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HEADER HYDROLASE 01-MAR-22 7Z2X
TITLE WILD-TYPE FERULIC ACID ESTERASE FROM LACTOBACILLUS BUCHNERI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LENTILACTOBACILLUS BUCHNERI;
SOURCE 3 ORGANISM_TAXID: 1581;
SOURCE 4 GENE: FAEA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: T1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS FERULIC ACID ESTERASE, LACTOBACILLUS BUCHNERI, WILD TYPE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,M.M.KESKITALO,C.DIVNE
REVDAT 1 30-NOV-22 7Z2X 0
JRNL AUTH K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,A.JIMENEZ QUERO,
JRNL AUTH 2 M.M.KESKITALO,F.VILAPLANA,C.DIVNE
JRNL TITL WILD-TYPE FERULIC ACID ESTERASE FROM LACTOBACILLUS BUCHNERI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.15.2_3472: ???)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 155652
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.280
REMARK 3 FREE R VALUE TEST SET COUNT : 1986
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 30.9340 - 3.6135 0.95 11136 142 0.1564 0.1457
REMARK 3 2 3.6135 - 2.8688 0.95 11119 144 0.1662 0.1887
REMARK 3 3 2.8688 - 2.5063 0.96 11184 147 0.1803 0.2423
REMARK 3 4 2.5063 - 2.2773 0.96 11245 139 0.1799 0.2273
REMARK 3 5 2.2773 - 2.1141 0.95 11181 150 0.1723 0.2078
REMARK 3 6 2.1141 - 1.9895 0.95 11197 126 0.1793 0.2338
REMARK 3 7 1.9895 - 1.8898 0.94 11046 158 0.1903 0.2257
REMARK 3 8 1.8898 - 1.8076 0.94 11072 145 0.1976 0.2332
REMARK 3 9 1.8076 - 1.7380 0.94 10943 136 0.2067 0.2471
REMARK 3 10 1.7380 - 1.6780 0.93 10906 144 0.2198 0.2839
REMARK 3 11 1.6780 - 1.6256 0.92 10876 135 0.2239 0.2460
REMARK 3 12 1.6256 - 1.5791 0.91 10660 138 0.2320 0.2552
REMARK 3 13 1.5791 - 1.5375 0.90 10583 153 0.2444 0.2564
REMARK 3 14 1.5375 - 1.5000 0.90 10518 129 0.2640 0.3002
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 8582
REMARK 3 ANGLE : 0.808 11581
REMARK 3 CHIRALITY : 0.051 1230
REMARK 3 PLANARITY : 0.005 1525
REMARK 3 DIHEDRAL : 16.205 5055
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 7Z2X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1292119942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-20
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 : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96852
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155659
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.934
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: L. BUCHNERI FAE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 0.2 M NACL, 25%
REMARK 280 P3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 LYS A 260
REMARK 465 MET B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 LYS B 260
REMARK 465 MET C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 SER C -14
REMARK 465 SER C -13
REMARK 465 GLY C -12
REMARK 465 VAL C -11
REMARK 465 ASP C -10
REMARK 465 LEU C -9
REMARK 465 GLY C -8
REMARK 465 THR C -7
REMARK 465 GLU C -6
REMARK 465 LYS C 260
REMARK 465 MET D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 SER D -14
REMARK 465 SER D -13
REMARK 465 GLY D -12
REMARK 465 VAL D -11
REMARK 465 ASP D -10
REMARK 465 LEU D -9
REMARK 465 GLY D -8
REMARK 465 THR D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
REMARK 465 LYS D 260
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 GLU A 44 -175.52 53.50
REMARK 500 SER A 114 -127.14 62.03
REMARK 500 ALA A 140 47.72 -88.85
REMARK 500 GLN A 236 41.28 -105.86
REMARK 500 GLU B 44 -175.49 54.24
REMARK 500 SER B 114 -126.63 62.53
REMARK 500 GLN B 236 42.18 -107.47
REMARK 500 GLU C 44 -176.67 56.63
REMARK 500 SER C 114 -127.71 63.20
REMARK 500 ALA C 140 48.56 -87.59
REMARK 500 GLU D 44 -172.77 54.70
REMARK 500 SER D 114 -126.10 62.63
REMARK 500 ALA D 140 49.99 -84.63
REMARK 500 GLN D 236 41.66 -105.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 518 DISTANCE = 6.09 ANGSTROMS
DBREF 7Z2X A 1 260 UNP D7RU28 D7RU28_LENBU 1 260
DBREF 7Z2X B 1 260 UNP D7RU28 D7RU28_LENBU 1 260
DBREF 7Z2X C 1 260 UNP D7RU28 D7RU28_LENBU 1 260
DBREF 7Z2X D 1 260 UNP D7RU28 D7RU28_LENBU 1 260
SEQADV 7Z2X MET A -21 UNP D7RU28 INITIATING METHIONINE
SEQADV 7Z2X HIS A -20 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS A -19 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS A -18 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS A -17 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS A -16 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS A -15 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER A -14 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER A -13 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY A -12 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X VAL A -11 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASP A -10 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU A -9 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY A -8 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X THR A -7 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLU A -6 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASN A -5 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU A -4 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X TYR A -3 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X PHE A -2 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLN A -1 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER A 0 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X MET B -21 UNP D7RU28 INITIATING METHIONINE
SEQADV 7Z2X HIS B -20 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS B -19 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS B -18 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS B -17 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS B -16 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS B -15 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER B -14 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER B -13 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY B -12 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X VAL B -11 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASP B -10 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU B -9 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY B -8 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X THR B -7 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLU B -6 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASN B -5 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU B -4 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X TYR B -3 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X PHE B -2 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLN B -1 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER B 0 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X MET C -21 UNP D7RU28 INITIATING METHIONINE
SEQADV 7Z2X HIS C -20 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS C -19 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS C -18 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS C -17 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS C -16 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS C -15 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER C -14 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER C -13 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY C -12 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X VAL C -11 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASP C -10 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU C -9 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY C -8 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X THR C -7 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLU C -6 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASN C -5 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU C -4 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X TYR C -3 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X PHE C -2 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLN C -1 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER C 0 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X MET D -21 UNP D7RU28 INITIATING METHIONINE
SEQADV 7Z2X HIS D -20 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS D -19 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS D -18 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS D -17 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS D -16 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X HIS D -15 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER D -14 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER D -13 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY D -12 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X VAL D -11 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASP D -10 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU D -9 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLY D -8 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X THR D -7 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLU D -6 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X ASN D -5 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X LEU D -4 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X TYR D -3 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X PHE D -2 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X GLN D -1 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2X SER D 0 UNP D7RU28 EXPRESSION TAG
SEQRES 1 A 282 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 282 GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES 3 A 282 VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES 4 A 282 ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES 5 A 282 THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES 6 A 282 GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES 7 A 282 MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES 8 A 282 CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES 9 A 282 PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES 10 A 282 ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES 11 A 282 SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES 12 A 282 ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES 13 A 282 CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES 14 A 282 LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES 15 A 282 VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES 16 A 282 LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES 17 A 282 ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES 18 A 282 ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES 19 A 282 SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES 20 A 282 VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES 21 A 282 PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES 22 A 282 PHE ARG LYS THR LEU LEU GLU ALA LYS
SEQRES 1 B 282 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 282 GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES 3 B 282 VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES 4 B 282 ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES 5 B 282 THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES 6 B 282 GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES 7 B 282 MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES 8 B 282 CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES 9 B 282 PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES 10 B 282 ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES 11 B 282 SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES 12 B 282 ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES 13 B 282 CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES 14 B 282 LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES 15 B 282 VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES 16 B 282 LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES 17 B 282 ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES 18 B 282 ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES 19 B 282 SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES 20 B 282 VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES 21 B 282 PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES 22 B 282 PHE ARG LYS THR LEU LEU GLU ALA LYS
SEQRES 1 C 282 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 282 GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES 3 C 282 VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES 4 C 282 ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES 5 C 282 THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES 6 C 282 GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES 7 C 282 MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES 8 C 282 CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES 9 C 282 PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES 10 C 282 ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES 11 C 282 SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES 12 C 282 ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES 13 C 282 CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES 14 C 282 LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES 15 C 282 VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES 16 C 282 LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES 17 C 282 ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES 18 C 282 ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES 19 C 282 SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES 20 C 282 VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES 21 C 282 PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES 22 C 282 PHE ARG LYS THR LEU LEU GLU ALA LYS
SEQRES 1 D 282 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 282 GLY THR GLU ASN LEU TYR PHE GLN SER MET ILE LYS PHE
SEQRES 3 D 282 VAL THR THR GLU ILE ASN GLY LEU THR LEU ARG GLY THR
SEQRES 4 D 282 ALA HIS VAL PRO ASP GLY GLU PRO GLY GLN GLN PHE PRO
SEQRES 5 D 282 THR VAL LEU MET PHE HIS GLY PHE GLY ALA VAL ARG ASP
SEQRES 6 D 282 GLU GLY PHE ARG LEU PHE ILE GLN MET SER ASN ARG LEU
SEQRES 7 D 282 MET GLU ASN GLY ILE ALA ALA VAL ARG PHE ASP PHE GLY
SEQRES 8 D 282 CYS HIS GLY GLU SER ASP GLY GLU PHE GLU ASP PHE THR
SEQRES 9 D 282 PHE SER GLN GLU LEU ASN GLU GLY SER ALA LEU ILE ASP
SEQRES 10 D 282 ALA VAL LYS SER MET SER PHE VAL ASP SER THR LYS PHE
SEQRES 11 D 282 SER LEU LEU GLY GLU SER LEU GLY SER VAL ALA ALA SER
SEQRES 12 D 282 ILE VAL ALA GLY LYS ARG SER THR GLU LEU THR SER LEU
SEQRES 13 D 282 CYS MET TRP SER PRO ALA ALA SER PHE LEU ASP GLU ILE
SEQRES 14 D 282 LEU ASN ASP HIS THR LEU GLN GLY LYS THR VAL ASP ASN
SEQRES 15 D 282 VAL GLU LYS ASP GLY TYR PHE ASP PHE TYR GLY LEU LYS
SEQRES 16 D 282 LEU GLY LYS ALA PHE PHE ASP ASP LEU LYS ASN ILE ASN
SEQRES 17 D 282 ILE PHE ASP ASN ALA LYS LYS TYR GLN GLY PRO VAL LYS
SEQRES 18 D 282 ILE VAL TYR GLY THR ASN ASP PHE ILE PRO GLU LYS TYR
SEQRES 19 D 282 SER HIS LYS TYR MET ASP GLY TYR GLU ASN GLY GLU LEU
SEQRES 20 D 282 VAL ILE VAL GLN ASP GLY ASP HIS GLY TRP GLN SER VAL
SEQRES 21 D 282 PRO SER ARG LYS ARG ILE LEU ASP GLU THR MET LYS PHE
SEQRES 22 D 282 PHE ARG LYS THR LEU LEU GLU ALA LYS
FORMUL 5 HOH *879(H2 O)
HELIX 1 AA1 GLU A 44 PHE A 46 5 3
HELIX 2 AA2 ARG A 47 ASN A 59 1 13
HELIX 3 AA3 GLU A 77 PHE A 81 5 5
HELIX 4 AA4 THR A 82 SER A 99 1 18
HELIX 5 AA5 LEU A 115 ARG A 127 1 13
HELIX 6 AA6 SER A 128 LEU A 131 5 4
HELIX 7 AA7 SER A 142 ASN A 149 1 8
HELIX 8 AA8 ASN A 160 GLY A 165 1 6
HELIX 9 AA9 GLY A 175 LEU A 182 1 8
HELIX 10 AB1 LYS A 183 ILE A 185 5 3
HELIX 11 AB2 ASN A 186 LYS A 192 1 7
HELIX 12 AB3 GLU A 210 TYR A 220 1 11
HELIX 13 AB4 SER A 237 LEU A 257 1 21
HELIX 14 AB5 GLU B 44 PHE B 46 5 3
HELIX 15 AB6 ARG B 47 ASN B 59 1 13
HELIX 16 AB7 GLU B 77 PHE B 81 5 5
HELIX 17 AB8 THR B 82 SER B 99 1 18
HELIX 18 AB9 SER B 114 ARG B 127 1 14
HELIX 19 AC1 SER B 128 LEU B 131 5 4
HELIX 20 AC2 SER B 142 ASN B 149 1 8
HELIX 21 AC3 ASN B 160 GLY B 165 1 6
HELIX 22 AC4 GLY B 175 LEU B 182 1 8
HELIX 23 AC5 LYS B 183 ILE B 185 5 3
HELIX 24 AC6 ILE B 187 LYS B 192 1 6
HELIX 25 AC7 GLU B 210 TYR B 220 1 11
HELIX 26 AC8 SER B 237 LEU B 257 1 21
HELIX 27 AC9 GLU C 44 PHE C 46 5 3
HELIX 28 AD1 ARG C 47 ASN C 59 1 13
HELIX 29 AD2 GLU C 77 PHE C 81 5 5
HELIX 30 AD3 THR C 82 SER C 99 1 18
HELIX 31 AD4 LEU C 115 ARG C 127 1 13
HELIX 32 AD5 SER C 128 LEU C 131 5 4
HELIX 33 AD6 SER C 142 HIS C 151 1 10
HELIX 34 AD7 ASN C 160 GLY C 165 1 6
HELIX 35 AD8 GLY C 175 LEU C 182 1 8
HELIX 36 AD9 LYS C 183 ILE C 185 5 3
HELIX 37 AE1 ILE C 187 LYS C 192 1 6
HELIX 38 AE2 GLU C 210 TYR C 220 1 11
HELIX 39 AE3 SER C 237 LEU C 257 1 21
HELIX 40 AE4 GLU D 44 PHE D 46 5 3
HELIX 41 AE5 ARG D 47 ASN D 59 1 13
HELIX 42 AE6 GLU D 77 PHE D 81 5 5
HELIX 43 AE7 THR D 82 SER D 99 1 18
HELIX 44 AE8 SER D 114 ARG D 127 1 14
HELIX 45 AE9 SER D 128 LEU D 131 5 4
HELIX 46 AF1 SER D 142 ASN D 149 1 8
HELIX 47 AF2 ASN D 160 GLY D 165 1 6
HELIX 48 AF3 GLY D 175 LEU D 182 1 8
HELIX 49 AF4 LYS D 183 ILE D 185 5 3
HELIX 50 AF5 ILE D 187 LYS D 192 1 6
HELIX 51 AF6 GLU D 210 TYR D 220 1 11
HELIX 52 AF7 SER D 237 LEU D 257 1 21
SHEET 1 AA1 8 MET A 1 ILE A 9 0
SHEET 2 AA1 8 LEU A 12 VAL A 20 -1 O ALA A 18 N LYS A 3
SHEET 3 AA1 8 ALA A 62 PHE A 66 -1 O ALA A 63 N HIS A 19
SHEET 4 AA1 8 PHE A 29 PHE A 35 1 N PRO A 30 O ALA A 62
SHEET 5 AA1 8 VAL A 103 GLU A 113 1 O LEU A 111 N PHE A 35
SHEET 6 AA1 8 SER A 133 TRP A 137 1 O TRP A 137 N GLY A 112
SHEET 7 AA1 8 VAL A 198 GLY A 203 1 O LYS A 199 N MET A 136
SHEET 8 AA1 8 GLY A 223 VAL A 228 1 O VAL A 226 N ILE A 200
SHEET 1 AA2 2 THR A 152 LEU A 153 0
SHEET 2 AA2 2 LYS A 156 THR A 157 -1 O LYS A 156 N LEU A 153
SHEET 1 AA3 2 PHE A 167 PHE A 169 0
SHEET 2 AA3 2 LEU A 172 LEU A 174 -1 O LEU A 174 N PHE A 167
SHEET 1 AA4 8 MET B 1 ILE B 9 0
SHEET 2 AA4 8 LEU B 12 VAL B 20 -1 O ALA B 18 N LYS B 3
SHEET 3 AA4 8 ALA B 62 PHE B 66 -1 O ALA B 63 N HIS B 19
SHEET 4 AA4 8 PHE B 29 PHE B 35 1 N PRO B 30 O ALA B 62
SHEET 5 AA4 8 VAL B 103 GLU B 113 1 O LEU B 111 N PHE B 35
SHEET 6 AA4 8 SER B 133 TRP B 137 1 O CYS B 135 N LEU B 110
SHEET 7 AA4 8 VAL B 198 GLY B 203 1 O LYS B 199 N MET B 136
SHEET 8 AA4 8 GLY B 223 VAL B 228 1 O VAL B 226 N ILE B 200
SHEET 1 AA5 2 THR B 152 LEU B 153 0
SHEET 2 AA5 2 LYS B 156 THR B 157 -1 O LYS B 156 N LEU B 153
SHEET 1 AA6 2 PHE B 167 PHE B 169 0
SHEET 2 AA6 2 LEU B 172 LEU B 174 -1 O LEU B 174 N PHE B 167
SHEET 1 AA7 8 MET C 1 ILE C 9 0
SHEET 2 AA7 8 LEU C 12 VAL C 20 -1 O ALA C 18 N LYS C 3
SHEET 3 AA7 8 ALA C 62 PHE C 66 -1 O ALA C 63 N HIS C 19
SHEET 4 AA7 8 PHE C 29 PHE C 35 1 N PRO C 30 O ALA C 62
SHEET 5 AA7 8 VAL C 103 GLU C 113 1 O LEU C 111 N PHE C 35
SHEET 6 AA7 8 SER C 133 TRP C 137 1 O TRP C 137 N GLY C 112
SHEET 7 AA7 8 VAL C 198 GLY C 203 1 O LYS C 199 N MET C 136
SHEET 8 AA7 8 GLY C 223 VAL C 228 1 O VAL C 226 N ILE C 200
SHEET 1 AA8 2 THR C 152 LEU C 153 0
SHEET 2 AA8 2 LYS C 156 THR C 157 -1 O LYS C 156 N LEU C 153
SHEET 1 AA9 2 PHE C 167 PHE C 169 0
SHEET 2 AA9 2 LEU C 172 LEU C 174 -1 O LEU C 174 N PHE C 167
SHEET 1 AB1 8 MET D 1 ILE D 9 0
SHEET 2 AB1 8 LEU D 12 VAL D 20 -1 O LEU D 14 N THR D 7
SHEET 3 AB1 8 ALA D 62 PHE D 66 -1 O ALA D 63 N HIS D 19
SHEET 4 AB1 8 PHE D 29 PHE D 35 1 N PRO D 30 O ALA D 62
SHEET 5 AB1 8 VAL D 103 GLU D 113 1 O SER D 109 N LEU D 33
SHEET 6 AB1 8 LEU D 134 TRP D 137 1 O CYS D 135 N LEU D 110
SHEET 7 AB1 8 VAL D 198 GLY D 203 1 O LYS D 199 N MET D 136
SHEET 8 AB1 8 GLY D 223 VAL D 228 1 O VAL D 226 N ILE D 200
SHEET 1 AB2 2 THR D 152 LEU D 153 0
SHEET 2 AB2 2 LYS D 156 THR D 157 -1 O LYS D 156 N LEU D 153
SHEET 1 AB3 2 PHE D 167 PHE D 169 0
SHEET 2 AB3 2 LEU D 172 LEU D 174 -1 O LEU D 172 N PHE D 169
CRYST1 47.830 62.230 94.850 103.05 101.52 92.80 P 1 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 0.020907 0.001023 0.004645 0.00000
SCALE2 0.000000 0.016089 0.003991 0.00000
SCALE3 0.000000 0.000000 0.011086 0.00000
TER 2121 ALA A 259
TER 4203 ALA B 259
TER 6315 ALA C 259
TER 8388 ALA D 259
MASTER 324 0 0 52 48 0 0 6 9163 4 0 88
END |