| content |
HEADER LYASE 19-OCT-22 8EUO
TITLE HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS WITH SEVEN MUTATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: (S)-ACETONE-CYANOHYDRIN LYASE,OXYNITRILASE;
COMPND 5 EC: 4.1.2.47;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEVEA BRASILIENSIS;
SOURCE 3 ORGANISM_COMMON: RUBBER TREE;
SOURCE 4 ORGANISM_TAXID: 3981;
SOURCE 5 GENE: HNL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENGINEERED PROTEIN, ALPHA/BETA HYDROLASE FOLD, ESTERASE, CATALYTIC
KEYWDS 2 PROMISCUITY, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.R.GREENBERG,M.E.WALSH,R.J.KAZLAUSKAS,C.T.PIERCE,K.SHI,H.AIHARA,
AUTHOR 2 R.L.EVANS
REVDAT 1 30-NOV-22 8EUO 0
JRNL AUTH L.R.GREENBERG,M.E.WALSH,R.J.KAZLAUSKAS,C.T.PIERCE,K.SHI,
JRNL AUTH 2 H.AIHARA,R.L.EVANS
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 68 352 2012
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 1 REFERENCE 2
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 V. 75 861 2019
REMARK 1 REF 2 BIOL
REMARK 1 REFN ISSN 2059-7983
REMARK 1 PMID 31588918
REMARK 1 DOI 10.1107/S2059798319011471
REMARK 2
REMARK 2 RESOLUTION. 1.99 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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 20181
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 43.0300 - 4.7900 0.84 1316 145 0.1580 0.2063
REMARK 3 2 4.7900 - 3.8100 0.77 1143 126 0.1371 0.1677
REMARK 3 3 3.8000 - 3.3200 0.80 1179 129 0.1723 0.2188
REMARK 3 4 3.3200 - 3.0200 0.86 1253 138 0.2079 0.2712
REMARK 3 5 3.0200 - 2.8000 0.88 1272 140 0.2111 0.2503
REMARK 3 6 2.8000 - 2.6400 0.89 1271 140 0.2130 0.2815
REMARK 3 7 2.6400 - 2.5100 0.91 1326 145 0.2032 0.2444
REMARK 3 8 2.5100 - 2.4000 0.94 1346 149 0.2088 0.3119
REMARK 3 9 2.4000 - 2.3100 0.94 1347 148 0.1985 0.2788
REMARK 3 10 2.3100 - 2.2300 0.95 1347 148 0.1915 0.2431
REMARK 3 11 2.2300 - 2.1600 0.96 1375 151 0.1888 0.2712
REMARK 3 12 2.1600 - 2.0900 0.97 1402 155 0.2155 0.2745
REMARK 3 13 2.0900 - 2.0400 0.97 1375 150 0.2145 0.2773
REMARK 3 14 2.0400 - 1.9900 0.85 1229 136 0.2309 0.2558
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.039
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.09
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.63
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 2090
REMARK 3 ANGLE : 1.028 2851
REMARK 3 CHIRALITY : 0.060 320
REMARK 3 PLANARITY : 0.008 359
REMARK 3 DIHEDRAL : 6.718 281
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 8EUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-22.
REMARK 100 THE DEPOSITION ID IS D_1000268394.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
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 EIGER2 S 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 721.3
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 721.3
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20181
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 43.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.74800
REMARK 200 R SYM FOR SHELL (I) : 0.74800
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: PHENIX 1.19.2_4158
REMARK 200 STARTING MODEL: 3C6X
REMARK 200
REMARK 200 REMARK: ELONGATED TRAPEZOID
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS TRIS, 2.0 M AMMONIUM
REMARK 280 SULFATE, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 64.19800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.19800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.52700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.18900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.52700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.18900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.19800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.52700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.18900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 64.19800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.52700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.18900
REMARK 290 SMTRY3 8 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 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 ALA A 2
REMARK 465 LEU A 258
REMARK 465 GLU A 259
REMARK 465 HIS A 260
REMARK 465 HIS A 261
REMARK 465 HIS A 262
REMARK 465 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
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 LEU A 29 CD1
REMARK 470 LYS A 32 CD CE NZ
REMARK 470 LYS A 73 CE NZ
REMARK 470 LYS A 92 CD CE NZ
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 GLU A 123 CG CD OE1 OE2
REMARK 470 LYS A 141 CD CE NZ
REMARK 470 GLU A 142 OE1 OE2
REMARK 470 LEU A 160 CD1
REMARK 470 GLU A 164 CB CG CD OE1 OE2
REMARK 470 LYS A 185 CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLU A 192 CD OE1 OE2
REMARK 470 GLU A 208 OE2
REMARK 470 LYS A 243 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP A 139 O HOH A 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 HIS A 14 -168.70 -115.48
REMARK 500 SER A 80 -125.62 57.22
REMARK 500 ASP A 109 -169.21 -125.05
REMARK 500 LYS A 129 -127.41 59.16
REMARK 500 TYR A 158 38.50 -96.03
REMARK 500 SER A 176 -157.22 -147.96
REMARK 500 SER A 176 -157.22 -147.81
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8EUO A 1 257 UNP P52704 HNL_HEVBR 1 257
SEQADV 8EUO GLY A 11 UNP P52704 THR 11 ENGINEERED MUTATION
SEQADV 8EUO HIS A 79 UNP P52704 GLU 79 ENGINEERED MUTATION
SEQADV 8EUO LEU A 81 UNP P52704 CYS 81 ENGINEERED MUTATION
SEQADV 8EUO VAL A 103 UNP P52704 HIS 103 ENGINEERED MUTATION
SEQADV 8EUO ALA A 104 UNP P52704 ASN 104 ENGINEERED MUTATION
SEQADV 8EUO SER A 176 UNP P52704 GLY 176 ENGINEERED MUTATION
SEQADV 8EUO MET A 236 UNP P52704 LYS 236 ENGINEERED MUTATION
SEQADV 8EUO LEU A 258 UNP P52704 EXPRESSION TAG
SEQADV 8EUO GLU A 259 UNP P52704 EXPRESSION TAG
SEQADV 8EUO HIS A 260 UNP P52704 EXPRESSION TAG
SEQADV 8EUO HIS A 261 UNP P52704 EXPRESSION TAG
SEQADV 8EUO HIS A 262 UNP P52704 EXPRESSION TAG
SEQADV 8EUO HIS A 263 UNP P52704 EXPRESSION TAG
SEQADV 8EUO HIS A 264 UNP P52704 EXPRESSION TAG
SEQADV 8EUO HIS A 265 UNP P52704 EXPRESSION TAG
SEQRES 1 A 265 MET ALA PHE ALA HIS PHE VAL LEU ILE HIS GLY ILE CYS
SEQRES 2 A 265 HIS GLY ALA TRP ILE TRP HIS LYS LEU LYS PRO LEU LEU
SEQRES 3 A 265 GLU ALA LEU GLY HIS LYS VAL THR ALA LEU ASP LEU ALA
SEQRES 4 A 265 ALA SER GLY VAL ASP PRO ARG GLN ILE GLU GLU ILE GLY
SEQRES 5 A 265 SER PHE ASP GLU TYR SER GLU PRO LEU LEU THR PHE LEU
SEQRES 6 A 265 GLU ALA LEU PRO PRO GLY GLU LYS VAL ILE LEU VAL GLY
SEQRES 7 A 265 HIS SER LEU GLY GLY LEU ASN ILE ALA ILE ALA ALA ASP
SEQRES 8 A 265 LYS TYR CYS GLU LYS ILE ALA ALA ALA VAL PHE VAL ALA
SEQRES 9 A 265 SER VAL LEU PRO ASP THR GLU HIS CYS PRO SER TYR VAL
SEQRES 10 A 265 VAL ASP LYS LEU MET GLU VAL PHE PRO ASP TRP LYS ASP
SEQRES 11 A 265 THR THR TYR PHE THR TYR THR LYS ASP GLY LYS GLU ILE
SEQRES 12 A 265 THR GLY LEU LYS LEU GLY PHE THR LEU LEU ARG GLU ASN
SEQRES 13 A 265 LEU TYR THR LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA
SEQRES 14 A 265 LYS MET LEU THR ARG LYS SER SER LEU PHE GLN ASN ILE
SEQRES 15 A 265 LEU ALA LYS ARG PRO PHE PHE THR LYS GLU GLY TYR GLY
SEQRES 16 A 265 SER ILE LYS LYS ILE TYR VAL TRP THR ASP GLN ASP GLU
SEQRES 17 A 265 ILE PHE LEU PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN
SEQRES 18 A 265 TYR LYS PRO ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP
SEQRES 19 A 265 HIS MET LEU GLN LEU THR LYS THR LYS GLU ILE ALA GLU
SEQRES 20 A 265 ILE LEU GLN GLU VAL ALA ASP THR TYR ASN LEU GLU HIS
SEQRES 21 A 265 HIS HIS HIS HIS HIS
FORMUL 2 HOH *132(H2 O)
HELIX 1 AA1 GLY A 15 HIS A 20 5 6
HELIX 2 AA2 LYS A 21 LEU A 29 1 9
HELIX 3 AA3 GLN A 47 ILE A 51 5 5
HELIX 4 AA4 SER A 53 SER A 58 1 6
HELIX 5 AA5 SER A 58 ALA A 67 1 10
HELIX 6 AA6 LEU A 81 CYS A 94 1 14
HELIX 7 AA7 SER A 115 PHE A 125 1 11
HELIX 8 AA8 GLY A 149 LEU A 157 1 9
HELIX 9 AA9 GLY A 162 THR A 173 1 12
HELIX 10 AB1 PHE A 179 ARG A 186 1 8
HELIX 11 AB2 GLY A 193 ILE A 197 5 5
HELIX 12 AB3 LEU A 211 TYR A 222 1 12
HELIX 13 AB4 MET A 236 LYS A 241 1 6
HELIX 14 AB5 LYS A 241 ASN A 257 1 17
SHEET 1 AA1 6 LYS A 32 LEU A 36 0
SHEET 2 AA1 6 HIS A 5 ILE A 9 1 N LEU A 8 O THR A 34
SHEET 3 AA1 6 VAL A 74 SER A 80 1 O VAL A 77 N ILE A 9
SHEET 4 AA1 6 ILE A 97 SER A 105 1 O VAL A 103 N GLY A 78
SHEET 5 AA1 6 LYS A 199 TRP A 203 1 O VAL A 202 N PHE A 102
SHEET 6 AA1 6 LYS A 226 LYS A 229 1 O LYS A 226 N TYR A 201
SHEET 1 AA2 3 THR A 132 LYS A 138 0
SHEET 2 AA2 3 LYS A 141 LYS A 147 -1 O ILE A 143 N TYR A 136
SHEET 3 AA2 3 SER A 176 SER A 177 -1 O SER A 176 N LEU A 146
CRYST1 47.054 106.378 128.396 90.00 90.00 90.00 C 2 2 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 0.021252 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007788 0.00000
TER 2030 ASN A 257
MASTER 313 0 0 14 9 0 0 6 2136 1 0 21
END |