HEADER HYDROLASE 02-AUG-10 3O8D
TITLE VISUALIZING ATP-DEPENDENT RNA TRANSLOCATION BY THE NS3 HELICASE FROM
TITLE 2 HCV
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HCV NS3 PROTEASE/HELICASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.4.21.98, 3.6.1.15, 3.6.4.13;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS SUBTYPE 1B;
SOURCE 3 ORGANISM_TAXID: 31647;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HELICASE, NTPASE, HCV, RNA, TRANSLOCATION, ADP, BERYLLIUM
KEYWDS 2 TRIFLUORIDE, PROTEASE/NTPASE/HELICASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.C.APPLEBY,J.R.SOMOZA
REVDAT 3 06-SEP-23 3O8D 1 REMARK SEQADV LINK
REVDAT 2 02-FEB-11 3O8D 1 JRNL
REVDAT 1 05-JAN-11 3O8D 0
JRNL AUTH T.C.APPLEBY,R.ANDERSON,O.FEDOROVA,A.M.PYLE,R.WANG,X.LIU,
JRNL AUTH 2 K.M.BRENDZA,J.R.SOMOZA
JRNL TITL VISUALIZING ATP-DEPENDENT RNA TRANSLOCATION BY THE NS3
JRNL TITL 2 HELICASE FROM HCV.
JRNL REF J.MOL.BIOL. V. 405 1139 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21145896
JRNL DOI 10.1016/J.JMB.2010.11.034
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 86664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1908
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 47.0359 - 4.4158 1.00 9211 209 0.1673 0.1948
REMARK 3 2 4.4158 - 3.5053 1.00 8931 202 0.1635 0.1924
REMARK 3 3 3.5053 - 3.0623 0.99 8807 198 0.1919 0.2305
REMARK 3 4 3.0623 - 2.7824 0.98 8626 196 0.2014 0.2263
REMARK 3 5 2.7824 - 2.5830 0.96 8484 194 0.2069 0.2756
REMARK 3 6 2.5830 - 2.4307 0.95 8398 187 0.2160 0.2825
REMARK 3 7 2.4307 - 2.3090 0.94 8267 184 0.2134 0.2834
REMARK 3 8 2.3090 - 2.2085 0.92 8097 176 0.2137 0.2803
REMARK 3 9 2.2085 - 2.1234 0.92 8072 183 0.2256 0.2820
REMARK 3 10 2.1234 - 2.0500 0.90 7863 179 0.2380 0.3102
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 31.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.940
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.14470
REMARK 3 B22 (A**2) : -2.13300
REMARK 3 B33 (A**2) : -1.01170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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 : 0.008 9907
REMARK 3 ANGLE : 1.140 13544
REMARK 3 CHIRALITY : 0.070 1582
REMARK 3 PLANARITY : 0.005 1736
REMARK 3 DIHEDRAL : 13.728 3534
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 3O8D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000060793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-09
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 : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90501
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.42700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 3O8B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3350, 160 MM LISO4, 80
REMARK 280 MM BIS-TRIS, 10% (V/V) GLYCEROL, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 44.87450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.18700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.20800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.18700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.87450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.20800
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
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 -36
REMARK 465 GLY A -35
REMARK 465 SER A -34
REMARK 465 SER A -33
REMARK 465 HIS A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 SER A -26
REMARK 465 SER A -25
REMARK 465 GLY A -24
REMARK 465 LEU A -23
REMARK 465 VAL A -22
REMARK 465 PRO A -21
REMARK 465 ARG A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 MET A -16
REMARK 465 MET B -36
REMARK 465 GLY B -35
REMARK 465 SER B -34
REMARK 465 SER B -33
REMARK 465 HIS B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 SER B -26
REMARK 465 SER B -25
REMARK 465 GLY B -24
REMARK 465 LEU B -23
REMARK 465 VAL B -22
REMARK 465 PRO B -21
REMARK 465 ARG B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 MET B -16
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 PHE A 43 -164.53 -166.74
REMARK 500 CYS A 99 4.75 -150.79
REMARK 500 ASN A 187 40.12 -92.04
REMARK 500 THR A 212 -68.76 -124.20
REMARK 500 LYS A 352 -161.76 -121.36
REMARK 500 ASP A 412 6.69 -66.93
REMARK 500 THR A 443 -94.14 -131.04
REMARK 500 HIS A 541 41.43 74.08
REMARK 500 LEU B 14 151.25 -48.09
REMARK 500 CYS B 16 -79.55 -26.07
REMARK 500 THR B 38 -166.84 -101.80
REMARK 500 PHE B 197 134.30 -39.85
REMARK 500 THR B 212 -65.62 -128.87
REMARK 500 CYS B 292 6.23 -68.93
REMARK 500 LYS B 352 -160.18 -112.43
REMARK 500 ASP B 412 2.68 -67.08
REMARK 500 THR B 443 -94.44 -126.65
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 MG A 850 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 2 O
REMARK 620 2 SER A 211 OG 88.8
REMARK 620 3 GLU A 291 OE2 78.5 88.0
REMARK 620 4 HOH A 633 O 172.3 91.0 93.8
REMARK 620 5 ADP A 875 O1B 96.6 90.6 174.9 91.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF A 885 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 875 O3B
REMARK 620 2 BEF A 885 F1 113.6
REMARK 620 3 BEF A 885 F2 106.5 108.9
REMARK 620 4 BEF A 885 F3 110.4 107.1 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 850 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 211 OG
REMARK 620 2 GLU B 291 OE2 90.9
REMARK 620 3 HOH B 637 O 80.8 83.3
REMARK 620 4 HOH B 644 O 94.1 95.2 174.7
REMARK 620 5 ADP B 875 O1B 87.6 177.5 94.5 86.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF B 885 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 875 O3B
REMARK 620 2 BEF B 885 F1 112.9
REMARK 620 3 BEF B 885 F2 103.5 108.2
REMARK 620 4 BEF B 885 F3 111.5 109.4 111.1
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 MG A 850
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 875
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF A 885
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 895
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 850
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 875
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF B 885
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 895
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CU1 RELATED DB: PDB
REMARK 900 RELATED ID: 3O8B RELATED DB: PDB
REMARK 900 RELATED ID: 3O8C RELATED DB: PDB
REMARK 900 RELATED ID: 3O8R RELATED DB: PDB
DBREF 3O8D A 3 631 UNP Q99AU2 Q99AU2_9HEPC 1029 1657
DBREF 3O8D B 3 631 UNP Q99AU2 Q99AU2_9HEPC 1029 1657
SEQADV 3O8D MET A -36 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -35 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -34 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -33 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -32 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -31 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -30 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -29 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -28 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -27 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -26 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -25 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -24 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D LEU A -23 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL A -22 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D PRO A -21 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ARG A -20 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -19 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -18 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS A -17 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D MET A -16 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -15 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -14 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL A -13 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL A -12 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ILE A -11 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL A -10 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -9 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ARG A -8 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ILE A -7 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ILE A -6 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D LEU A -5 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -4 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -3 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A -2 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY A -1 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER A 0 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D MET B -36 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -35 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -34 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -33 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -32 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -31 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -30 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -29 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -28 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -27 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -26 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -25 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -24 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D LEU B -23 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL B -22 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D PRO B -21 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ARG B -20 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -19 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -18 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D HIS B -17 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D MET B -16 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -15 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -14 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL B -13 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL B -12 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ILE B -11 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D VAL B -10 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -9 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ARG B -8 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ILE B -7 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D ILE B -6 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D LEU B -5 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -4 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -3 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B -2 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D GLY B -1 UNP Q99AU2 EXPRESSION TAG
SEQADV 3O8D SER B 0 UNP Q99AU2 EXPRESSION TAG
SEQRES 1 A 666 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 666 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL VAL ILE
SEQRES 3 A 666 VAL GLY ARG ILE ILE LEU SER GLY SER GLY SER ILE THR
SEQRES 4 A 666 ALA TYR SER GLN GLN THR ARG GLY LEU LEU GLY CYS ILE
SEQRES 5 A 666 ILE THR SER LEU THR GLY ARG ASP LYS ASN GLN VAL GLU
SEQRES 6 A 666 GLY GLU VAL GLN VAL VAL SER THR ALA THR GLN SER PHE
SEQRES 7 A 666 LEU ALA THR CYS VAL ASN GLY VAL CYS TRP THR VAL TYR
SEQRES 8 A 666 HIS GLY ALA GLY SER LYS THR LEU ALA GLY PRO LYS GLY
SEQRES 9 A 666 PRO ILE THR GLN MET TYR THR ASN VAL ASP GLN ASP LEU
SEQRES 10 A 666 VAL GLY TRP GLN ALA PRO PRO GLY ALA ARG SER LEU THR
SEQRES 11 A 666 PRO CYS THR CYS GLY SER SER ASP LEU TYR LEU VAL THR
SEQRES 12 A 666 ARG HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG GLY ASP
SEQRES 13 A 666 SER ARG GLY SER LEU LEU SER PRO ARG PRO VAL SER TYR
SEQRES 14 A 666 LEU LYS GLY SER SER GLY GLY PRO LEU LEU CYS PRO SER
SEQRES 15 A 666 GLY HIS ALA VAL GLY ILE PHE ARG ALA ALA VAL CYS THR
SEQRES 16 A 666 ARG GLY VAL ALA LYS ALA VAL ASP PHE VAL PRO VAL GLU
SEQRES 17 A 666 SER MET GLU THR THR MET ARG SER PRO VAL PHE THR ASP
SEQRES 18 A 666 ASN SER SER PRO PRO ALA VAL PRO GLN SER PHE GLN VAL
SEQRES 19 A 666 ALA HIS LEU HIS ALA PRO THR GLY SER GLY LYS SER THR
SEQRES 20 A 666 LYS VAL PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL
SEQRES 21 A 666 LEU VAL LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE
SEQRES 22 A 666 GLY ALA TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN
SEQRES 23 A 666 ILE ARG THR GLY VAL ARG THR ILE THR THR GLY ALA PRO
SEQRES 24 A 666 VAL THR TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY
SEQRES 25 A 666 GLY CYS SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP
SEQRES 26 A 666 GLU CYS HIS SER THR ASP SER THR THR ILE LEU GLY ILE
SEQRES 27 A 666 GLY THR VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG
SEQRES 28 A 666 LEU VAL VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL
SEQRES 29 A 666 THR VAL PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER
SEQRES 30 A 666 ASN THR GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO
SEQRES 31 A 666 ILE GLU ALA ILE ARG GLY GLY ARG HIS LEU ILE PHE CYS
SEQRES 32 A 666 HIS SER LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU
SEQRES 33 A 666 SER GLY LEU GLY ILE ASN ALA VAL ALA TYR TYR ARG GLY
SEQRES 34 A 666 LEU ASP VAL SER VAL ILE PRO THR ILE GLY ASP VAL VAL
SEQRES 35 A 666 VAL VAL ALA THR ASP ALA LEU MET THR GLY TYR THR GLY
SEQRES 36 A 666 ASP PHE ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR
SEQRES 37 A 666 GLN THR VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE
SEQRES 38 A 666 GLU THR THR THR VAL PRO GLN ASP ALA VAL SER ARG SER
SEQRES 39 A 666 GLN ARG ARG GLY ARG THR GLY ARG GLY ARG ARG GLY ILE
SEQRES 40 A 666 TYR ARG PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET
SEQRES 41 A 666 PHE ASP SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY
SEQRES 42 A 666 CYS ALA TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL
SEQRES 43 A 666 ARG LEU ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL
SEQRES 44 A 666 CYS GLN ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR
SEQRES 45 A 666 GLY LEU THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR
SEQRES 46 A 666 LYS GLN ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR
SEQRES 47 A 666 GLN ALA THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO
SEQRES 48 A 666 SER TRP ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS
SEQRES 49 A 666 PRO THR LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU
SEQRES 50 A 666 GLY ALA VAL GLN ASN GLU VAL THR LEU THR HIS PRO ILE
SEQRES 51 A 666 THR LYS TYR ILE MET ALA CYS MET SER ALA ASP LEU GLU
SEQRES 52 A 666 VAL VAL THR
SEQRES 1 B 666 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 666 LEU VAL PRO ARG GLY SER HIS MET GLY SER VAL VAL ILE
SEQRES 3 B 666 VAL GLY ARG ILE ILE LEU SER GLY SER GLY SER ILE THR
SEQRES 4 B 666 ALA TYR SER GLN GLN THR ARG GLY LEU LEU GLY CYS ILE
SEQRES 5 B 666 ILE THR SER LEU THR GLY ARG ASP LYS ASN GLN VAL GLU
SEQRES 6 B 666 GLY GLU VAL GLN VAL VAL SER THR ALA THR GLN SER PHE
SEQRES 7 B 666 LEU ALA THR CYS VAL ASN GLY VAL CYS TRP THR VAL TYR
SEQRES 8 B 666 HIS GLY ALA GLY SER LYS THR LEU ALA GLY PRO LYS GLY
SEQRES 9 B 666 PRO ILE THR GLN MET TYR THR ASN VAL ASP GLN ASP LEU
SEQRES 10 B 666 VAL GLY TRP GLN ALA PRO PRO GLY ALA ARG SER LEU THR
SEQRES 11 B 666 PRO CYS THR CYS GLY SER SER ASP LEU TYR LEU VAL THR
SEQRES 12 B 666 ARG HIS ALA ASP VAL ILE PRO VAL ARG ARG ARG GLY ASP
SEQRES 13 B 666 SER ARG GLY SER LEU LEU SER PRO ARG PRO VAL SER TYR
SEQRES 14 B 666 LEU LYS GLY SER SER GLY GLY PRO LEU LEU CYS PRO SER
SEQRES 15 B 666 GLY HIS ALA VAL GLY ILE PHE ARG ALA ALA VAL CYS THR
SEQRES 16 B 666 ARG GLY VAL ALA LYS ALA VAL ASP PHE VAL PRO VAL GLU
SEQRES 17 B 666 SER MET GLU THR THR MET ARG SER PRO VAL PHE THR ASP
SEQRES 18 B 666 ASN SER SER PRO PRO ALA VAL PRO GLN SER PHE GLN VAL
SEQRES 19 B 666 ALA HIS LEU HIS ALA PRO THR GLY SER GLY LYS SER THR
SEQRES 20 B 666 LYS VAL PRO ALA ALA TYR ALA ALA GLN GLY TYR LYS VAL
SEQRES 21 B 666 LEU VAL LEU ASN PRO SER VAL ALA ALA THR LEU GLY PHE
SEQRES 22 B 666 GLY ALA TYR MET SER LYS ALA HIS GLY ILE ASP PRO ASN
SEQRES 23 B 666 ILE ARG THR GLY VAL ARG THR ILE THR THR GLY ALA PRO
SEQRES 24 B 666 VAL THR TYR SER THR TYR GLY LYS PHE LEU ALA ASP GLY
SEQRES 25 B 666 GLY CYS SER GLY GLY ALA TYR ASP ILE ILE ILE CYS ASP
SEQRES 26 B 666 GLU CYS HIS SER THR ASP SER THR THR ILE LEU GLY ILE
SEQRES 27 B 666 GLY THR VAL LEU ASP GLN ALA GLU THR ALA GLY ALA ARG
SEQRES 28 B 666 LEU VAL VAL LEU ALA THR ALA THR PRO PRO GLY SER VAL
SEQRES 29 B 666 THR VAL PRO HIS PRO ASN ILE GLU GLU VAL ALA LEU SER
SEQRES 30 B 666 ASN THR GLY GLU ILE PRO PHE TYR GLY LYS ALA ILE PRO
SEQRES 31 B 666 ILE GLU ALA ILE ARG GLY GLY ARG HIS LEU ILE PHE CYS
SEQRES 32 B 666 HIS SER LYS LYS LYS CYS ASP GLU LEU ALA ALA LYS LEU
SEQRES 33 B 666 SER GLY LEU GLY ILE ASN ALA VAL ALA TYR TYR ARG GLY
SEQRES 34 B 666 LEU ASP VAL SER VAL ILE PRO THR ILE GLY ASP VAL VAL
SEQRES 35 B 666 VAL VAL ALA THR ASP ALA LEU MET THR GLY TYR THR GLY
SEQRES 36 B 666 ASP PHE ASP SER VAL ILE ASP CYS ASN THR CYS VAL THR
SEQRES 37 B 666 GLN THR VAL ASP PHE SER LEU ASP PRO THR PHE THR ILE
SEQRES 38 B 666 GLU THR THR THR VAL PRO GLN ASP ALA VAL SER ARG SER
SEQRES 39 B 666 GLN ARG ARG GLY ARG THR GLY ARG GLY ARG ARG GLY ILE
SEQRES 40 B 666 TYR ARG PHE VAL THR PRO GLY GLU ARG PRO SER GLY MET
SEQRES 41 B 666 PHE ASP SER SER VAL LEU CYS GLU CYS TYR ASP ALA GLY
SEQRES 42 B 666 CYS ALA TRP TYR GLU LEU THR PRO ALA GLU THR SER VAL
SEQRES 43 B 666 ARG LEU ARG ALA TYR LEU ASN THR PRO GLY LEU PRO VAL
SEQRES 44 B 666 CYS GLN ASP HIS LEU GLU PHE TRP GLU SER VAL PHE THR
SEQRES 45 B 666 GLY LEU THR HIS ILE ASP ALA HIS PHE LEU SER GLN THR
SEQRES 46 B 666 LYS GLN ALA GLY ASP ASN PHE PRO TYR LEU VAL ALA TYR
SEQRES 47 B 666 GLN ALA THR VAL CYS ALA ARG ALA GLN ALA PRO PRO PRO
SEQRES 48 B 666 SER TRP ASP GLN MET TRP LYS CYS LEU ILE ARG LEU LYS
SEQRES 49 B 666 PRO THR LEU HIS GLY PRO THR PRO LEU LEU TYR ARG LEU
SEQRES 50 B 666 GLY ALA VAL GLN ASN GLU VAL THR LEU THR HIS PRO ILE
SEQRES 51 B 666 THR LYS TYR ILE MET ALA CYS MET SER ALA ASP LEU GLU
SEQRES 52 B 666 VAL VAL THR
HET MG A 850 1
HET ADP A 875 27
HET BEF A 885 4
HET SO4 A 895 5
HET MG B 850 1
HET ADP B 875 27
HET BEF B 885 4
HET SO4 B 895 5
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 3 MG 2(MG 2+)
FORMUL 4 ADP 2(C10 H15 N5 O10 P2)
FORMUL 5 BEF 2(BE F3 1-)
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 11 HOH *838(H2 O)
HELIX 1 1 GLY A 12 GLY A 23 1 12
HELIX 2 2 TYR A 56 GLY A 60 1 5
HELIX 3 3 VAL A 78 GLN A 80 5 3
HELIX 4 4 SER A 133 LEU A 135 5 3
HELIX 5 5 VAL A 172 ARG A 180 1 9
HELIX 6 6 THR A 212 GLN A 221 1 10
HELIX 7 7 SER A 231 GLY A 247 1 17
HELIX 8 8 TYR A 270 ASP A 276 1 7
HELIX 9 9 ASP A 296 ALA A 310 1 15
HELIX 10 10 PRO A 355 ILE A 359 5 5
HELIX 11 11 SER A 370 LEU A 384 1 15
HELIX 12 12 ASP A 396 ILE A 400 5 5
HELIX 13 13 ASP A 412 MET A 415 5 4
HELIX 14 14 ASP A 454 GLY A 463 1 10
HELIX 15 15 ASP A 487 TRP A 501 1 15
HELIX 16 16 THR A 505 ASN A 518 1 14
HELIX 17 17 HIS A 528 GLY A 538 1 11
HELIX 18 18 ASP A 543 GLY A 554 1 12
HELIX 19 19 PHE A 557 ALA A 571 1 15
HELIX 20 20 ASP A 579 LEU A 592 5 14
HELIX 21 21 HIS A 613 MET A 623 1 11
HELIX 22 22 GLY B 15 GLY B 23 1 9
HELIX 23 23 TYR B 56 GLY B 60 1 5
HELIX 24 24 VAL B 78 GLN B 80 5 3
HELIX 25 25 SER B 133 LYS B 136 5 4
HELIX 26 26 VAL B 172 ARG B 180 1 9
HELIX 27 27 THR B 212 GLN B 221 1 10
HELIX 28 28 SER B 231 GLY B 247 1 17
HELIX 29 29 TYR B 270 ASP B 276 1 7
HELIX 30 30 ASP B 296 ALA B 310 1 15
HELIX 31 31 PRO B 355 ILE B 359 5 5
HELIX 32 32 SER B 370 SER B 382 1 13
HELIX 33 33 ASP B 396 ILE B 400 5 5
HELIX 34 34 ASP B 412 MET B 415 5 4
HELIX 35 35 ASP B 454 GLY B 463 1 10
HELIX 36 36 ASP B 487 TRP B 501 1 15
HELIX 37 37 THR B 505 ASN B 518 1 14
HELIX 38 38 HIS B 528 GLY B 538 1 11
HELIX 39 39 ASP B 543 GLY B 554 1 12
HELIX 40 40 PHE B 557 ALA B 571 1 15
HELIX 41 41 ASP B 579 LEU B 592 5 14
HELIX 42 42 HIS B 613 MET B 623 1 11
SHEET 1 A 7 ALA A 5 GLN A 9 0
SHEET 2 A 7 VAL A -12 LEU A -5 -1 N ILE A -6 O TYR A 6
SHEET 3 A 7 VAL A 33 SER A 37 -1 O VAL A 35 N GLY A -9
SHEET 4 A 7 SER A 42 VAL A 48 -1 O PHE A 43 N VAL A 36
SHEET 5 A 7 VAL A 51 VAL A 55 -1 O VAL A 51 N VAL A 48
SHEET 6 A 7 LEU A 82 GLN A 86 -1 O TRP A 85 N CYS A 52
SHEET 7 A 7 TYR A 75 ASN A 77 -1 N ASN A 77 O LEU A 82
SHEET 1 B 8 LEU A 627 VAL A 630 0
SHEET 2 B 8 ALA A 150 THR A 160 -1 N ALA A 157 O VAL A 629
SHEET 3 B 8 VAL A 163 PRO A 171 -1 O ASP A 168 N ALA A 156
SHEET 4 B 8 ARG A 123 PRO A 131 -1 N GLY A 124 O VAL A 167
SHEET 5 B 8 VAL A 113 ARG A 118 -1 N ARG A 117 O SER A 125
SHEET 6 B 8 ASP A 103 VAL A 107 -1 N LEU A 104 O VAL A 116
SHEET 7 B 8 PRO A 142 LEU A 144 -1 O LEU A 144 N TYR A 105
SHEET 8 B 8 ALA A 150 THR A 160 -1 O VAL A 151 N LEU A 143
SHEET 1 C 7 GLN A 198 HIS A 203 0
SHEET 2 C 7 LEU A 317 THR A 322 1 O LEU A 320 N ALA A 200
SHEET 3 C 7 ILE A 286 CYS A 289 1 N CYS A 289 O VAL A 319
SHEET 4 C 7 VAL A 225 ASN A 229 1 N LEU A 226 O ILE A 288
SHEET 5 C 7 VAL A 265 THR A 269 1 O THR A 266 N VAL A 227
SHEET 6 C 7 ASN A 251 ARG A 253 1 N ASN A 251 O VAL A 265
SHEET 7 C 7 THR A 258 ILE A 259 -1 O ILE A 259 N ILE A 252
SHEET 1 D 6 ILE A 336 ALA A 340 0
SHEET 2 D 6 GLY A 471 PHE A 475 1 O TYR A 473 N GLU A 337
SHEET 3 D 6 SER A 424 ASP A 427 1 N ASP A 427 O ARG A 474
SHEET 4 D 6 ARG A 363 PHE A 367 1 N PHE A 367 O ILE A 426
SHEET 5 D 6 VAL A 406 ALA A 410 1 O VAL A 408 N ILE A 366
SHEET 6 D 6 ALA A 388 TYR A 391 1 N VAL A 389 O VAL A 409
SHEET 1 E 2 ILE A 347 PHE A 349 0
SHEET 2 E 2 LYS A 352 ILE A 354 -1 O LYS A 352 N PHE A 349
SHEET 1 F 2 THR A 430 ASP A 437 0
SHEET 2 F 2 THR A 445 PRO A 452 -1 O GLU A 447 N THR A 435
SHEET 1 G 2 THR A 596 PRO A 597 0
SHEET 2 G 2 VAL A 609 THR A 610 1 O THR A 610 N THR A 596
SHEET 1 H 7 ALA B 5 GLN B 9 0
SHEET 2 H 7 VAL B -12 LEU B -5 -1 N ILE B -6 O TYR B 6
SHEET 3 H 7 VAL B 33 SER B 37 -1 O VAL B 35 N VAL B -10
SHEET 4 H 7 SER B 42 VAL B 48 -1 O ALA B 45 N GLN B 34
SHEET 5 H 7 VAL B 51 VAL B 55 -1 O TRP B 53 N THR B 46
SHEET 6 H 7 LEU B 82 GLN B 86 -1 O TRP B 85 N CYS B 52
SHEET 7 H 7 TYR B 75 ASN B 77 -1 N ASN B 77 O LEU B 82
SHEET 1 I 8 LEU B 627 VAL B 630 0
SHEET 2 I 8 ALA B 150 THR B 160 -1 N ALA B 157 O VAL B 629
SHEET 3 I 8 VAL B 163 PRO B 171 -1 O ASP B 168 N ALA B 156
SHEET 4 I 8 ARG B 123 PRO B 131 -1 N GLY B 124 O VAL B 167
SHEET 5 I 8 VAL B 113 ARG B 118 -1 N ARG B 117 O SER B 125
SHEET 6 I 8 ASP B 103 VAL B 107 -1 N LEU B 104 O VAL B 116
SHEET 7 I 8 PRO B 142 LEU B 144 -1 O LEU B 144 N TYR B 105
SHEET 8 I 8 ALA B 150 THR B 160 -1 O VAL B 151 N LEU B 143
SHEET 1 J 7 GLN B 198 HIS B 203 0
SHEET 2 J 7 LEU B 317 THR B 322 1 O LEU B 320 N ALA B 200
SHEET 3 J 7 ILE B 286 CYS B 289 1 N CYS B 289 O VAL B 319
SHEET 4 J 7 VAL B 225 ASN B 229 1 N LEU B 226 O ILE B 288
SHEET 5 J 7 VAL B 265 THR B 269 1 O THR B 266 N VAL B 227
SHEET 6 J 7 ASN B 251 ARG B 253 1 N ARG B 253 O TYR B 267
SHEET 7 J 7 THR B 258 ILE B 259 -1 O ILE B 259 N ILE B 252
SHEET 1 K 6 ILE B 336 ALA B 340 0
SHEET 2 K 6 GLY B 471 PHE B 475 1 O TYR B 473 N GLU B 337
SHEET 3 K 6 SER B 424 ASP B 427 1 N VAL B 425 O ARG B 474
SHEET 4 K 6 ARG B 363 PHE B 367 1 N PHE B 367 O ILE B 426
SHEET 5 K 6 VAL B 406 ALA B 410 1 O VAL B 408 N HIS B 364
SHEET 6 K 6 ALA B 388 TYR B 391 1 N VAL B 389 O VAL B 409
SHEET 1 L 2 ILE B 347 PHE B 349 0
SHEET 2 L 2 LYS B 352 ILE B 354 -1 O ILE B 354 N ILE B 347
SHEET 1 M 2 THR B 430 ASP B 437 0
SHEET 2 M 2 THR B 445 PRO B 452 -1 O VAL B 451 N CYS B 431
SHEET 1 N 2 THR B 596 PRO B 597 0
SHEET 2 N 2 VAL B 609 THR B 610 1 O THR B 610 N THR B 596
SSBOND 1 CYS A 97 CYS A 145 1555 1555 2.71
SSBOND 2 CYS B 97 CYS B 145 1555 1555 2.05
LINK O HOH A 2 MG MG A 850 1555 1555 2.29
LINK OG SER A 211 MG MG A 850 1555 1555 2.21
LINK OE2 GLU A 291 MG MG A 850 1555 1555 2.31
LINK O HOH A 633 MG MG A 850 1555 1555 2.17
LINK MG MG A 850 O1B ADP A 875 1555 1555 2.03
LINK O3B ADP A 875 BE BEF A 885 1555 1555 1.70
LINK OG SER B 211 MG MG B 850 1555 1555 2.15
LINK OE2 GLU B 291 MG MG B 850 1555 1555 2.38
LINK O HOH B 637 MG MG B 850 1555 1555 2.31
LINK O HOH B 644 MG MG B 850 1555 1555 2.25
LINK MG MG B 850 O1B ADP B 875 1555 1555 2.14
LINK O3B ADP B 875 BE BEF B 885 1555 1555 1.70
CISPEP 1 ASP A 441 PRO A 442 0 7.61
CISPEP 2 ARG B 360 GLY B 361 0 -0.84
CISPEP 3 SER B 382 GLY B 383 0 -12.36
CISPEP 4 ASP B 441 PRO B 442 0 10.23
SITE 1 AC1 6 HOH A 2 SER A 211 GLU A 291 HOH A 633
SITE 2 AC1 6 ADP A 875 BEF A 885
SITE 1 AC2 16 GLY A 207 SER A 208 GLY A 209 LYS A 210
SITE 2 AC2 16 SER A 211 THR A 212 GLY A 237 TYR A 241
SITE 3 AC2 16 THR A 419 ARG A 467 GLY A 468 HOH A 633
SITE 4 AC2 16 HOH A 694 MG A 850 BEF A 885 HOH A 914
SITE 1 AC3 11 HOH A 1 THR A 206 LYS A 210 GLU A 291
SITE 2 AC3 11 ALA A 323 ARG A 464 ARG A 467 HOH A 633
SITE 3 AC3 11 HOH A 638 MG A 850 ADP A 875
SITE 1 AC4 6 VAL A 232 THR A 254 GLY A 255 THR A 269
SITE 2 AC4 6 HOH A 925 HOH A 980
SITE 1 AC5 6 SER B 211 GLU B 291 HOH B 637 HOH B 644
SITE 2 AC5 6 ADP B 875 BEF B 885
SITE 1 AC6 14 GLY B 207 SER B 208 GLY B 209 LYS B 210
SITE 2 AC6 14 SER B 211 THR B 212 TYR B 241 THR B 419
SITE 3 AC6 14 ARG B 467 GLY B 468 HOH B 644 HOH B 807
SITE 4 AC6 14 MG B 850 BEF B 885
SITE 1 AC7 11 THR B 206 LYS B 210 GLU B 291 ALA B 323
SITE 2 AC7 11 ARG B 464 ARG B 467 HOH B 632 HOH B 644
SITE 3 AC7 11 HOH B 662 MG B 850 ADP B 875
SITE 1 AC8 4 VAL B 232 GLY B 255 THR B 269 HOH B1043
CRYST1 89.749 110.416 144.374 90.00 90.00 90.00 P 21 21 21 8
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 0.011142 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009057 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
