| content |
HEADER HYDROLASE 09-FEB-25 9N8R
TITLE LIPASE 1 FROM PSEUDOMONAS CHLORORAPHIS PA23
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS CHLORORAPHIS;
SOURCE 3 ORGANISM_TAXID: 587753;
SOURCE 4 STRAIN: PA23;
SOURCE 5 GENE: HLB40_08715;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: EXPRESSION VECTOR;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21(+)
KEYWDS A/B HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ROYAN,S.NEWTON,A.ARDEVOL,A.T.CAPUTO
REVDAT 1 11-FEB-26 9N8R 0
JRNL AUTH S.ROYAN,S.NEWTON,A.ARDEVOL,A.T.CAPUTO
JRNL TITL STRUCTURE OF BIOPLASTIC DEGRADING ENZYME LIP1 FROM
JRNL TITL 2 PSEUDOMONAS CHLORORAPHIS PA23 TO 1.62 ANGSTROMS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN,
REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY,
REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON,
REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL,
REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS,
REMARK 1 AUTH 6 P.D.ADAMS
REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS,
REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX
REMARK 1 REF ACTA CRYSTALLOGR D STRUCT 2019
REMARK 1 REF 2 BIOL
REMARK 1 REFN
REMARK 1 PMID 31588918
REMARK 1 DOI 10.1107/S2059798319011471
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 36337
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1819
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 42.5100 - 3.8100 1.00 2851 139 0.1805 0.1890
REMARK 3 2 3.8100 - 3.0200 1.00 2720 132 0.1383 0.1477
REMARK 3 3 3.0200 - 2.6400 1.00 2689 142 0.1375 0.1618
REMARK 3 4 2.6400 - 2.4000 1.00 2687 131 0.1324 0.1663
REMARK 3 5 2.4000 - 2.2300 1.00 2656 137 0.1378 0.1857
REMARK 3 6 2.2300 - 2.1000 1.00 2606 164 0.1350 0.1756
REMARK 3 7 2.1000 - 1.9900 1.00 2666 116 0.1376 0.1711
REMARK 3 8 1.9900 - 1.9000 1.00 2626 148 0.1433 0.1949
REMARK 3 9 1.9000 - 1.8300 1.00 2619 134 0.1658 0.2159
REMARK 3 10 1.8300 - 1.7700 1.00 2646 156 0.1873 0.2177
REMARK 3 11 1.7700 - 1.7100 1.00 2572 145 0.1907 0.2202
REMARK 3 12 1.7100 - 1.6600 1.00 2642 143 0.2023 0.2221
REMARK 3 13 1.6600 - 1.6200 0.97 2538 132 0.2300 0.2977
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.141
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.567
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.63
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.79
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 2208
REMARK 3 ANGLE : 0.971 3018
REMARK 3 CHIRALITY : 0.059 337
REMARK 3 PLANARITY : 0.010 394
REMARK 3 DIHEDRAL : 15.356 786
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 9N8R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-25.
REMARK 100 THE DEPOSITION ID IS D_1000292622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36418
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 43.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.61900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 7.1, 20.79% (W/V) PEG
REMARK 280 6000, 0.12 M CALCIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 34.29750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.65450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.29750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.65450
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA CA A 301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 502 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 565 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 587 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 9 OD2
REMARK 480 GLN A 23 NE2
REMARK 480 ALA A 70 CB
REMARK 480 GLU A 130 OE1 OE2
REMARK 480 GLY A 143 N CA
REMARK 480 HIS A 144 CG ND1 CD2 CE1 NE2
REMARK 480 GLU A 189 OE2
REMARK 480 ASP A 208 CG OD1 OD2
REMARK 480 LYS A 209 CD CE NZ
REMARK 480 LYS A 262 CE NZ
REMARK 480 GLN A 264 CB CG CD OE1 NE2
REMARK 480 GLU A 277 OE1 OE2
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 ARG A 8 -122.77 48.58
REMARK 500 CYS A 86 165.75 83.52
REMARK 500 HIS A 144 -114.62 71.96
REMARK 500 SER A 152 -122.75 59.99
REMARK 500 SER A 152 -121.26 57.51
REMARK 500 HIS A 206 47.55 -140.81
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 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 36 OE1
REMARK 620 2 GLN A 36 OE1 0.0
REMARK 620 3 ASP A 90 OD1 89.9 89.9
REMARK 620 4 ASP A 90 OD1 89.9 89.9 0.0
REMARK 620 5 HOH A 502 O 89.8 89.8 87.5 87.5
REMARK 620 6 HOH A 502 O 89.8 89.8 87.5 87.5 0.0
REMARK 620 7 HOH A 565 O 90.2 90.2 92.5 92.5 180.0 180.0
REMARK 620 8 HOH A 565 O 90.2 90.2 92.5 92.5 180.0 180.0 0.0
REMARK 620 N 1 2 3 4 5 6 7
DBREF 9N8R A 1 283 PDB 9N8R 9N8R 1 283
SEQRES 1 A 283 MET THR MET THR LEU LEU TYR ARG ASP MET ASN GLN ALA
SEQRES 2 A 283 GLN LEU ASP ALA ALA TYR ASN ASN THR GLN ALA VAL PRO
SEQRES 3 A 283 ASP PHE PRO GLY ILE TYR ALA ALA LEU GLN ALA ARG SER
SEQRES 4 A 283 ALA SER PHE TYR ALA SER ALA ALA GLY ARG LEU ASN LEU
SEQRES 5 A 283 PRO TYR GLY THR ALA PRO ARG GLN ARG TYR ASP TRP LEU
SEQRES 6 A 283 PRO CYS GLY LYS ALA ASP ALA PRO THR LEU ILE PHE ILE
SEQRES 7 A 283 HIS GLY GLY TYR TRP GLN ASN CYS SER LYS GLU ASP PHE
SEQRES 8 A 283 ALA PHE ILE ALA ALA GLY PRO LEU ALA ALA GLY PHE ASN
SEQRES 9 A 283 ILE VAL LEU ALA GLU TYR THR LEU ALA PRO GLN ALA SER
SEQRES 10 A 283 MET THR GLN ILE VAL SER GLU ILE GLY SER LEU LEU GLU
SEQRES 11 A 283 HIS LEU GLN ALA ASP ALA ASP GLN LEU GLY ILE ALA GLY
SEQRES 12 A 283 HIS LYS VAL VAL LEU SER GLY HIS SER ALA GLY GLY HIS
SEQRES 13 A 283 LEU ALA LEU GLN PHE ARG SER HIS PRO TRP VAL THR ASP
SEQRES 14 A 283 VAL LEU ALA ILE SER ALA LEU VAL ASP LEU GLU PRO ILE
SEQRES 15 A 283 SER LEU SER TRP LEU ASN GLU LYS LEU SER LEU SER GLU
SEQRES 16 A 283 ALA GLU ILE ASP ALA TYR SER PRO LEU TYR HIS ILE ASP
SEQRES 17 A 283 LYS GLY ALA ASN THR TRP VAL ALA VAL GLY ALA ASP GLU
SEQRES 18 A 283 LEU SER GLU LEU VAL ARG GLN SER ASP GLU TYR ALA LYS
SEQRES 19 A 283 GLN ALA LEU ALA ARG GLY GLU SER VAL GLN LEU ILE HIS
SEQRES 20 A 283 VAL PRO GLY CYS THR HIS PHE SER VAL LEU ASP GLU MET
SEQRES 21 A 283 ALA LYS PRO GLN GLY ALA LEU LEU GLN ALA LEU SER SER
SEQRES 22 A 283 ILE ARG LEU GLU HIS HIS HIS HIS HIS HIS
HET CA A 301 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
FORMUL 3 HOH *193(H2 O)
HELIX 1 AA1 ASN A 11 ASN A 20 1 10
HELIX 2 AA2 ASN A 20 VAL A 25 1 6
HELIX 3 AA3 ASP A 27 ALA A 46 1 20
HELIX 4 AA4 SER A 87 ALA A 92 1 6
HELIX 5 AA5 ALA A 95 ALA A 101 1 7
HELIX 6 AA6 SER A 117 ALA A 134 1 18
HELIX 7 AA7 SER A 152 PHE A 161 1 10
HELIX 8 AA8 ASP A 178 SER A 185 1 8
HELIX 9 AA9 LEU A 187 SER A 192 1 6
HELIX 10 AB1 SER A 194 TYR A 201 1 8
HELIX 11 AB2 SER A 202 HIS A 206 5 5
HELIX 12 AB3 LEU A 222 ARG A 239 1 18
HELIX 13 AB4 PHE A 254 VAL A 256 5 3
HELIX 14 AB5 LEU A 257 LYS A 262 1 6
HELIX 15 AB6 LEU A 267 HIS A 280 1 14
SHEET 1 AA1 8 ARG A 49 PRO A 53 0
SHEET 2 AA1 8 ARG A 61 LEU A 65 -1 O TYR A 62 N LEU A 52
SHEET 3 AA1 8 ASN A 104 ALA A 108 -1 O ILE A 105 N LEU A 65
SHEET 4 AA1 8 THR A 74 ILE A 78 1 N PHE A 77 O VAL A 106
SHEET 5 AA1 8 VAL A 146 HIS A 151 1 O VAL A 147 N ILE A 76
SHEET 6 AA1 8 ASP A 169 ILE A 173 1 O ILE A 173 N GLY A 150
SHEET 7 AA1 8 ASN A 212 GLY A 218 1 O TRP A 214 N ALA A 172
SHEET 8 AA1 8 VAL A 243 VAL A 248 1 O GLN A 244 N VAL A 215
LINK OE1 GLN A 36 CA CA A 301 1555 1555 2.32
LINK OE1 GLN A 36 CA CA A 301 1555 2655 2.32
LINK OD1 ASP A 90 CA CA A 301 1555 1555 2.31
LINK OD1 ASP A 90 CA CA A 301 1555 2655 2.31
LINK CA CA A 301 O HOH A 502 1555 1555 2.39
LINK CA CA A 301 O HOH A 502 1555 2655 2.39
LINK CA CA A 301 O HOH A 565 1555 1555 2.43
LINK CA CA A 301 O HOH A 565 1555 2655 2.43
CISPEP 1 ALA A 113 PRO A 114 0 7.46
CRYST1 68.595 75.309 54.155 90.00 90.00 90.00 P 21 21 2 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 0.014578 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018466 0.00000
TER 4258 HIS A 280
MASTER 297 0 1 15 8 0 0 6 2322 1 5 22
END |