HEADER HYDROLASE 06-APR-12 4EJ5
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF BOTULINUM NEUROTOXIN
TITLE 2 BONT/A WILD-TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOTULINUM NEUROTOXIN A LIGHT CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-425;
COMPND 5 SYNONYM: BONT/A, BONTOXILYSIN-A, BOTOX;
COMPND 6 EC: 3.4.24.69;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM;
SOURCE 3 ORGANISM_TAXID: 1491;
SOURCE 4 STRAIN: HALL ATCC 3502;
SOURCE 5 GENE: BOTA, ATX, BNA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS METALLOPROTEASE, PEPTIDASE M27 SUPERFAMILY, CLOSTRIDIAL NEUROTOXIN
KEYWDS 2 ZINC PROTEASE, HUMAN TARGET SNAP-25, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.STURA,L.VERA,V.DIVE
REVDAT 5 20-SEP-23 4EJ5 1 REMARK
REVDAT 4 21-DEC-22 4EJ5 1 REMARK SEQADV LINK
REVDAT 3 17-OCT-12 4EJ5 1 JRNL
REVDAT 2 29-AUG-12 4EJ5 1 JRNL
REVDAT 1 15-AUG-12 4EJ5 0
JRNL AUTH E.A.STURA,L.LE ROUX,K.GUITOT,S.GARCIA,S.BREGANT,F.BEAU,
JRNL AUTH 2 L.VERA,G.COLLET,D.PTCHELKINE,H.BAKIRCI,V.DIVE
JRNL TITL STRUCTURAL FRAMEWORK FOR COVALENT INHIBITION OF CLOSTRIDIUM
JRNL TITL 2 BOTULINUM NEUROTOXIN A BY TARGETING CYS165.
JRNL REF J.BIOL.CHEM. V. 287 33607 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22869371
JRNL DOI 10.1074/JBC.M112.396697
REMARK 2
REMARK 2 RESOLUTION. 1.87 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-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) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 34577
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1731
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 42.1660 - 4.2821 0.98 2757 148 0.1640 0.1877
REMARK 3 2 4.2821 - 3.3993 1.00 2757 145 0.1356 0.1761
REMARK 3 3 3.3993 - 2.9697 1.00 2749 144 0.1502 0.1898
REMARK 3 4 2.9697 - 2.6982 1.00 2756 145 0.1523 0.2063
REMARK 3 5 2.6982 - 2.5049 1.00 2710 143 0.1572 0.1928
REMARK 3 6 2.5049 - 2.3572 1.00 2750 145 0.1624 0.2163
REMARK 3 7 2.3572 - 2.2391 1.00 2703 142 0.1613 0.2485
REMARK 3 8 2.2391 - 2.1417 1.00 2751 145 0.1659 0.2355
REMARK 3 9 2.1417 - 2.0592 1.00 2732 144 0.1727 0.2475
REMARK 3 10 2.0592 - 1.9882 1.00 2719 143 0.1803 0.2412
REMARK 3 11 1.9882 - 1.9260 1.00 2735 144 0.2044 0.2522
REMARK 3 12 1.9260 - 1.8700 0.99 2727 143 0.2407 0.2875
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 62.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.09
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.85270
REMARK 3 B22 (A**2) : -0.76570
REMARK 3 B33 (A**2) : -1.08700
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.13300
REMARK 3 B23 (A**2) : 0.00000
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 : 0.007 3663
REMARK 3 ANGLE : 1.041 4957
REMARK 3 CHIRALITY : 0.075 532
REMARK 3 PLANARITY : 0.005 647
REMARK 3 DIHEDRAL : 18.134 1327
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 4EJ5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34616
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 42.170
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.190
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.17
REMARK 200 R MERGE FOR SHELL (I) : 0.31700
REMARK 200 R SYM FOR SHELL (I) : 0.36300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.830
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2ILP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8.3% MONOMETHYL POLYETHYLENE GLYCOL
REMARK 280 2000, 0.17 M LITHIUM SULFATE, 6.25% 4,2 METHYL PENTANE DIOL, 0.1
REMARK 280 M IMIDAZOLE MALATE, PH 6.0, CRYOPROTECTANT: 18% MPEG2K, 22% MPD,
REMARK 280 10% DMSO, .050 M BICINE, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.0K
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 33.18500
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
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 VAL A 17 -72.80 -122.10
REMARK 500 ASN A 26 -63.56 81.10
REMARK 500 SER A 157 -144.68 -81.98
REMARK 500 ASN A 409 45.63 -97.45
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 223 NE2
REMARK 620 2 HIS A 227 NE2 98.8
REMARK 620 3 GLU A 262 OE2 101.7 96.7
REMARK 620 4 GLU A 262 OE1 152.9 91.8 52.0
REMARK 620 5 HOH A 944 O 106.5 107.6 139.0 93.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ISE RELATED DB: PDB
REMARK 900 BOTULINUM NEUROTOXIN A LIGHT CHAIN WT CRYSTAL FORM A
REMARK 900 RELATED ID: 3BWI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF BOTULINUM NEUROTOXIN
REMARK 900 SEROTYPE A WITH AN ACETATE ION BOUND AT THE ACTIVE SITE
REMARK 900 RELATED ID: 4ELC RELATED DB: PDB
REMARK 900 RELATED ID: 4EL4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF BOTULINUM NEUROTOXIN
REMARK 900 BONT/A C134S/C165S DOUBLE MUTANT
DBREF 4EJ5 A 1 425 UNP P10845 BXA1_CLOBO 1 425
SEQADV 4EJ5 MET A -19 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 GLY A -18 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 SER A -17 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 SER A -16 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A -15 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A -14 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A -13 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A -12 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A -11 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A -10 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 SER A -9 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 SER A -8 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 GLY A -7 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 LEU A -6 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 VAL A -5 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 PRO A -4 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 ARG A -3 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 GLY A -2 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 SER A -1 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 HIS A 0 UNP P10845 EXPRESSION TAG
SEQADV 4EJ5 ALA A 27 UNP P10845 VAL 27 VARIANT
SEQRES 1 A 445 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 445 LEU VAL PRO ARG GLY SER HIS MET PRO PHE VAL ASN LYS
SEQRES 3 A 445 GLN PHE ASN TYR LYS ASP PRO VAL ASN GLY VAL ASP ILE
SEQRES 4 A 445 ALA TYR ILE LYS ILE PRO ASN ALA GLY GLN MET GLN PRO
SEQRES 5 A 445 VAL LYS ALA PHE LYS ILE HIS ASN LYS ILE TRP VAL ILE
SEQRES 6 A 445 PRO GLU ARG ASP THR PHE THR ASN PRO GLU GLU GLY ASP
SEQRES 7 A 445 LEU ASN PRO PRO PRO GLU ALA LYS GLN VAL PRO VAL SER
SEQRES 8 A 445 TYR TYR ASP SER THR TYR LEU SER THR ASP ASN GLU LYS
SEQRES 9 A 445 ASP ASN TYR LEU LYS GLY VAL THR LYS LEU PHE GLU ARG
SEQRES 10 A 445 ILE TYR SER THR ASP LEU GLY ARG MET LEU LEU THR SER
SEQRES 11 A 445 ILE VAL ARG GLY ILE PRO PHE TRP GLY GLY SER THR ILE
SEQRES 12 A 445 ASP THR GLU LEU LYS VAL ILE ASP THR ASN CYS ILE ASN
SEQRES 13 A 445 VAL ILE GLN PRO ASP GLY SER TYR ARG SER GLU GLU LEU
SEQRES 14 A 445 ASN LEU VAL ILE ILE GLY PRO SER ALA ASP ILE ILE GLN
SEQRES 15 A 445 PHE GLU CYS LYS SER PHE GLY HIS GLU VAL LEU ASN LEU
SEQRES 16 A 445 THR ARG ASN GLY TYR GLY SER THR GLN TYR ILE ARG PHE
SEQRES 17 A 445 SER PRO ASP PHE THR PHE GLY PHE GLU GLU SER LEU GLU
SEQRES 18 A 445 VAL ASP THR ASN PRO LEU LEU GLY ALA GLY LYS PHE ALA
SEQRES 19 A 445 THR ASP PRO ALA VAL THR LEU ALA HIS GLU LEU ILE HIS
SEQRES 20 A 445 ALA GLY HIS ARG LEU TYR GLY ILE ALA ILE ASN PRO ASN
SEQRES 21 A 445 ARG VAL PHE LYS VAL ASN THR ASN ALA TYR TYR GLU MET
SEQRES 22 A 445 SER GLY LEU GLU VAL SER PHE GLU GLU LEU ARG THR PHE
SEQRES 23 A 445 GLY GLY HIS ASP ALA LYS PHE ILE ASP SER LEU GLN GLU
SEQRES 24 A 445 ASN GLU PHE ARG LEU TYR TYR TYR ASN LYS PHE LYS ASP
SEQRES 25 A 445 ILE ALA SER THR LEU ASN LYS ALA LYS SER ILE VAL GLY
SEQRES 26 A 445 THR THR ALA SER LEU GLN TYR MET LYS ASN VAL PHE LYS
SEQRES 27 A 445 GLU LYS TYR LEU LEU SER GLU ASP THR SER GLY LYS PHE
SEQRES 28 A 445 SER VAL ASP LYS LEU LYS PHE ASP LYS LEU TYR LYS MET
SEQRES 29 A 445 LEU THR GLU ILE TYR THR GLU ASP ASN PHE VAL LYS PHE
SEQRES 30 A 445 PHE LYS VAL LEU ASN ARG LYS THR TYR LEU ASN PHE ASP
SEQRES 31 A 445 LYS ALA VAL PHE LYS ILE ASN ILE VAL PRO LYS VAL ASN
SEQRES 32 A 445 TYR THR ILE TYR ASP GLY PHE ASN LEU ARG ASN THR ASN
SEQRES 33 A 445 LEU ALA ALA ASN PHE ASN GLY GLN ASN THR GLU ILE ASN
SEQRES 34 A 445 ASN MET ASN PHE THR LYS LEU LYS ASN PHE THR GLY LEU
SEQRES 35 A 445 PHE GLU PHE
HET ZN A 501 1
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET SO4 A 505 5
HET IMD A 506 5
HET CO3 A 507 4
HET GOL A 508 6
HETNAM ZN ZINC ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM IMD IMIDAZOLE
HETNAM CO3 CARBONATE ION
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 EDO 3(C2 H6 O2)
FORMUL 6 SO4 O4 S 2-
FORMUL 7 IMD C3 H5 N2 1+
FORMUL 8 CO3 C O3 2-
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *387(H2 O)
HELIX 1 1 ASN A 53 GLY A 57 5 5
HELIX 2 2 THR A 80 SER A 100 1 21
HELIX 3 3 THR A 101 GLY A 114 1 14
HELIX 4 4 ILE A 130 THR A 132 5 3
HELIX 5 5 SER A 199 THR A 204 1 6
HELIX 6 6 ASP A 216 TYR A 233 1 18
HELIX 7 7 ASN A 248 SER A 254 1 7
HELIX 8 8 PHE A 260 GLY A 267 1 8
HELIX 9 9 GLY A 268 ILE A 274 5 7
HELIX 10 10 ASP A 275 ALA A 300 1 26
HELIX 11 11 SER A 309 TYR A 321 1 13
HELIX 12 12 ASP A 334 GLU A 347 1 14
HELIX 13 13 THR A 350 LYS A 359 1 10
HELIX 14 14 PHE A 401 ASN A 405 5 5
HELIX 15 15 ASN A 409 PHE A 413 5 5
SHEET 1 A 8 TYR A 144 GLU A 148 0
SHEET 2 A 8 CYS A 134 ILE A 138 -1 N ILE A 135 O GLU A 147
SHEET 3 A 8 ILE A 19 LYS A 23 -1 N TYR A 21 O ILE A 138
SHEET 4 A 8 VAL A 33 HIS A 39 -1 O ALA A 35 N ALA A 20
SHEET 5 A 8 ILE A 42 ARG A 48 -1 O VAL A 44 N PHE A 36
SHEET 6 A 8 LEU A 151 GLY A 155 1 O ILE A 153 N ILE A 45
SHEET 7 A 8 GLN A 184 ARG A 187 1 O ILE A 186 N VAL A 152
SHEET 8 A 8 GLU A 164 LYS A 166 -1 N LYS A 166 O TYR A 185
SHEET 1 B 2 GLU A 126 LYS A 128 0
SHEET 2 B 2 SER A 302 VAL A 304 1 O SER A 302 N LEU A 127
SHEET 1 C 4 PHE A 213 ALA A 214 0
SHEET 2 C 4 PHE A 192 PHE A 196 -1 N PHE A 196 O PHE A 213
SHEET 3 C 4 ALA A 372 LYS A 375 -1 O PHE A 374 N THR A 193
SHEET 4 C 4 THR A 414 ASN A 418 -1 O LEU A 416 N VAL A 373
SHEET 1 D 2 VAL A 242 LYS A 244 0
SHEET 2 D 2 GLU A 257 SER A 259 -1 O VAL A 258 N PHE A 243
SHEET 1 E 2 SER A 324 GLU A 325 0
SHEET 2 E 2 PHE A 331 SER A 332 -1 O SER A 332 N SER A 324
LINK NE2 HIS A 223 ZN ZN A 501 1555 1555 2.08
LINK NE2 HIS A 227 ZN ZN A 501 1555 1555 2.12
LINK OE2 GLU A 262 ZN ZN A 501 1555 1555 2.12
LINK OE1 GLU A 262 ZN ZN A 501 1555 1555 2.61
LINK ZN ZN A 501 O HOH A 944 1555 1555 2.08
CISPEP 1 GLY A 28 GLN A 29 0 -22.98
SITE 1 AC1 5 HIS A 223 HIS A 227 GLU A 262 HOH A 935
SITE 2 AC1 5 HOH A 944
SITE 1 AC2 5 ASN A 238 ARG A 241 PHE A 282 TYR A 285
SITE 2 AC2 5 TYR A 286
SITE 1 AC3 7 ASN A 174 LEU A 175 THR A 176 ARG A 177
SITE 2 AC3 7 ASN A 394 HOH A 617 HOH A 978
SITE 1 AC4 5 LYS A 375 ASN A 412 PHE A 413 THR A 414
SITE 2 AC4 5 HOH A 778
SITE 1 AC5 6 GLU A 198 SER A 199 LEU A 200 HOH A 708
SITE 2 AC5 6 HOH A 757 HOH A 758
SITE 1 AC6 5 ALA A 210 LYS A 415 ASN A 418 HOH A 693
SITE 2 AC6 5 HOH A 860
SITE 1 AC7 7 ARG A 363 ASP A 370 HOH A 834 HOH A 923
SITE 2 AC7 7 HOH A 934 HOH A 940 HOH A 941
SITE 1 AC8 5 ALA A 65 LYS A 66 GLN A 67 HOH A 956
SITE 2 AC8 5 HOH A 957
CRYST1 49.950 66.370 64.720 90.00 98.24 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 0.020020 0.000000 0.002899 0.00000
SCALE2 0.000000 0.015067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015612 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
