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HEADER HYDROLASE 04-FEB-15 5AH1
TITLE STRUCTURE OF ESTA FROM CLOSTRIDIUM BOTULINUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 30-480;
COMPND 5 SYNONYM: ESTERASE A;
COMPND 6 EC: 3.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM;
SOURCE 3 ORGANISM_TAXID: 1491;
SOURCE 4 ATCC: 3502;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET26B(PLUS)
KEYWDS HYDROLASE, POLYESTERASE, POLYMER HYDROLYSIS, ZINC BINDING,
KEYWDS 2 ALPHA/BETA- HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAIRITSCH,A.LYSKOWSKI,A.HROMIC,G.STEINKELLNER,K.GRUBER,V.PERZ,
AUTHOR 2 A.BAUMSCHLAGER,K.BLEYMAIER,S.ZITZENBACHER,C.SINKEL,U.KUEPER,
AUTHOR 3 D.RIBITSCH,G.M.GUEBITZ
REVDAT 1 11-NOV-15 5AH1 0
JRNL AUTH V.PERZ,A.BAUMSCHLAGER,K.BLEYMAIER,S.ZITZENBACHER,A.HROMIC,
JRNL AUTH 2 G.STEINKELLNER,A.PAIRITSCH,A.LYSKOWSKI,K.GRUBER,C.SINKEL,
JRNL AUTH 3 U.KUEPER,D.RIBITSCH,G.M.GUEBITZ
JRNL TITL HYDROLYSIS OF SYNTHETIC POLYESTERS BY CLOSTRIDIUM BOTULINUM
JRNL TITL 2 ESTERASES.
JRNL REF BIOTECHNOL.BIOENG. 2015
JRNL REFN ESSN 1097-0290
JRNL PMID 26524601
JRNL DOI 10.1002/BIT.25874
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.954
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.00
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.75
REMARK 3 NUMBER OF REFLECTIONS : 113119
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1296
REMARK 3 R VALUE (WORKING SET) : 0.1293
REMARK 3 FREE R VALUE : 0.1493
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.7
REMARK 3 FREE R VALUE TEST SET COUNT : 1876
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 34.9694 - 2.8164 0.99 10470 175 0.1289 0.1423
REMARK 3 2 2.8164 - 2.2356 0.99 10234 169 0.1258 0.1307
REMARK 3 3 2.2356 - 1.9530 0.97 10063 168 0.1198 0.1397
REMARK 3 4 1.9530 - 1.7744 0.95 9814 171 0.1256 0.1522
REMARK 3 5 1.7744 - 1.6473 0.94 9699 166 0.1261 0.1369
REMARK 3 6 1.6473 - 1.5501 0.92 9534 154 0.1175 0.1500
REMARK 3 7 1.5501 - 1.4725 0.90 9246 163 0.1227 0.1613
REMARK 3 8 1.4725 - 1.4084 0.89 9210 145 0.1306 0.1607
REMARK 3 9 1.4084 - 1.3542 0.87 8896 164 0.1381 0.1942
REMARK 3 10 1.3542 - 1.3075 0.83 8519 136 0.1489 0.1869
REMARK 3 11 1.3075 - 1.2666 0.66 6761 133 0.1636 0.1927
REMARK 3 12 1.2666 - 1.2304 0.49 5043 72 0.1669 0.2357
REMARK 3 13 1.2304 - 1.1980 0.36 3754 60 0.1956 0.1770
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) : 0.09
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.85
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.2
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 3685
REMARK 3 ANGLE : 1.182 5041
REMARK 3 CHIRALITY : 0.070 537
REMARK 3 PLANARITY : 0.007 670
REMARK 3 DIHEDRAL : 13.093 1373
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: ANISOTROPIC ATOMIC DISPLACEMENT
REMARK 3 PARAMETERS WERE REFINED FOR ALL NON-H ATOMS EXCEPT FOR THE SOLVENT
REMARK 4
REMARK 4 5AH1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-15.
REMARK 100 THE PDBE ID CODE IS EBI-62956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-13
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 : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9777
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121016
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.20
REMARK 200 RESOLUTION RANGE LOW (A) : 49.02
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.6
REMARK 200 DATA REDUNDANCY : 4.9
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 50.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.8
REMARK 200 R MERGE FOR SHELL (I) : 0.41
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.80
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: PDB ENTRY 1KU0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 8.5 AND 2 M AMMONIUM
REMARK 280 SULFATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.35500
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 GLU A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 GLN A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 GLN A 10
REMARK 465 LYS A 11
REMARK 465 VAL A 12
REMARK 465 GLU A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 THR A 16
REMARK 465 THR A 17
REMARK 465 LYS A 18
REMARK 465 LYS A 19
REMARK 465 GLU A 20
REMARK 465 VAL A 21
REMARK 465 LYS A 22
REMARK 465 ASP A 23
REMARK 465 ALA A 24
REMARK 465 GLU A 25
REMARK 465 GLU A 26
REMARK 465 THR A 27
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 465 HIS A 461
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 GLU A 455 CA C O CB CG CD OE1 OE2
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 OE2 GLU A 201 O HOH A 2349 2.20
REMARK 500 O HOH A 2033 O HOH A 2089 2.19
REMARK 500 O HOH A 2043 O HOH A 2601 2.14
REMARK 500 O HOH A 2051 O HOH A 2141 2.11
REMARK 500 O HOH A 2052 O HOH A 2142 2.08
REMARK 500 O HOH A 2119 O HOH A 2262 2.16
REMARK 500 O HOH A 2202 O HOH A 2203 2.16
REMARK 500 O HOH A 2299 O HOH A 2550 2.13
REMARK 500 O HOH A 2354 O HOH A 2371 2.09
REMARK 500 O HOH A 2472 O HOH A 2474 2.13
REMARK 500 O HOH A 2560 O HOH A 2561 2.18
REMARK 500 O HOH A 2594 O HOH A 2595 2.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2107 O HOH A 2472 2555 2.16
REMARK 500 O HOH A 2185 O HOH A 2470 2555 2.20
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 THR A 32 -169.74 -122.49
REMARK 500 SER A 182 -139.31 59.84
REMARK 500 LEU A 271 33.72 -96.64
REMARK 500 ALA A 335 22.80 -143.96
REMARK 500 ASP A 377 -169.36 -126.09
REMARK 500 VAL A 386 -39.20 -132.27
REMARK 500 LYS A 396 -42.89 -130.32
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 K A1456 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 425 OD2
REMARK 620 2 HOH A2010 O 84.7
REMARK 620 3 ASP A 428 OD2 81.8 131.3
REMARK 620 4 PRO A 351 O 85.0 144.0 80.8
REMARK 620 5 HOH A2012 O 115.8 76.4 150.2 77.4
REMARK 620 6 ASP A 428 OD1 84.9 80.6 51.8 132.5 147.0
REMARK 620 7 HOH A2582 O 153.9 85.5 86.7 116.3 85.1 69.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1457 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 67 O
REMARK 620 2 VAL A 67 O 2.8
REMARK 620 3 ARG A 70 O 74.6 76.9
REMARK 620 4 HOH A2087 O 61.1 61.0 56.4
REMARK 620 5 SER A 237 O 141.4 139.6 141.2 141.9
REMARK 620 6 ASP A 238 O 85.6 86.6 102.9 143.6 73.8
REMARK 620 7 HOH A2090 O 152.7 155.2 78.4 105.9 64.1 97.2
REMARK 620 8 MET A 240 O 85.9 83.1 143.3 87.0 69.7 106.2 118.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1455 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 302 OD2
REMARK 620 2 HIS A 150 NE2 104.5
REMARK 620 3 HIS A 156 NE2 96.5 104.6
REMARK 620 4 ASP A 130 OD1 131.8 97.9 118.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1457
DBREF 5AH1 A 2 452 UNP A7FSB2 A7FSB2_CLOB1 30 480
SEQADV 5AH1 MET A 1 UNP A7FSB2 CLONING ARTIFACT
SEQADV 5AH1 ALA A 453 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 LEU A 454 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 GLU A 455 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 HIS A 456 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 HIS A 457 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 HIS A 458 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 HIS A 459 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 HIS A 460 UNP A7FSB2 EXPRESSION TAG
SEQADV 5AH1 HIS A 461 UNP A7FSB2 EXPRESSION TAG
SEQRES 1 A 461 MET ALA GLU PRO LYS ALA GLN GLY THR GLN LYS VAL GLU
SEQRES 2 A 461 SER SER THR THR LYS LYS GLU VAL LYS ASP ALA GLU GLU
SEQRES 3 A 461 THR ILE LYS ILE PRO THR LEU GLU ASP ILE ASP ASN LEU
SEQRES 4 A 461 ILE ASP SER ALA GLU GLU VAL LYS SER GLU GLU ASP ILE
SEQRES 5 A 461 ASN LYS MET PRO PRO LEU LYS PHE PRO VAL GLU PHE PRO
SEQRES 6 A 461 GLU VAL ASN THR ARG SER ILE ILE GLY GLY ASN ASN TYR
SEQRES 7 A 461 PRO ILE VAL LEU VAL HIS GLY PHE MET GLY PHE GLY ARG
SEQRES 8 A 461 ASP GLU LEU LEU GLY TYR LYS TYR TRP GLY GLY VAL VAL
SEQRES 9 A 461 ASP LEU GLN GLU LYS LEU ASN ALA SER GLY HIS GLU THR
SEQRES 10 A 461 TYR THR ALA THR VAL GLY PRO VAL SER SER ASN TRP ASP
SEQRES 11 A 461 ARG ALA CYS GLU LEU TYR ALA TYR ILE VAL GLY GLY THR
SEQRES 12 A 461 VAL ASP TYR GLY GLU ALA HIS ALA LYS LYS PHE LYS HIS
SEQRES 13 A 461 ASN ARG TYR GLY ARG THR TYR PRO GLY ILE TYR LYS ASN
SEQRES 14 A 461 ILE SER ASN GLU ASN LYS ILE HIS LEU ILE GLY HIS SER
SEQRES 15 A 461 MET GLY GLY GLN THR ILE ARG THR LEU THR GLN LEU LEU
SEQRES 16 A 461 SER GLU GLY SER GLU GLU GLU ILE ASN CYS GLY GLN GLU
SEQRES 17 A 461 ASN ILE SER PRO LEU PHE GLU GLY GLY LYS HIS TRP ILE
SEQRES 18 A 461 HIS SER VAL SER THR ILE SER THR PRO ASN ASP GLY THR
SEQRES 19 A 461 THR LEU SER ASP LEU MET PRO ALA LYS ASP LEU ILE SER
SEQRES 20 A 461 TYR THR PHE GLY VAL LEU GLY THR ILE THR GLY LYS ASN
SEQRES 21 A 461 LYS LEU PHE SER SER ILE TYR ASP LEU LYS LEU ASP GLN
SEQRES 22 A 461 TRP GLY LEU LYS LYS GLN ASN GLY GLU SER GLN ARG ASP
SEQRES 23 A 461 TYR ILE GLU ARG VAL LEU ASP SER ASN ILE TRP ASN SER
SEQRES 24 A 461 THR LYS ASP ILE ALA THR TYR ASP LEU SER THR GLU GLY
SEQRES 25 A 461 ALA GLN GLU LEU ASN THR TRP VAL LYS ALA GLN PRO ASP
SEQRES 26 A 461 VAL TYR TYR PHE SER TRP THR THR GLN ALA THR LYS GLU
SEQRES 27 A 461 SER ILE LEU THR GLY HIS SER VAL ALA GLN ILE GLY PRO
SEQRES 28 A 461 MET ASN PRO ILE PHE TYR PRO THR ALA ASN LEU MET GLY
SEQRES 29 A 461 ARG TYR SER ARG ASN GLN LYS ASP LEU PRO ILE ILE ASP
SEQRES 30 A 461 LYS LYS TRP PHE PRO ASN ASP GLY VAL VAL ASN CYS ILE
SEQRES 31 A 461 SER GLN ASP GLY PRO LYS LEU GLY SER ASN ASP VAL ILE
SEQRES 32 A 461 GLU GLN TYR ASN GLY GLY VAL LYS ILE GLY GLN TRP ASN
SEQRES 33 A 461 ALA MET PRO ARG ILE ILE ASN THR ASP HIS MET ASP ILE
SEQRES 34 A 461 VAL GLY THR PHE GLY ASN VAL LYS ASP TRP TYR MET ASP
SEQRES 35 A 461 TYR ALA SER PHE LEU SER ASN LEU SER ARG ALA LEU GLU
SEQRES 36 A 461 HIS HIS HIS HIS HIS HIS
HET ZN A1455 1
HET K A1456 1
HET K A1457 1
HETNAM K POTASSIUM ION
HETNAM ZN ZINC ION
FORMUL 2 K 2(K 1+)
FORMUL 3 ZN ZN 2+
FORMUL 4 HOH *602(H2 O)
HELIX 1 1 THR A 32 GLU A 34 5 3
HELIX 2 2 ASP A 35 ALA A 43 1 9
HELIX 3 3 SER A 48 ASN A 53 1 6
HELIX 4 4 GLU A 93 TYR A 97 5 5
HELIX 5 5 ASP A 105 SER A 113 1 9
HELIX 6 6 SER A 127 GLY A 141 1 15
HELIX 7 7 GLY A 147 LYS A 155 1 9
HELIX 8 8 SER A 182 GLY A 198 1 17
HELIX 9 9 SER A 199 CYS A 205 1 7
HELIX 10 10 SER A 211 GLY A 216 5 6
HELIX 11 11 THR A 234 MET A 240 1 7
HELIX 12 12 PRO A 241 GLY A 258 1 18
HELIX 13 13 ASN A 260 SER A 264 5 5
HELIX 14 14 LEU A 271 GLY A 275 5 5
HELIX 15 15 SER A 283 ASP A 293 1 11
HELIX 16 16 ASN A 295 THR A 300 1 6
HELIX 17 17 ILE A 303 SER A 309 1 7
HELIX 18 18 SER A 309 THR A 318 1 10
HELIX 19 19 ASN A 353 ILE A 355 5 3
HELIX 20 20 PHE A 356 GLY A 364 1 9
HELIX 21 21 ASP A 377 PHE A 381 5 5
HELIX 22 22 CYS A 389 GLN A 392 5 4
HELIX 23 23 MET A 427 GLY A 431 5 5
HELIX 24 24 VAL A 436 ASN A 449 1 14
SHEET 1 AA 7 THR A 117 ALA A 120 0
SHEET 2 AA 7 ILE A 80 VAL A 83 1 O ILE A 80 N TYR A 118
SHEET 3 AA 7 ILE A 176 HIS A 181 1 O HIS A 177 N VAL A 81
SHEET 4 AA 7 ILE A 221 ILE A 227 1 N HIS A 222 O ILE A 176
SHEET 5 AA 7 TYR A 327 TRP A 331 1 O TYR A 327 N VAL A 224
SHEET 6 AA 7 TRP A 415 ALA A 417 1 O ASN A 416 N SER A 330
SHEET 7 AA 7 ILE A 403 GLN A 405 1 O GLU A 404 N ALA A 417
SHEET 1 AB 2 GLY A 142 ASP A 145 0
SHEET 2 AB 2 TYR A 159 TYR A 163 -1 N GLY A 160 O VAL A 144
SHEET 1 AC 2 THR A 336 GLU A 338 0
SHEET 2 AC 2 SER A 345 ALA A 347 -1 O VAL A 346 N LYS A 337
LINK ZN ZN A1455 OD2 ASP A 302 1555 1555 1.97
LINK ZN ZN A1455 OD1 ASP A 130 1555 1555 1.94
LINK ZN ZN A1455 NE2 HIS A 156 1555 1555 2.07
LINK ZN ZN A1455 NE2 HIS A 150 1555 1555 2.08
LINK K K A1456 O HOH A2012 1555 1555 2.44
LINK K K A1456 OD1 ASP A 428 1555 1555 2.57
LINK K K A1456 O HOH A2582 1555 1555 2.56
LINK K K A1456 O HOH A2010 1555 1555 2.44
LINK K K A1456 OD2 ASP A 428 1555 1555 2.47
LINK K K A1456 O PRO A 351 1555 1555 2.42
LINK K K A1456 OD2 ASP A 425 1555 1555 2.47
LINK K K A1457 O ASP A 238 1555 1555 2.69
LINK K K A1457 O HOH A2090 1555 1455 2.80
LINK K K A1457 O MET A 240 1555 1555 2.68
LINK K K A1457 O SER A 237 1555 1555 2.77
LINK K K A1457 O HOH A2087 1555 1455 2.95
LINK K K A1457 O ARG A 70 1555 1455 2.91
LINK K K A1457 O BVAL A 67 1555 1455 2.87
LINK K K A1457 O AVAL A 67 1555 1455 2.78
CISPEP 1 THR A 432 PHE A 433 0 7.01
SITE 1 AC1 4 ASP A 130 HIS A 150 HIS A 156 ASP A 302
SITE 1 AC2 7 PRO A 351 ASN A 353 ASP A 425 ASP A 428
SITE 2 AC2 7 HOH A2010 HOH A2012 HOH A2582
SITE 1 AC3 7 VAL A 67 ARG A 70 SER A 237 ASP A 238
SITE 2 AC3 7 MET A 240 HOH A2087 HOH A2090
CRYST1 51.240 64.710 69.790 90.00 106.93 90.00 P 1 21 1 2
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 0.019516 0.000000 0.005941 0.00000
SCALE2 0.000000 0.015454 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014978 0.00000
TER 7077 GLU A 455
MASTER 358 0 3 24 11 0 5 6 7683 1 18 36
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