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HEADER HYDROLASE 28-FEB-22 7Z2V
TITLE FERULIC ACID ESTERASE VARIANT S114A FROM LACTOBACILLUS BUCHNERI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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, MUTANT S114, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.K.MOGODINIYAI,T.REICHENBACH,D.C.KALYANI,M.M.KESKITALO,C.DIVNE
REVDAT 1 30-NOV-22 7Z2V 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 FERULIC ACID ESTERASE VARIANT S114A FROM LACTOBACILLUS
JRNL TITL 2 BUCHNERI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 130607
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.530
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 40.1400 - 3.4900 1.00 9851 154 0.1418 0.1513
REMARK 3 2 3.4900 - 2.7700 1.00 9439 146 0.1619 0.1626
REMARK 3 3 2.7700 - 2.4200 1.00 9312 145 0.1664 0.1681
REMARK 3 4 2.4200 - 2.2000 1.00 9286 144 0.1668 0.1762
REMARK 3 5 2.2000 - 2.0400 1.00 9229 143 0.1610 0.1968
REMARK 3 6 2.0400 - 1.9200 1.00 9208 144 0.1645 0.1802
REMARK 3 7 1.9200 - 1.8300 1.00 9157 142 0.1744 0.1902
REMARK 3 8 1.8300 - 1.7500 1.00 9177 143 0.1765 0.1779
REMARK 3 9 1.7500 - 1.6800 1.00 9142 142 0.1752 0.1957
REMARK 3 10 1.6800 - 1.6200 1.00 9122 142 0.1891 0.2068
REMARK 3 11 1.6200 - 1.5700 1.00 9067 141 0.2144 0.2341
REMARK 3 12 1.5700 - 1.5300 1.00 9129 142 0.2527 0.2836
REMARK 3 13 1.5300 - 1.4900 0.99 8973 139 0.2925 0.2968
REMARK 3 14 1.4900 - 1.4500 0.94 8515 133 0.3385 0.3354
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.15
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7Z2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1292121410.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-20
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97629
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 130627
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 46.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 22.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : 1.200
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 (%): 60.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M
REMARK 280 CALCIUM ACETATE, 18% PEG8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 113.97000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 39.98000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 39.98000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 170.95500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 39.98000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 39.98000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 56.98500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 39.98000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.98000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 170.95500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 39.98000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.98000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.98500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 113.97000
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: 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 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 ASN A -5
REMARK 465 LEU A -4
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 ALA B 259
REMARK 465 LYS B 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 -175.31 54.86
REMARK 500 ALA A 114 -123.57 61.55
REMARK 500 ARG A 127 57.63 -118.24
REMARK 500 ALA A 140 49.72 -89.94
REMARK 500 GLN A 236 40.05 -107.58
REMARK 500 GLU B 44 -175.11 55.96
REMARK 500 ALA B 114 -126.33 63.07
REMARK 500 ALA B 140 46.99 -89.28
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 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A -1 OE1
REMARK 620 2 ASP A 22 OD1 71.6
REMARK 620 3 ASP A 22 OD2 90.2 49.0
REMARK 620 4 HOH A 406 O 63.4 63.7 112.6
REMARK 620 5 HOH A 590 O 146.4 78.5 81.2 90.1
REMARK 620 N 1 2 3 4
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 THR A 13 OG1
REMARK 620 2 ASP A 75 OD2 76.6
REMARK 620 3 HOH A 462 O 73.6 86.3
REMARK 620 4 HOH A 483 O 106.9 76.8 162.3
REMARK 620 5 HOH A 514 O 72.2 140.2 61.8 135.8
REMARK 620 6 HOH A 579 O 73.9 131.1 120.5 75.6 61.4
REMARK 620 7 HOH A 601 O 147.8 77.8 85.6 85.6 119.2 138.3
REMARK 620 8 HOH A 691 O 142.0 141.4 103.0 87.4 73.2 76.1 66.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 218 O
REMARK 620 2 HOH A 418 O 33.5
REMARK 620 3 HOH A 609 O 37.2 4.2
REMARK 620 4 HOH A 611 O 33.4 3.0 4.0
REMARK 620 5 GLU B 8 O 34.3 2.8 3.1 0.9
REMARK 620 6 HOH B 535 O 36.2 4.7 2.4 2.9 2.2
REMARK 620 7 HOH B 603 O 36.4 2.9 1.8 4.1 3.3 3.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B -1 OE1
REMARK 620 2 ASP B 22 OD1 74.0
REMARK 620 3 ASP B 22 OD2 82.9 50.9
REMARK 620 4 HOH B 553 O 77.6 75.6 126.2
REMARK 620 5 HOH B 615 O 148.7 76.1 85.5 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 13 OG1
REMARK 620 2 ASP B 75 OD2 77.5
REMARK 620 3 HOH B 482 O 108.6 77.4
REMARK 620 4 HOH B 516 O 71.4 87.6 164.4
REMARK 620 5 HOH B 557 O 74.0 129.7 73.7 120.0
REMARK 620 6 HOH B 569 O 147.1 78.4 87.4 85.6 138.8
REMARK 620 7 HOH B 610 O 81.9 151.7 128.2 67.3 60.5 111.1
REMARK 620 8 HOH B 658 O 140.4 142.1 85.4 104.5 75.0 67.2 61.4
REMARK 620 N 1 2 3 4 5 6 7
DBREF 7Z2V A 1 260 UNP D7RU28 D7RU28_LENBU 1 260
DBREF 7Z2V B 1 260 UNP D7RU28 D7RU28_LENBU 1 260
SEQADV 7Z2V MET A -21 UNP D7RU28 INITIATING METHIONINE
SEQADV 7Z2V HIS A -20 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS A -19 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS A -18 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS A -17 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS A -16 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS A -15 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V SER A -14 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V SER A -13 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLY A -12 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V VAL A -11 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V ASP A -10 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V LEU A -9 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLY A -8 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V THR A -7 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLU A -6 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V ASN A -5 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V LEU A -4 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V TYR A -3 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V PHE A -2 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLN A -1 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V SER A 0 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V ALA A 114 UNP D7RU28 SER 114 ENGINEERED MUTATION
SEQADV 7Z2V MET B -21 UNP D7RU28 INITIATING METHIONINE
SEQADV 7Z2V HIS B -20 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS B -19 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS B -18 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS B -17 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS B -16 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V HIS B -15 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V SER B -14 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V SER B -13 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLY B -12 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V VAL B -11 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V ASP B -10 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V LEU B -9 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLY B -8 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V THR B -7 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLU B -6 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V ASN B -5 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V LEU B -4 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V TYR B -3 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V PHE B -2 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V GLN B -1 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V SER B 0 UNP D7RU28 EXPRESSION TAG
SEQADV 7Z2V ALA B 114 UNP D7RU28 SER 114 ENGINEERED MUTATION
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 ALA 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 ALA 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
HET CA A 301 1
HET CA A 302 1
HET ACT A 303 4
HET CA B 301 1
HET CA B 302 1
HET ACT B 303 4
HET ACT B 304 4
HET CA B 305 1
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
FORMUL 3 CA 5(CA 2+)
FORMUL 5 ACT 3(C2 H3 O2 1-)
FORMUL 11 HOH *575(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 ALA A 114 ARG A 127 1 14
HELIX 6 AA6 SER A 142 ASP A 150 1 9
HELIX 7 AA7 ASN A 160 GLY A 165 1 6
HELIX 8 AA8 LYS A 176 LEU A 182 1 7
HELIX 9 AA9 LYS A 183 ILE A 185 5 3
HELIX 10 AB1 ILE A 187 LYS A 192 1 6
HELIX 11 AB2 GLU A 210 TYR A 220 1 11
HELIX 12 AB3 SER A 237 LEU A 257 1 21
HELIX 13 AB4 GLU B 44 PHE B 46 5 3
HELIX 14 AB5 ARG B 47 ASN B 59 1 13
HELIX 15 AB6 GLU B 77 PHE B 81 5 5
HELIX 16 AB7 THR B 82 SER B 99 1 18
HELIX 17 AB8 ALA B 114 ARG B 127 1 14
HELIX 18 AB9 SER B 128 LEU B 131 5 4
HELIX 19 AC1 SER B 142 HIS B 151 1 10
HELIX 20 AC2 ASN B 160 GLY B 165 1 6
HELIX 21 AC3 GLY B 175 LEU B 182 1 8
HELIX 22 AC4 LYS B 183 ILE B 185 5 3
HELIX 23 AC5 ILE B 187 LYS B 192 1 6
HELIX 24 AC6 GLU B 210 TYR B 220 1 11
HELIX 25 AC7 SER B 237 LEU B 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 MET A 34 O VAL A 64
SHEET 5 AA1 8 VAL A 103 GLU A 113 1 O ASP A 104 N PHE A 29
SHEET 6 AA1 8 LEU A 134 TRP A 137 1 O CYS A 135 N LEU A 110
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 TYR A 166 PHE A 169 0
SHEET 2 AA3 2 LEU A 172 GLY A 175 -1 O LEU A 172 N PHE A 169
SHEET 1 AA4 8 MET B 1 ILE B 9 0
SHEET 2 AA4 8 LEU B 12 VAL B 20 -1 O VAL B 20 N MET B 1
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 VAL B 32 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 LEU B 134 TRP B 137 1 O TRP B 137 N GLY B 112
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 228 N TYR B 202
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
LINK OE1 GLN A -1 CA CA A 302 1555 1555 2.55
LINK OG1 THR A 13 CA CA A 301 1555 1555 2.46
LINK OD1 ASP A 22 CA CA A 302 1555 1555 2.88
LINK OD2 ASP A 22 CA CA A 302 1555 1555 2.21
LINK OD2 ASP A 75 CA CA A 301 1555 1555 2.39
LINK O ASP A 218 CA CA B 305 1555 3554 2.37
LINK CA CA A 301 O HOH A 462 1555 1555 2.47
LINK CA CA A 301 O HOH A 483 1555 1555 2.41
LINK CA CA A 301 O HOH A 514 1555 1555 2.26
LINK CA CA A 301 O HOH A 579 1555 1555 2.40
LINK CA CA A 301 O HOH A 601 1555 1555 2.36
LINK CA CA A 301 O HOH A 691 1555 1555 2.31
LINK CA CA A 302 O HOH A 406 1555 1555 2.17
LINK CA CA A 302 O HOH A 590 1555 1555 2.32
LINK O HOH A 418 CA CA B 305 4455 1555 2.42
LINK O HOH A 609 CA CA B 305 4455 1555 2.48
LINK O HOH A 611 CA CA B 305 4455 1555 2.20
LINK OE1 GLN B -1 CA CA B 302 1555 1555 2.45
LINK O GLU B 8 CA CA B 305 1555 1555 2.30
LINK OG1 THR B 13 CA CA B 301 1555 1555 2.50
LINK OD1 ASP B 22 CA CA B 302 1555 1555 2.75
LINK OD2 ASP B 22 CA CA B 302 1555 1555 2.24
LINK OD2 ASP B 75 CA CA B 301 1555 1555 2.38
LINK CA CA B 301 O HOH B 482 1555 1555 2.44
LINK CA CA B 301 O HOH B 516 1555 1555 2.38
LINK CA CA B 301 O HOH B 557 1555 1555 2.31
LINK CA CA B 301 O HOH B 569 1555 1555 2.29
LINK CA CA B 301 O HOH B 610 1555 1555 2.32
LINK CA CA B 301 O HOH B 658 1555 1555 2.31
LINK CA CA B 302 O HOH B 553 1555 1555 2.14
LINK CA CA B 302 O HOH B 615 1555 1555 2.43
LINK CA CA B 305 O HOH B 535 1555 1555 2.37
LINK CA CA B 305 O HOH B 603 1555 1555 2.58
CRYST1 79.960 79.960 227.940 90.00 90.00 90.00 P 43 21 2 16
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 0.012506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012506 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004387 0.00000
TER 2103 ALA A 259
TER 4212 GLU B 258
MASTER 350 0 8 25 24 0 0 6 4743 2 50 44
END |