HEADER TOXIN 11-APR-17 5VGX
TITLE STRUCTURE OF THE C. BOTULINUM NEUROTOXIN SEROTYPE A WITH HG BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BOTULINUM NEUROTOXIN TYPE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BONT/A,BONTOXILYSIN-A,BOTOX;
COMPND 5 EC: 3.4.24.69;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: POLYHISTIDINE-TAGGED BOTULINUM NEUROTOXIN A LIGHT
COMPND 8 CHAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM BOTULINUM;
SOURCE 3 ORGANISM_TAXID: 1491;
SOURCE 4 GENE: BOTA, ATX, BNA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS BOTULINUM, NEUROTOXIN, METALLOPROTEASE, TOXIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.CAROLAN,K.N.ALLEN
REVDAT 5 04-OCT-23 5VGX 1 REMARK
REVDAT 4 11-DEC-19 5VGX 1 REMARK
REVDAT 3 20-SEP-17 5VGX 1 REMARK
REVDAT 2 14-JUN-17 5VGX 1 JRNL
REVDAT 1 31-MAY-17 5VGX 0
JRNL AUTH P.T.BREMER,S.PELLETT,J.P.CAROLAN,W.H.TEPP,L.M.EUBANKS,
JRNL AUTH 2 K.N.ALLEN,E.A.JOHNSON,K.D.JANDA
JRNL TITL METAL IONS EFFECTIVELY ABLATE THE ACTION OF BOTULINUM
JRNL TITL 2 NEUROTOXIN A.
JRNL REF J. AM. CHEM. SOC. V. 139 7264 2017
JRNL REFN ESSN 1520-5126
JRNL PMID 28475321
JRNL DOI 10.1021/JACS.7B01084
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 22328
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.830
REMARK 3 FREE R VALUE TEST SET COUNT : 2477
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 27.5393 - 5.6195 0.95 2237 137 0.1835 0.1968
REMARK 3 2 5.6195 - 4.4665 0.94 2171 136 0.1648 0.1856
REMARK 3 3 4.4665 - 3.9037 0.95 2235 140 0.1521 0.1997
REMARK 3 4 3.9037 - 3.5476 0.98 2270 141 0.1713 0.1975
REMARK 3 5 3.5476 - 3.2938 0.98 2295 142 0.1891 0.2486
REMARK 3 6 3.2938 - 3.0999 0.94 2181 134 0.2125 0.2533
REMARK 3 7 3.0999 - 2.9448 0.95 2241 139 0.2218 0.2992
REMARK 3 8 2.9448 - 2.8168 0.97 2255 138 0.2257 0.3131
REMARK 3 9 2.8168 - 2.7084 0.98 2290 141 0.2265 0.2918
REMARK 3 10 2.7084 - 2.6150 0.98 2304 143 0.2180 0.3085
REMARK 3 11 2.6150 - 2.5333 0.99 2324 144 0.2091 0.2745
REMARK 3 12 2.5333 - 2.4610 0.98 2273 138 0.2158 0.3085
REMARK 3 13 2.4610 - 2.3962 0.89 2068 130 0.2232 0.3056
REMARK 3 14 2.3962 - 2.3378 0.94 2183 139 0.2215 0.2724
REMARK 3 15 2.3378 - 2.2847 0.94 2218 138 0.2174 0.2580
REMARK 3 16 2.2847 - 2.2361 0.94 2186 133 0.2102 0.2669
REMARK 3 17 2.2361 - 2.1913 0.92 2187 138 0.2136 0.2877
REMARK 3 18 2.1913 - 2.1500 0.90 2084 126 0.2314 0.3066
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.46
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 : 0.003 3491
REMARK 3 ANGLE : 0.514 4725
REMARK 3 CHIRALITY : 0.042 516
REMARK 3 PLANARITY : 0.005 612
REMARK 3 DIHEDRAL : 15.854 2075
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1333 -0.5830 80.5388
REMARK 3 T TENSOR
REMARK 3 T11: 0.2359 T22: 0.1384
REMARK 3 T33: 0.1485 T12: -0.0329
REMARK 3 T13: -0.0269 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.0926 L22: 1.1085
REMARK 3 L33: 1.3802 L12: -0.5579
REMARK 3 L13: -0.3380 L23: 0.3151
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: 0.0912 S13: -0.0082
REMARK 3 S21: -0.0648 S22: -0.0686 S23: 0.1076
REMARK 3 S31: -0.0832 S32: -0.1195 S33: 0.0005
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT PERFORMED UTILIZING XYZ
REMARK 3 COORDINATE, REAL SPACE, TLS, ANOMALOUS GROUPS, AND INDIVIDUAL B-
REMARK 3 FACTOR PARAMETERS.
REMARK 4
REMARK 4 5VGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227411.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-17
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 : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99164
REMARK 200 MONOCHROMATOR : SI(111) AND SI(220) DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : MIRROR: RH COATED FLAT, TOROIDAL
REMARK 200 FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22337
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 27.539
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.15150
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.31440
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3BOK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000 8%, CALCIUM ACETATE 0.2 M,
REMARK 280 SODIUM CACODYLATE 0.1 M, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
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 33.33850
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 TOTAL BURIED SURFACE AREA: 380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
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 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 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PHE A 423
REMARK 465 GLU A 424
REMARK 465 PHE A 425
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 H2 ACT A 502 O HOH A 693 1.48
REMARK 500 O ASN A 26 O HOH A 601 1.96
REMARK 500 OE2 GLU A 262 O HOH A 602 1.99
REMARK 500 O GLY A 28 O HOH A 601 2.06
REMARK 500 OD2 ASP A 388 O HOH A 603 2.14
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 OE2 GLU A 197 NZ LYS A 343 2647 2.17
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 VAL A 17 -73.17 -113.65
REMARK 500 GLU A 56 56.89 -118.01
REMARK 500 PRO A 63 55.46 -96.81
REMARK 500 GLN A 67 117.64 -165.94
REMARK 500 ASP A 74 98.56 -166.40
REMARK 500 THR A 132 0.52 -68.87
REMARK 500 SER A 157 -148.51 -84.16
REMARK 500 ASN A 368 -162.21 -124.20
REMARK 500 ASN A 409 44.07 -98.17
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 HG A 501 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 165 SG
REMARK 620 2 HOH A 691 O 174.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VGV RELATED DB: PDB
REMARK 900 5VGV CONTAINS THE SAME PROTEIN COMPLEXED WITH MERCURY IN PLACE OF
REMARK 900 COPPER
DBREF 5VGX A 1 425 UNP P10845 BXA1_CLOBO 1 425
SEQADV 5VGX HIS A -15 UNP P10845 EXPRESSION TAG
SEQADV 5VGX HIS A -14 UNP P10845 EXPRESSION TAG
SEQADV 5VGX HIS A -13 UNP P10845 EXPRESSION TAG
SEQADV 5VGX HIS A -12 UNP P10845 EXPRESSION TAG
SEQADV 5VGX HIS A -11 UNP P10845 EXPRESSION TAG
SEQADV 5VGX HIS A -10 UNP P10845 EXPRESSION TAG
SEQADV 5VGX SER A -9 UNP P10845 EXPRESSION TAG
SEQADV 5VGX SER A -8 UNP P10845 EXPRESSION TAG
SEQADV 5VGX GLY A -7 UNP P10845 EXPRESSION TAG
SEQADV 5VGX LEU A -6 UNP P10845 EXPRESSION TAG
SEQADV 5VGX VAL A -5 UNP P10845 EXPRESSION TAG
SEQADV 5VGX PRO A -4 UNP P10845 EXPRESSION TAG
SEQADV 5VGX ARG A -3 UNP P10845 EXPRESSION TAG
SEQADV 5VGX GLY A -2 UNP P10845 EXPRESSION TAG
SEQADV 5VGX SER A -1 UNP P10845 EXPRESSION TAG
SEQADV 5VGX HIS A 0 UNP P10845 EXPRESSION TAG
SEQADV 5VGX GLN A 2 UNP P10845 PRO 2 ENGINEERED MUTATION
SEQRES 1 A 441 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG
SEQRES 2 A 441 GLY SER HIS MET GLN PHE VAL ASN LYS GLN PHE ASN TYR
SEQRES 3 A 441 LYS ASP PRO VAL ASN GLY VAL ASP ILE ALA TYR ILE LYS
SEQRES 4 A 441 ILE PRO ASN VAL GLY GLN MET GLN PRO VAL LYS ALA PHE
SEQRES 5 A 441 LYS ILE HIS ASN LYS ILE TRP VAL ILE PRO GLU ARG ASP
SEQRES 6 A 441 THR PHE THR ASN PRO GLU GLU GLY ASP LEU ASN PRO PRO
SEQRES 7 A 441 PRO GLU ALA LYS GLN VAL PRO VAL SER TYR TYR ASP SER
SEQRES 8 A 441 THR TYR LEU SER THR ASP ASN GLU LYS ASP ASN TYR LEU
SEQRES 9 A 441 LYS GLY VAL THR LYS LEU PHE GLU ARG ILE TYR SER THR
SEQRES 10 A 441 ASP LEU GLY ARG MET LEU LEU THR SER ILE VAL ARG GLY
SEQRES 11 A 441 ILE PRO PHE TRP GLY GLY SER THR ILE ASP THR GLU LEU
SEQRES 12 A 441 LYS VAL ILE ASP THR ASN CYS ILE ASN VAL ILE GLN PRO
SEQRES 13 A 441 ASP GLY SER TYR ARG SER GLU GLU LEU ASN LEU VAL ILE
SEQRES 14 A 441 ILE GLY PRO SER ALA ASP ILE ILE GLN PHE GLU CYS LYS
SEQRES 15 A 441 SER PHE GLY HIS GLU VAL LEU ASN LEU THR ARG ASN GLY
SEQRES 16 A 441 TYR GLY SER THR GLN TYR ILE ARG PHE SER PRO ASP PHE
SEQRES 17 A 441 THR PHE GLY PHE GLU GLU SER LEU GLU VAL ASP THR ASN
SEQRES 18 A 441 PRO LEU LEU GLY ALA GLY LYS PHE ALA THR ASP PRO ALA
SEQRES 19 A 441 VAL THR LEU ALA HIS GLU LEU ILE HIS ALA GLY HIS ARG
SEQRES 20 A 441 LEU TYR GLY ILE ALA ILE ASN PRO ASN ARG VAL PHE LYS
SEQRES 21 A 441 VAL ASN THR ASN ALA TYR TYR GLU MET SER GLY LEU GLU
SEQRES 22 A 441 VAL SER PHE GLU GLU LEU ARG THR PHE GLY GLY HIS ASP
SEQRES 23 A 441 ALA LYS PHE ILE ASP SER LEU GLN GLU ASN GLU PHE ARG
SEQRES 24 A 441 LEU TYR TYR TYR ASN LYS PHE LYS ASP ILE ALA SER THR
SEQRES 25 A 441 LEU ASN LYS ALA LYS SER ILE VAL GLY THR THR ALA SER
SEQRES 26 A 441 LEU GLN TYR MET LYS ASN VAL PHE LYS GLU LYS TYR LEU
SEQRES 27 A 441 LEU SER GLU ASP THR SER GLY LYS PHE SER VAL ASP LYS
SEQRES 28 A 441 LEU LYS PHE ASP LYS LEU TYR LYS MET LEU THR GLU ILE
SEQRES 29 A 441 TYR THR GLU ASP ASN PHE VAL LYS PHE PHE LYS VAL LEU
SEQRES 30 A 441 ASN ARG LYS THR TYR LEU ASN PHE ASP LYS ALA VAL PHE
SEQRES 31 A 441 LYS ILE ASN ILE VAL PRO LYS VAL ASN TYR THR ILE TYR
SEQRES 32 A 441 ASP GLY PHE ASN LEU ARG ASN THR ASN LEU ALA ALA ASN
SEQRES 33 A 441 PHE ASN GLY GLN ASN THR GLU ILE ASN ASN MET ASN PHE
SEQRES 34 A 441 THR LYS LEU LYS ASN PHE THR GLY LEU PHE GLU PHE
HET HG A 501 1
HET ACT A 502 7
HETNAM HG MERCURY (II) ION
HETNAM ACT ACETATE ION
FORMUL 2 HG HG 2+
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 HOH *98(H2 O)
HELIX 1 AA1 ASN A 53 GLY A 57 5 5
HELIX 2 AA2 THR A 80 SER A 100 1 21
HELIX 3 AA3 THR A 101 GLY A 114 1 14
HELIX 4 AA4 ILE A 130 THR A 132 5 3
HELIX 5 AA5 ASN A 174 ASN A 178 5 5
HELIX 6 AA6 SER A 199 THR A 204 1 6
HELIX 7 AA7 ASP A 216 TYR A 233 1 18
HELIX 8 AA8 ASN A 248 SER A 254 1 7
HELIX 9 AA9 PHE A 260 GLY A 267 1 8
HELIX 10 AB1 HIS A 269 ILE A 274 5 6
HELIX 11 AB2 ASP A 275 ALA A 300 1 26
HELIX 12 AB3 SER A 309 TYR A 321 1 13
HELIX 13 AB4 ASP A 334 GLU A 347 1 14
HELIX 14 AB5 THR A 350 LYS A 359 1 10
HELIX 15 AB6 ASN A 409 PHE A 413 5 5
SHEET 1 AA1 8 TYR A 144 GLU A 148 0
SHEET 2 AA1 8 CYS A 134 ILE A 138 -1 N VAL A 137 O ARG A 145
SHEET 3 AA1 8 ILE A 19 LYS A 23 -1 N TYR A 21 O ILE A 138
SHEET 4 AA1 8 VAL A 33 HIS A 39 -1 O ALA A 35 N ALA A 20
SHEET 5 AA1 8 ILE A 42 ARG A 48 -1 O ILE A 42 N HIS A 39
SHEET 6 AA1 8 LEU A 151 GLY A 155 1 O ILE A 153 N ILE A 45
SHEET 7 AA1 8 GLN A 184 ARG A 187 1 O ILE A 186 N VAL A 152
SHEET 8 AA1 8 GLU A 164 LYS A 166 -1 N LYS A 166 O TYR A 185
SHEET 1 AA2 2 GLU A 126 LEU A 127 0
SHEET 2 AA2 2 SER A 302 ILE A 303 1 O SER A 302 N LEU A 127
SHEET 1 AA3 4 PHE A 213 ALA A 214 0
SHEET 2 AA3 4 PHE A 192 PHE A 196 -1 N PHE A 196 O PHE A 213
SHEET 3 AA3 4 ALA A 372 LYS A 375 -1 O PHE A 374 N THR A 193
SHEET 4 AA3 4 THR A 414 ASN A 418 -1 O THR A 414 N LYS A 375
SHEET 1 AA4 2 VAL A 242 LYS A 244 0
SHEET 2 AA4 2 GLU A 257 SER A 259 -1 O VAL A 258 N PHE A 243
SHEET 1 AA5 2 SER A 324 GLU A 325 0
SHEET 2 AA5 2 PHE A 331 SER A 332 -1 O SER A 332 N SER A 324
LINK SG CYS A 165 HG HG A 501 1555 1555 2.54
LINK HG HG A 501 O HOH A 691 1555 1555 2.44
SITE 1 AC1 4 CYS A 165 GLU A 224 HIS A 227 HOH A 691
SITE 1 AC2 4 CYS A 134 SER A 146 GLU A 148 HOH A 693
CRYST1 49.449 66.677 65.115 90.00 98.92 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 0.020223 0.000000 0.003174 0.00000
SCALE2 0.000000 0.014998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015545 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
