+143L+177W+211L
TITLE 2 MUTANT (LINB86) FROM SPHINGOBIUM JAPONICUM UT26 AT 1.3 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM JAPONICUM;
SOURCE 3 ORGANISM_TAXID: 332056;
SOURCE 4 GENE: LINB, DHAA, SJA_C1-19590;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, BACTERIAL ENZYME, MUTANT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.DEGTJARIK,P.REZACOVA,I.IERMAK,R.CHALOUPKOVA,J.DAMBORSKY,I.KUTA
AUTHOR 2 SMATANOVA
REVDAT 1 05-OCT-16 5LKA 0
JRNL AUTH J.BREZOVSKY,P.BABKOVA,O.DEGTJARIK,A.FORTOVA,A.GORA,I.IERMAK,
JRNL AUTH 2 P.REZACOVA,P.DVORAK,I.KUTA SMATANOVA,Z.PROKOP,R.CHALOUPKOVA,
JRNL AUTH 3 J.DAMBORSKY
JRNL TITL ENGINEERING A DE NOVO TRANSPORT TUNNEL.
JRNL REF ACS CATALYSIS 2016
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.6B02081
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.52
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 64467
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.260
REMARK 3 FREE R VALUE TEST SET COUNT : 2101
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 40.5413 - 3.2009 1.00 4423 149 0.1307 0.1548
REMARK 3 2 3.2009 - 2.5407 1.00 4248 143 0.1471 0.1503
REMARK 3 3 2.5407 - 2.2196 1.00 4207 142 0.1396 0.1654
REMARK 3 4 2.2196 - 2.0167 1.00 4173 141 0.1313 0.1926
REMARK 3 5 2.0167 - 1.8721 1.00 4173 140 0.1272 0.1811
REMARK 3 6 1.8721 - 1.7617 1.00 4142 140 0.1235 0.1553
REMARK 3 7 1.7617 - 1.6735 1.00 4143 139 0.1224 0.1592
REMARK 3 8 1.6735 - 1.6007 1.00 4173 140 0.1200 0.1791
REMARK 3 9 1.6007 - 1.5390 1.00 4128 139 0.1272 0.1746
REMARK 3 10 1.5390 - 1.4859 1.00 4111 139 0.1298 0.1668
REMARK 3 11 1.4859 - 1.4395 1.00 4146 140 0.1417 0.1865
REMARK 3 12 1.4395 - 1.3983 1.00 4104 138 0.1655 0.2405
REMARK 3 13 1.3983 - 1.3615 1.00 4105 138 0.1791 0.2262
REMARK 3 14 1.3615 - 1.3283 1.00 4115 139 0.1891 0.2614
REMARK 3 15 1.3283 - 1.2981 0.97 3975 134 0.2047 0.2266
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.69
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 : 0.006 2623
REMARK 3 ANGLE : 0.921 3595
REMARK 3 CHIRALITY : 0.085 370
REMARK 3 PLANARITY : 0.006 487
REMARK 3 DIHEDRAL : 21.922 992
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 5LKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000874.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-15
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 : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 3, 2014
REMARK 200 DATA SCALING SOFTWARE : XDS NOVEMBER 3, 2014
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64480
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.298
REMARK 200 RESOLUTION RANGE LOW (A) : 46.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.350
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.50600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.6.0
REMARK 200 STARTING MODEL: 4WDR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM THIOCYANATE, 20 % (W/V)
REMARK 280 PEG 3350., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 23.43350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.32400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.18100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.32400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.43350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.18100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 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 6 CD CE NZ
REMARK 470 HIS A 302 CG ND1 CD2 CE1 NE2
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 39 51.36 -104.62
REMARK 500 THR A 40 -162.36 -103.23
REMARK 500 HIS A 107 -114.01 -108.43
REMARK 500 ASP A 108 -130.63 63.21
REMARK 500 ASP A 108 -91.45 -90.80
REMARK 500 HIS A 121 47.88 -140.07
REMARK 500 ALA A 247 -64.11 -152.66
REMARK 500 THR A 249 74.02 -116.93
REMARK 500 ALA A 271 -96.50 -98.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WDR RELATED DB: PDB
REMARK 900 SAME VARIANT, H32 SPACE GROUP, 2.5A RESOLUTION
REMARK 900 RELATED ID: 4WDQ RELATED DB: PDB
REMARK 900 LINB L177W VARIANT
REMARK 900 RELATED ID: 1CV2 RELATED DB: PDB
REMARK 900 LINB WILD TYPE
DBREF 5LKA A 2 296 UNP D4Z2G1 D4Z2G1_SPHJU 2 296
SEQADV 5LKA ALA A 140 UNP D4Z2G1 TRP 140 ENGINEERED MUTATION
SEQADV 5LKA LEU A 143 UNP D4Z2G1 PHE 143 ENGINEERED MUTATION
SEQADV 5LKA TRP A 177 UNP D4Z2G1 LEU 177 ENGINEERED MUTATION
SEQADV 5LKA LEU A 211 UNP D4Z2G1 ILE 211 ENGINEERED MUTATION
SEQADV 5LKA HIS A 297 UNP D4Z2G1 EXPRESSION TAG
SEQADV 5LKA HIS A 298 UNP D4Z2G1 EXPRESSION TAG
SEQADV 5LKA HIS A 299 UNP D4Z2G1 EXPRESSION TAG
SEQADV 5LKA HIS A 300 UNP D4Z2G1 EXPRESSION TAG
SEQADV 5LKA HIS A 301 UNP D4Z2G1 EXPRESSION TAG
SEQADV 5LKA HIS A 302 UNP D4Z2G1 EXPRESSION TAG
SEQRES 1 A 301 SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE ILE
SEQRES 2 A 301 GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU GLY
SEQRES 3 A 301 THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO THR
SEQRES 4 A 301 SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS ALA
SEQRES 5 A 301 GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET
SEQRES 6 A 301 GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU ARG
SEQRES 7 A 301 TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA LEU
SEQRES 8 A 301 TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU VAL
SEQRES 9 A 301 VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA
SEQRES 10 A 301 ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR MET
SEQRES 11 A 301 GLU ALA ILE ALA MET PRO ILE GLU ALA ALA ASP LEU PRO
SEQRES 12 A 301 GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER GLN
SEQRES 13 A 301 ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE VAL
SEQRES 14 A 301 GLU GLN VAL LEU PRO GLY TRP ILE LEU ARG PRO LEU SER
SEQRES 15 A 301 GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU ALA
SEQRES 16 A 301 ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 17 A 301 GLN LEU PRO ILE ALA GLY THR PRO ALA ASP VAL VAL ALA
SEQRES 18 A 301 ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER PRO
SEQRES 19 A 301 ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA LEU
SEQRES 20 A 301 THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP PRO
SEQRES 21 A 301 ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE ILE
SEQRES 22 A 301 GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA
SEQRES 23 A 301 ALA PHE VAL ARG ARG LEU ARG PRO ALA HIS HIS HIS HIS
SEQRES 24 A 301 HIS HIS
HET SCN A 401 3
HETNAM SCN THIOCYANATE ION
FORMUL 2 SCN C N S 1-
FORMUL 3 HOH *434(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 5 6
HELIX 3 AA3 ALA A 81 LEU A 96 1 16
HELIX 4 AA4 TRP A 109 HIS A 121 1 13
HELIX 5 AA5 GLU A 139 LEU A 143 5 5
HELIX 6 AA6 PRO A 144 GLN A 146 5 3
HELIX 7 AA7 ASP A 147 SER A 156 1 10
HELIX 8 AA8 ALA A 158 GLN A 165 1 8
HELIX 9 AA9 ASN A 167 GLN A 172 1 6
HELIX 10 AB1 GLN A 172 TRP A 177 1 6
HELIX 11 AB2 SER A 183 GLU A 192 1 10
HELIX 12 AB3 PRO A 193 LEU A 195 5 3
HELIX 13 AB4 GLY A 198 ALA A 200 5 3
HELIX 14 AB5 ARG A 201 LEU A 211 1 11
HELIX 15 AB6 PRO A 217 SER A 232 1 16
HELIX 16 AB7 THR A 250 ARG A 258 1 9
HELIX 17 AB8 PHE A 273 ASP A 277 5 5
HELIX 18 AB9 SER A 278 ARG A 294 1 17
SHEET 1 AA1 8 LYS A 12 ILE A 16 0
SHEET 2 AA1 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 AA1 8 ARG A 57 CYS A 61 -1 O LEU A 58 N GLU A 26
SHEET 4 AA1 8 PRO A 31 GLN A 35 1 N PHE A 34 O ILE A 59
SHEET 5 AA1 8 VAL A 102 ASP A 108 1 O VAL A 103 N LEU A 33
SHEET 6 AA1 8 VAL A 125 ALA A 133 1 O ALA A 129 N LEU A 104
SHEET 7 AA1 8 LYS A 238 PRO A 245 1 O ILE A 241 N TYR A 130
SHEET 8 AA1 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
CISPEP 1 ASN A 38 PRO A 39 0 -5.79
CISPEP 2 ASP A 73 PRO A 74 0 12.01
CISPEP 3 THR A 216 PRO A 217 0 -4.19
CISPEP 4 THR A 216 PRO A 217 0 -1.95
CISPEP 5 GLU A 244 PRO A 245 0 3.73
SITE 1 AC1 5 ASN A 38 ASP A 108 TRP A 109 TRP A 207
SITE 2 AC1 5 PRO A 208
CRYST1 46.867 68.362 80.648 90.00 90.00 90.00 P 21 21 21 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 0.021337 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014628 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012400 0.00000
TER 2532 HIS A 302
MASTER 253 0 1 18 8 0 2 6 2810 1 3 24
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