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HEADER LYASE 27-APR-23 8SNI
TITLE HYDROXYNITRILE LYASE FROM HEVEA BRASILIENSIS WITH FORTY MUTATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: (S)-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B;
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 M.E.WALSH,L.R.GREENBERG,R.J.KAZLAUSKAS,C.T.PIERCE,H.AIHARA,R.L.EVANS,
AUTHOR 2 K.SHI
REVDAT 1 28-FEB-24 8SNI 0
JRNL AUTH M.E.WALSH,L.R.GREENBERG
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
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) : 60.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 39116
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 2007
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 60.8500 - 4.8000 0.92 2664 143 0.1602 0.1703
REMARK 3 2 4.8000 - 3.8100 0.97 2676 142 0.1494 0.1547
REMARK 3 3 3.8100 - 3.3300 0.98 2667 147 0.1962 0.2228
REMARK 3 4 3.3300 - 3.0200 0.97 2618 145 0.2172 0.2375
REMARK 3 5 3.0200 - 2.8000 0.98 2670 149 0.2340 0.2537
REMARK 3 6 2.8000 - 2.6400 0.99 2661 135 0.2344 0.2984
REMARK 3 7 2.6400 - 2.5100 1.00 2673 160 0.2192 0.2865
REMARK 3 8 2.5100 - 2.4000 1.00 2666 129 0.2181 0.2720
REMARK 3 9 2.4000 - 2.3100 1.00 2670 147 0.2222 0.2548
REMARK 3 10 2.3100 - 2.2300 0.98 2608 140 0.2394 0.2709
REMARK 3 11 2.2300 - 2.1600 0.98 2597 141 0.2437 0.2970
REMARK 3 12 2.1600 - 2.0900 0.99 2666 134 0.2702 0.3065
REMARK 3 13 2.0900 - 2.0400 0.99 2613 150 0.2834 0.3296
REMARK 3 14 2.0400 - 1.9900 0.99 2660 145 0.3055 0.3504
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) : 0.272
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.022
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.61
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 4150
REMARK 3 ANGLE : 0.937 5643
REMARK 3 CHIRALITY : 0.056 609
REMARK 3 PLANARITY : 0.007 719
REMARK 3 DIHEDRAL : 11.291 550
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 8SNI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1000273121.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-22
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 : 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 EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39196
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 60.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : 0.06600
REMARK 200 FOR THE DATA SET : 10.5000
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.96700
REMARK 200 R SYM FOR SHELL (I) : 0.96700
REMARK 200 FOR SHELL : 1.300
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 (%): 43.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 0.2 M L-PROLINE,
REMARK 280 10 % W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295K
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 38.26350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.46450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.94200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.46450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.26350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.94200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 -33
REMARK 465 GLY A -32
REMARK 465 SER A -31
REMARK 465 SER A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 SER A -23
REMARK 465 SER A -22
REMARK 465 GLY A -21
REMARK 465 LEU A -20
REMARK 465 VAL A -19
REMARK 465 PRO A -18
REMARK 465 ARG A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 MET A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET B -33
REMARK 465 GLY B -32
REMARK 465 SER B -31
REMARK 465 SER B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 SER B -23
REMARK 465 SER B -22
REMARK 465 GLY B -21
REMARK 465 LEU B -20
REMARK 465 VAL B -19
REMARK 465 PRO B -18
REMARK 465 ARG B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
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 ALA A 2 CB
REMARK 470 LYS A 32 CD CE NZ
REMARK 470 GLU A 66 OE1 OE2
REMARK 470 LEU A 68 CD2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 GLU A 95 CG CD OE1 OE2
REMARK 470 LYS A 120 CD CE NZ
REMARK 470 ASN A 122 ND2
REMARK 470 LEU A 131 CD2
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 LYS A 153 CD CE NZ
REMARK 470 LYS A 177 NZ
REMARK 470 LEU A 180 CD1
REMARK 470 ILE A 184 CG2 CD1
REMARK 470 ALA A 186 CB
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 GLU A 194 CG CD OE1 OE2
REMARK 470 LYS A 200 CE NZ
REMARK 470 GLU A 215 CD OE1 OE2
REMARK 470 LEU A 218 CD2
REMARK 470 GLU A 222 CD OE1 OE2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 LYS A 228 CG CD CE NZ
REMARK 470 GLU A 233 CB CG CD OE1 OE2
REMARK 470 LYS A 243 NZ
REMARK 470 ALA B 2 CB
REMARK 470 LYS B 32 CE NZ
REMARK 470 GLU B 66 OE1 OE2
REMARK 470 LYS B 73 CE NZ
REMARK 470 LYS B 92 CG CD CE NZ
REMARK 470 LYS B 120 CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 LYS B 153 CG CD CE NZ
REMARK 470 GLU B 166 CD OE1 OE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 LYS B 193 CD CE NZ
REMARK 470 LYS B 200 CE NZ
REMARK 470 LEU B 218 CD1
REMARK 470 LYS B 228 NZ
REMARK 470 LYS B 245 CG CD 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 -1.63 69.03
REMARK 500 HIS A 14 -164.53 -107.86
REMARK 500 SER A 80 -123.04 61.75
REMARK 500 LEU A 131 -120.64 47.30
REMARK 500 TYR A 224 88.57 -152.41
REMARK 500 MET A 238 54.42 -97.12
REMARK 500 HIS B 14 -166.88 -109.80
REMARK 500 SER B 80 -122.12 62.25
REMARK 500 LEU B 131 -120.70 46.10
REMARK 500 TYR B 224 87.61 -151.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8SNI A 1 259 UNP P52704 HNL_HEVBR 1 257
DBREF 8SNI B 1 259 UNP P52704 HNL_HEVBR 1 257
SEQADV 8SNI MET A -33 UNP P52704 INITIATING METHIONINE
SEQADV 8SNI GLY A -32 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A -31 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A -30 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -29 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -28 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -27 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -26 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -25 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -24 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A -23 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A -22 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY A -21 UNP P52704 EXPRESSION TAG
SEQADV 8SNI LEU A -20 UNP P52704 EXPRESSION TAG
SEQADV 8SNI VAL A -19 UNP P52704 EXPRESSION TAG
SEQADV 8SNI PRO A -18 UNP P52704 EXPRESSION TAG
SEQADV 8SNI ARG A -17 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY A -16 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A -15 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS A -14 UNP P52704 EXPRESSION TAG
SEQADV 8SNI MET A -13 UNP P52704 EXPRESSION TAG
SEQADV 8SNI ALA A -12 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A -11 UNP P52704 EXPRESSION TAG
SEQADV 8SNI MET A -10 UNP P52704 EXPRESSION TAG
SEQADV 8SNI THR A -9 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY A -8 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY A -7 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLN A -6 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLN A -5 UNP P52704 EXPRESSION TAG
SEQADV 8SNI MET A -4 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY A -3 UNP P52704 EXPRESSION TAG
SEQADV 8SNI ARG A -2 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY A -1 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER A 0 UNP P52704 EXPRESSION TAG
SEQADV 8SNI VAL A 9 UNP P52704 ILE 9 ENGINEERED MUTATION
SEQADV 8SNI GLY A 11 UNP P52704 THR 11 ENGINEERED MUTATION
SEQADV 8SNI ALA A 12 UNP P52704 ILE 12 ENGINEERED MUTATION
SEQADV 8SNI SER A 18 UNP P52704 ILE 18 ENGINEERED MUTATION
SEQADV 8SNI HIS A 79 UNP P52704 GLU 79 ENGINEERED MUTATION
SEQADV 8SNI LEU A 81 UNP P52704 CYS 81 ENGINEERED MUTATION
SEQADV 8SNI MET A 84 UNP P52704 LEU 84 ENGINEERED MUTATION
SEQADV 8SNI LEU A 103 UNP P52704 HIS 103 ENGINEERED MUTATION
SEQADV 8SNI ALA A 104 UNP P52704 ASN 104 ENGINEERED MUTATION
SEQADV 8SNI ALA A 105 UNP P52704 SER 105 ENGINEERED MUTATION
SEQADV 8SNI PHE A 106 UNP P52704 VAL 106 ENGINEERED MUTATION
SEQADV 8SNI LEU A 118 UNP P52704 VAL 118 ENGINEERED MUTATION
SEQADV 8SNI TYR A 121 UNP P52704 LEU 121 ENGINEERED MUTATION
SEQADV 8SNI ASN A 122 UNP P52704 MET 122 ENGINEERED MUTATION
SEQADV 8SNI THR A 125 UNP P52704 PHE 125 ENGINEERED MUTATION
SEQADV 8SNI ALA A 127 UNP P52704 INSERTION
SEQADV 8SNI GLU A 128 UNP P52704 INSERTION
SEQADV 8SNI ASN A 129 UNP P52704 ASP 127 ENGINEERED MUTATION
SEQADV 8SNI LEU A 131 UNP P52704 LYS 129 ENGINEERED MUTATION
SEQADV 8SNI PHE A 135 UNP P52704 TYR 133 ENGINEERED MUTATION
SEQADV 8SNI MET A 148 UNP P52704 LEU 146 ENGINEERED MUTATION
SEQADV 8SNI PHE A 149 UNP P52704 LYS 147 ENGINEERED MUTATION
SEQADV 8SNI PHE A 150 UNP P52704 LEU 148 ENGINEERED MUTATION
SEQADV 8SNI PRO A 152 UNP P52704 PHE 150 ENGINEERED MUTATION
SEQADV 8SNI LYS A 153 UNP P52704 THR 151 ENGINEERED MUTATION
SEQADV 8SNI PHE A 154 UNP P52704 LEU 152 ENGINEERED MUTATION
SEQADV 8SNI ALA A 156 UNP P52704 ARG 154 ENGINEERED MUTATION
SEQADV 8SNI HIS A 157 UNP P52704 GLU 155 ENGINEERED MUTATION
SEQADV 8SNI LYS A 158 UNP P52704 ASN 156 ENGINEERED MUTATION
SEQADV 8SNI GLN A 161 UNP P52704 THR 159 ENGINEERED MUTATION
SEQADV 8SNI VAL A 175 UNP P52704 THR 173 ENGINEERED MUTATION
SEQADV 8SNI SER A 178 UNP P52704 GLY 176 ENGINEERED MUTATION
SEQADV 8SNI MET A 182 UNP P52704 GLN 180 ENGINEERED MUTATION
SEQADV 8SNI LYS A 210 UNP P52704 GLU 208 ENGINEERED MUTATION
SEQADV 8SNI GLY A 211 UNP P52704 ILE 209 ENGINEERED MUTATION
SEQADV 8SNI ILE A 212 UNP P52704 PHE 210 ENGINEERED MUTATION
SEQADV 8SNI PRO A 213 UNP P52704 LEU 211 ENGINEERED MUTATION
SEQADV 8SNI MET A 238 UNP P52704 LYS 236 ENGINEERED MUTATION
SEQADV 8SNI ALA A 239 UNP P52704 LEU 237 ENGINEERED MUTATION
SEQADV 8SNI MET A 240 UNP P52704 GLN 238 ENGINEERED MUTATION
SEQADV 8SNI MET B -33 UNP P52704 INITIATING METHIONINE
SEQADV 8SNI GLY B -32 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B -31 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B -30 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -29 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -28 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -27 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -26 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -25 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -24 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B -23 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B -22 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY B -21 UNP P52704 EXPRESSION TAG
SEQADV 8SNI LEU B -20 UNP P52704 EXPRESSION TAG
SEQADV 8SNI VAL B -19 UNP P52704 EXPRESSION TAG
SEQADV 8SNI PRO B -18 UNP P52704 EXPRESSION TAG
SEQADV 8SNI ARG B -17 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY B -16 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B -15 UNP P52704 EXPRESSION TAG
SEQADV 8SNI HIS B -14 UNP P52704 EXPRESSION TAG
SEQADV 8SNI MET B -13 UNP P52704 EXPRESSION TAG
SEQADV 8SNI ALA B -12 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B -11 UNP P52704 EXPRESSION TAG
SEQADV 8SNI MET B -10 UNP P52704 EXPRESSION TAG
SEQADV 8SNI THR B -9 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY B -8 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY B -7 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLN B -6 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLN B -5 UNP P52704 EXPRESSION TAG
SEQADV 8SNI MET B -4 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY B -3 UNP P52704 EXPRESSION TAG
SEQADV 8SNI ARG B -2 UNP P52704 EXPRESSION TAG
SEQADV 8SNI GLY B -1 UNP P52704 EXPRESSION TAG
SEQADV 8SNI SER B 0 UNP P52704 EXPRESSION TAG
SEQADV 8SNI VAL B 9 UNP P52704 ILE 9 ENGINEERED MUTATION
SEQADV 8SNI GLY B 11 UNP P52704 THR 11 ENGINEERED MUTATION
SEQADV 8SNI ALA B 12 UNP P52704 ILE 12 ENGINEERED MUTATION
SEQADV 8SNI SER B 18 UNP P52704 ILE 18 ENGINEERED MUTATION
SEQADV 8SNI HIS B 79 UNP P52704 GLU 79 ENGINEERED MUTATION
SEQADV 8SNI LEU B 81 UNP P52704 CYS 81 ENGINEERED MUTATION
SEQADV 8SNI MET B 84 UNP P52704 LEU 84 ENGINEERED MUTATION
SEQADV 8SNI LEU B 103 UNP P52704 HIS 103 ENGINEERED MUTATION
SEQADV 8SNI ALA B 104 UNP P52704 ASN 104 ENGINEERED MUTATION
SEQADV 8SNI ALA B 105 UNP P52704 SER 105 ENGINEERED MUTATION
SEQADV 8SNI PHE B 106 UNP P52704 VAL 106 ENGINEERED MUTATION
SEQADV 8SNI LEU B 118 UNP P52704 VAL 118 ENGINEERED MUTATION
SEQADV 8SNI TYR B 121 UNP P52704 LEU 121 ENGINEERED MUTATION
SEQADV 8SNI ASN B 122 UNP P52704 MET 122 ENGINEERED MUTATION
SEQADV 8SNI THR B 125 UNP P52704 PHE 125 ENGINEERED MUTATION
SEQADV 8SNI ALA B 127 UNP P52704 INSERTION
SEQADV 8SNI GLU B 128 UNP P52704 INSERTION
SEQADV 8SNI ASN B 129 UNP P52704 ASP 127 ENGINEERED MUTATION
SEQADV 8SNI LEU B 131 UNP P52704 LYS 129 ENGINEERED MUTATION
SEQADV 8SNI PHE B 135 UNP P52704 TYR 133 ENGINEERED MUTATION
SEQADV 8SNI MET B 148 UNP P52704 LEU 146 ENGINEERED MUTATION
SEQADV 8SNI PHE B 149 UNP P52704 LYS 147 ENGINEERED MUTATION
SEQADV 8SNI PHE B 150 UNP P52704 LEU 148 ENGINEERED MUTATION
SEQADV 8SNI PRO B 152 UNP P52704 PHE 150 ENGINEERED MUTATION
SEQADV 8SNI LYS B 153 UNP P52704 THR 151 ENGINEERED MUTATION
SEQADV 8SNI PHE B 154 UNP P52704 LEU 152 ENGINEERED MUTATION
SEQADV 8SNI ALA B 156 UNP P52704 ARG 154 ENGINEERED MUTATION
SEQADV 8SNI HIS B 157 UNP P52704 GLU 155 ENGINEERED MUTATION
SEQADV 8SNI LYS B 158 UNP P52704 ASN 156 ENGINEERED MUTATION
SEQADV 8SNI GLN B 161 UNP P52704 THR 159 ENGINEERED MUTATION
SEQADV 8SNI VAL B 175 UNP P52704 THR 173 ENGINEERED MUTATION
SEQADV 8SNI SER B 178 UNP P52704 GLY 176 ENGINEERED MUTATION
SEQADV 8SNI MET B 182 UNP P52704 GLN 180 ENGINEERED MUTATION
SEQADV 8SNI LYS B 210 UNP P52704 GLU 208 ENGINEERED MUTATION
SEQADV 8SNI GLY B 211 UNP P52704 ILE 209 ENGINEERED MUTATION
SEQADV 8SNI ILE B 212 UNP P52704 PHE 210 ENGINEERED MUTATION
SEQADV 8SNI PRO B 213 UNP P52704 LEU 211 ENGINEERED MUTATION
SEQADV 8SNI MET B 238 UNP P52704 LYS 236 ENGINEERED MUTATION
SEQADV 8SNI ALA B 239 UNP P52704 LEU 237 ENGINEERED MUTATION
SEQADV 8SNI MET B 240 UNP P52704 GLN 238 ENGINEERED MUTATION
SEQRES 1 A 293 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 293 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 293 GLY GLN GLN MET GLY ARG GLY SER MET ALA PHE ALA HIS
SEQRES 4 A 293 PHE VAL LEU VAL HIS GLY ALA CYS HIS GLY ALA TRP SER
SEQRES 5 A 293 TRP HIS LYS LEU LYS PRO LEU LEU GLU ALA LEU GLY HIS
SEQRES 6 A 293 LYS VAL THR ALA LEU ASP LEU ALA ALA SER GLY VAL ASP
SEQRES 7 A 293 PRO ARG GLN ILE GLU GLU ILE GLY SER PHE ASP GLU TYR
SEQRES 8 A 293 SER GLU PRO LEU LEU THR PHE LEU GLU ALA LEU PRO PRO
SEQRES 9 A 293 GLY GLU LYS VAL ILE LEU VAL GLY HIS SER LEU GLY GLY
SEQRES 10 A 293 MET ASN ILE ALA ILE ALA ALA ASP LYS TYR CYS GLU LYS
SEQRES 11 A 293 ILE ALA ALA ALA VAL PHE LEU ALA ALA PHE LEU PRO ASP
SEQRES 12 A 293 THR GLU HIS CYS PRO SER TYR VAL LEU ASP LYS TYR ASN
SEQRES 13 A 293 GLU VAL THR PRO ALA GLU ASN TRP LEU ASP THR THR PHE
SEQRES 14 A 293 PHE THR TYR THR LYS ASP GLY LYS GLU ILE THR GLY MET
SEQRES 15 A 293 PHE PHE GLY PRO LYS PHE LEU ALA HIS LYS LEU TYR GLN
SEQRES 16 A 293 LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA LYS MET LEU
SEQRES 17 A 293 VAL ARG LYS SER SER LEU PHE MET ASN ILE LEU ALA LYS
SEQRES 18 A 293 ARG PRO PHE PHE THR LYS GLU GLY TYR GLY SER ILE LYS
SEQRES 19 A 293 LYS ILE TYR VAL TRP THR ASP GLN ASP LYS GLY ILE PRO
SEQRES 20 A 293 PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN TYR LYS PRO
SEQRES 21 A 293 ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP HIS MET ALA
SEQRES 22 A 293 MET LEU THR LYS THR LYS GLU ILE ALA GLU ILE LEU GLN
SEQRES 23 A 293 GLU VAL ALA ASP THR TYR ASN
SEQRES 1 B 293 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 293 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 293 GLY GLN GLN MET GLY ARG GLY SER MET ALA PHE ALA HIS
SEQRES 4 B 293 PHE VAL LEU VAL HIS GLY ALA CYS HIS GLY ALA TRP SER
SEQRES 5 B 293 TRP HIS LYS LEU LYS PRO LEU LEU GLU ALA LEU GLY HIS
SEQRES 6 B 293 LYS VAL THR ALA LEU ASP LEU ALA ALA SER GLY VAL ASP
SEQRES 7 B 293 PRO ARG GLN ILE GLU GLU ILE GLY SER PHE ASP GLU TYR
SEQRES 8 B 293 SER GLU PRO LEU LEU THR PHE LEU GLU ALA LEU PRO PRO
SEQRES 9 B 293 GLY GLU LYS VAL ILE LEU VAL GLY HIS SER LEU GLY GLY
SEQRES 10 B 293 MET ASN ILE ALA ILE ALA ALA ASP LYS TYR CYS GLU LYS
SEQRES 11 B 293 ILE ALA ALA ALA VAL PHE LEU ALA ALA PHE LEU PRO ASP
SEQRES 12 B 293 THR GLU HIS CYS PRO SER TYR VAL LEU ASP LYS TYR ASN
SEQRES 13 B 293 GLU VAL THR PRO ALA GLU ASN TRP LEU ASP THR THR PHE
SEQRES 14 B 293 PHE THR TYR THR LYS ASP GLY LYS GLU ILE THR GLY MET
SEQRES 15 B 293 PHE PHE GLY PRO LYS PHE LEU ALA HIS LYS LEU TYR GLN
SEQRES 16 B 293 LEU CYS GLY PRO GLU GLU TYR GLU LEU ALA LYS MET LEU
SEQRES 17 B 293 VAL ARG LYS SER SER LEU PHE MET ASN ILE LEU ALA LYS
SEQRES 18 B 293 ARG PRO PHE PHE THR LYS GLU GLY TYR GLY SER ILE LYS
SEQRES 19 B 293 LYS ILE TYR VAL TRP THR ASP GLN ASP LYS GLY ILE PRO
SEQRES 20 B 293 PRO GLU PHE GLN LEU TRP GLN ILE GLU ASN TYR LYS PRO
SEQRES 21 B 293 ASP LYS VAL TYR LYS VAL GLU GLY GLY ASP HIS MET ALA
SEQRES 22 B 293 MET LEU THR LYS THR LYS GLU ILE ALA GLU ILE LEU GLN
SEQRES 23 B 293 GLU VAL ALA ASP THR TYR ASN
HET EDO A 301 4
HET SO4 A 302 5
HET SO4 A 303 5
HET BEZ A 304 9
HET BEZ B 301 9
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM BEZ BENZOIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO C2 H6 O2
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 6 BEZ 2(C7 H6 O2)
FORMUL 8 HOH *68(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 THR A 125 1 11
HELIX 8 AA8 PRO A 126 LEU A 131 5 6
HELIX 9 AA9 GLY A 151 LEU A 159 1 9
HELIX 10 AB1 GLY A 164 VAL A 175 1 12
HELIX 11 AB2 PHE A 181 LYS A 187 1 7
HELIX 12 AB3 GLY A 195 ILE A 199 5 5
HELIX 13 AB4 PRO A 213 TYR A 224 1 12
HELIX 14 AB5 MET A 238 LYS A 243 1 6
HELIX 15 AB6 LYS A 243 ASN A 259 1 17
HELIX 16 AB7 GLY B 15 HIS B 20 5 6
HELIX 17 AB8 LYS B 21 LEU B 29 1 9
HELIX 18 AB9 GLN B 47 ILE B 51 5 5
HELIX 19 AC1 SER B 53 SER B 58 1 6
HELIX 20 AC2 SER B 58 ALA B 67 1 10
HELIX 21 AC3 LEU B 81 TYR B 93 1 13
HELIX 22 AC4 SER B 115 THR B 125 1 11
HELIX 23 AC5 PRO B 126 LEU B 131 5 6
HELIX 24 AC6 GLY B 151 LEU B 159 1 9
HELIX 25 AC7 GLY B 164 VAL B 175 1 12
HELIX 26 AC8 PHE B 181 LYS B 187 1 7
HELIX 27 AC9 GLY B 195 ILE B 199 5 5
HELIX 28 AD1 PRO B 213 TYR B 224 1 12
HELIX 29 AD2 MET B 238 LYS B 243 1 6
HELIX 30 AD3 LYS B 243 ASN B 259 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 LYS A 201 THR A 206 1 O ILE A 202 N PHE A 102
SHEET 6 AA1 6 LYS A 228 VAL A 232 1 O VAL A 232 N TRP A 205
SHEET 1 AA2 3 THR A 134 LYS A 140 0
SHEET 2 AA2 3 LYS A 143 PHE A 149 -1 O ILE A 145 N TYR A 138
SHEET 3 AA2 3 SER A 178 SER A 179 -1 O SER A 178 N MET A 148
SHEET 1 AA3 6 LYS B 32 ALA B 35 0
SHEET 2 AA3 6 HIS B 5 VAL B 9 1 N PHE B 6 O LYS B 32
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 LEU B 103 N GLY B 78
SHEET 5 AA3 6 LYS B 201 THR B 206 1 O ILE B 202 N PHE B 102
SHEET 6 AA3 6 LYS B 228 VAL B 232 1 O TYR B 230 N TRP B 205
SHEET 1 AA4 2 THR B 134 LYS B 140 0
SHEET 2 AA4 2 LYS B 143 PHE B 149 -1 O GLY B 147 N PHE B 136
CRYST1 76.527 81.884 90.929 90.00 90.00 90.00 P 21 21 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 0.013067 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010998 0.00000
TER 1995 ASN A 259
TER 4005 ASN B 259
MASTER 359 0 5 30 17 0 0 6 4103 2 32 46
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