HEADER TRANSFERASE/HYDROLASE 25-JUL-13 4LV5
TITLE MURINE IRGA6 BOUND TO TOXOPLASMA ROP5B, A PSEUDOKINASE GDI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHOPTRY PROTEIN 5B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 175-541;
COMPND 5 SYNONYM: TYPE I RHOPTRY PROTEIN 5, TYPE I RHOPTRY PROTEIN 5B, TYPE
COMPND 6 III RHOPTRY PROTEIN 5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERFERON-INDUCIBLE GTPASE 1;
COMPND 10 CHAIN: B;
COMPND 11 EC: 3.6.5.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII;
SOURCE 3 ORGANISM_TAXID: 5811;
SOURCE 4 STRAIN: RH;
SOURCE 5 GENE: ROP5, ROP5B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: IIGP1, IRGA6;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX4T
KEYWDS IMMUNE RELATED GTPASE, GUANINE DISSOCIATION INHIBITOR, PARASITE
KEYWDS 2 EFFECTOR, TRANSFERASE-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.REESE,J.C.BOOTHROYD
REVDAT 3 20-SEP-23 4LV5 1 REMARK SEQADV LINK
REVDAT 2 02-OCT-13 4LV5 1 REMARK
REVDAT 1 25-SEP-13 4LV5 0
JRNL AUTH M.L.REESE,N.SHAH,J.C.BOOTHROYD
JRNL TITL MURINE IRGA6 BOUND TO TOXOPLASMA ROP5B, A PSEUDOKINASE GDI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 92476
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 4650
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 39.3381 - 5.2782 0.99 2918 138 0.1731 0.1828
REMARK 3 2 5.2782 - 4.1910 1.00 2943 158 0.1464 0.1776
REMARK 3 3 4.1910 - 3.6617 0.98 2901 155 0.1587 0.1901
REMARK 3 4 3.6617 - 3.3271 1.00 2913 165 0.1730 0.1970
REMARK 3 5 3.3271 - 3.0887 1.00 2930 150 0.1868 0.2266
REMARK 3 6 3.0887 - 2.9066 1.00 2927 155 0.1905 0.2274
REMARK 3 7 2.9066 - 2.7611 1.00 2950 160 0.1970 0.2368
REMARK 3 8 2.7611 - 2.6410 0.98 2893 155 0.2004 0.2465
REMARK 3 9 2.6410 - 2.5393 0.99 2922 148 0.1993 0.2400
REMARK 3 10 2.5393 - 2.4517 1.00 2942 148 0.2037 0.2728
REMARK 3 11 2.4517 - 2.3750 1.00 2907 152 0.2007 0.2250
REMARK 3 12 2.3750 - 2.3072 1.00 2964 158 0.1974 0.2279
REMARK 3 13 2.3072 - 2.2464 1.00 2935 164 0.2030 0.2526
REMARK 3 14 2.2464 - 2.1916 1.00 2890 140 0.1991 0.2662
REMARK 3 15 2.1916 - 2.1418 1.00 3023 147 0.2020 0.2435
REMARK 3 16 2.1418 - 2.0962 1.00 2877 147 0.2129 0.2238
REMARK 3 17 2.0962 - 2.0543 0.99 2961 143 0.2263 0.2696
REMARK 3 18 2.0543 - 2.0155 1.00 2899 161 0.2292 0.3187
REMARK 3 19 2.0155 - 1.9795 1.00 2987 150 0.2370 0.2877
REMARK 3 20 1.9795 - 1.9460 1.00 2886 150 0.2450 0.3046
REMARK 3 21 1.9460 - 1.9146 1.00 2924 195 0.2476 0.3230
REMARK 3 22 1.9146 - 1.8851 1.00 2864 157 0.2672 0.3312
REMARK 3 23 1.8851 - 1.8574 1.00 3004 172 0.2671 0.3535
REMARK 3 24 1.8574 - 1.8313 1.00 2929 143 0.2813 0.2975
REMARK 3 25 1.8313 - 1.8065 1.00 2947 140 0.2872 0.3036
REMARK 3 26 1.8065 - 1.7830 1.00 2965 142 0.2954 0.3290
REMARK 3 27 1.7830 - 1.7608 0.99 2895 167 0.3214 0.3552
REMARK 3 28 1.7608 - 1.7395 0.99 2928 167 0.3319 0.3483
REMARK 3 29 1.7395 - 1.7193 0.99 2889 163 0.3405 0.3839
REMARK 3 30 1.7193 - 1.7000 0.99 2913 160 0.3671 0.4078
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.830
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.03
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 6307
REMARK 3 ANGLE : 1.106 8554
REMARK 3 CHIRALITY : 0.078 963
REMARK 3 PLANARITY : 0.005 1092
REMARK 3 DIHEDRAL : 14.425 2385
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 4LV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081125.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92554
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 39.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.01800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.150
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: 3Q60 AND THEN 1TPZ:A USING PHASER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M AMMONIUM CITRATE,
REMARK 280 PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 350
REMARK 350 BIOMOLECULE: 2
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 171
REMARK 465 SER A 172
REMARK 465 HIS A 173
REMARK 465 MET A 174
REMARK 465 ARG A 288
REMARK 465 LEU A 289
REMARK 465 LEU A 290
REMARK 465 GLY A 291
REMARK 465 GLU A 292
REMARK 465 SER A 293
REMARK 465 PRO A 294
REMARK 465 GLU A 295
REMARK 465 GLU A 296
REMARK 465 ALA A 297
REMARK 465 ARG A 298
REMARK 465 ASP A 299
REMARK 465 ARG A 300
REMARK 465 ARG A 301
REMARK 465 THR A 539
REMARK 465 GLY A 540
REMARK 465 GLN A 541
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 PRO B -7
REMARK 465 GLY B -6
REMARK 465 ILE B -5
REMARK 465 PRO B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 THR B -1
REMARK 465 THR B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLN B 3
REMARK 465 LEU B 4
REMARK 465 PHE B 5
REMARK 465 SER B 6
REMARK 465 SER B 7
REMARK 465 PRO B 8
REMARK 465 LYS B 9
REMARK 465 SER B 10
REMARK 465 ASP B 11
REMARK 465 GLU B 12
REMARK 465 ASN B 13
REMARK 465 THR B 354
REMARK 465 ASP B 355
REMARK 465 ARG B 412
REMARK 465 ASN B 413
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 O HOH A 828 O HOH A 843 1.84
REMARK 500 O HOH B 828 O HOH B 842 1.86
REMARK 500 OD1 ASN B 28 O HOH B 850 1.87
REMARK 500 O HOH B 826 O HOH B 834 1.87
REMARK 500 O HOH A 890 O HOH A 902 1.88
REMARK 500 O HOH B 829 O HOH B 832 1.90
REMARK 500 O2B ADP A 601 O HOH A 895 1.90
REMARK 500 O1 EDO B 503 O HOH B 796 1.91
REMARK 500 OE1 GLN A 528 O HOH A 879 1.95
REMARK 500 OE2 GLU B 95 O HOH B 741 1.97
REMARK 500 OE1 GLU B 148 O HOH B 759 1.98
REMARK 500 O HOH A 884 O HOH A 889 2.02
REMARK 500 O1B ADP A 601 O HOH A 868 2.02
REMARK 500 O HOH B 835 O HOH B 836 2.03
REMARK 500 O HOH A 901 O HOH A 910 2.04
REMARK 500 O HOH A 927 O HOH A 933 2.06
REMARK 500 O HOH A 885 O HOH A 893 2.06
REMARK 500 O HOH B 810 O HOH B 815 2.08
REMARK 500 O HOH B 785 O HOH B 790 2.08
REMARK 500 O HOH B 787 O HOH B 788 2.08
REMARK 500 O HOH B 724 O HOH B 726 2.10
REMARK 500 O HOH A 776 O HOH A 798 2.10
REMARK 500 OE2 GLU A 255 O HOH A 931 2.14
REMARK 500 O HOH A 908 O HOH A 916 2.14
REMARK 500 O HOH A 894 O HOH A 904 2.14
REMARK 500 OH TYR B 114 O HOH B 755 2.15
REMARK 500 OE1 GLU A 275 O HOH A 932 2.15
REMARK 500 ND2 ASN B 138 O HOH B 628 2.16
REMARK 500 O HOH B 750 O HOH B 810 2.16
REMARK 500 O HOH B 762 O HOH B 799 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 GLN A 217 -99.76 -95.67
REMARK 500 ASN A 218 -144.72 -118.39
REMARK 500 LEU A 227 -139.12 -106.35
REMARK 500 PHE A 318 -37.59 78.18
REMARK 500 ASP A 407 72.94 55.97
REMARK 500 ASP A 407 72.64 55.97
REMARK 500 LEU A 459 -48.57 70.26
REMARK 500 PRO A 494 89.04 -62.70
REMARK 500 LEU A 507 33.81 -94.17
REMARK 500 ASN B 134 40.05 -106.32
REMARK 500 THR B 158 -52.73 65.96
REMARK 500 TYR B 238 -151.49 65.88
REMARK 500 ASP B 290 126.81 85.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LV8 RELATED DB: PDB
DBREF 4LV5 A 175 541 UNP F2YGR7 F2YGR7_TOXGO 175 541
DBREF 4LV5 B 1 413 UNP Q9QZ85 IIGP1_MOUSE 1 413
SEQADV 4LV5 GLY A 171 UNP F2YGR7 EXPRESSION TAG
SEQADV 4LV5 SER A 172 UNP F2YGR7 EXPRESSION TAG
SEQADV 4LV5 HIS A 173 UNP F2YGR7 EXPRESSION TAG
SEQADV 4LV5 MET A 174 UNP F2YGR7 EXPRESSION TAG
SEQADV 4LV5 GLY B -9 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 SER B -8 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 PRO B -7 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 GLY B -6 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 ILE B -5 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 PRO B -4 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 GLY B -3 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 SER B -2 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 THR B -1 UNP Q9QZ85 EXPRESSION TAG
SEQADV 4LV5 THR B 0 UNP Q9QZ85 EXPRESSION TAG
SEQRES 1 A 371 GLY SER HIS MET GLU ALA GLY ASP SER PHE MET ARG ASP
SEQRES 2 A 371 LEU LEU LYS ARG GLU GLU GLU LEU ILE GLY TYR CYS ARG
SEQRES 3 A 371 GLU GLU ALA LEU LYS GLU PRO ALA ALA MET VAL GLU ALA
SEQRES 4 A 371 VAL THR ALA THR VAL TRP PRO GLN ASN ALA GLU THR THR
SEQRES 5 A 371 VAL ASP SER LEU LEU SER GLN GLY GLU ARG LYS LEU LYS
SEQRES 6 A 371 LEU VAL GLU PRO LEU ARG VAL GLY ASP ARG SER VAL VAL
SEQRES 7 A 371 PHE LEU VAL ARG ASP VAL GLU ARG LEU GLU ASP PHE ALA
SEQRES 8 A 371 LEU LYS VAL PHE THR MET GLY ALA GLU ASN SER ARG SER
SEQRES 9 A 371 GLU LEU GLU ARG LEU HIS GLU ALA THR PHE ALA ALA ALA
SEQRES 10 A 371 ARG LEU LEU GLY GLU SER PRO GLU GLU ALA ARG ASP ARG
SEQRES 11 A 371 ARG ARG LEU LEU LEU PRO SER ASP ALA VAL ALA VAL GLN
SEQRES 12 A 371 SER GLN PRO PRO PHE ALA GLN LEU SER PRO GLY GLN ASP
SEQRES 13 A 371 ASP TYR ALA VAL ALA ASN TYR LEU LEU LEU MET PRO ALA
SEQRES 14 A 371 ALA SER VAL ASP LEU GLU LEU LEU PHE SER THR LEU ASP
SEQRES 15 A 371 PHE VAL TYR VAL PHE ARG GLY ASP GLU GLY ILE LEU ALA
SEQRES 16 A 371 LEU HIS ILE LEU THR ALA GLN LEU ILE ARG LEU ALA ALA
SEQRES 17 A 371 ASN LEU GLN SER LYS GLY LEU VAL HIS GLY HIS PHE THR
SEQRES 18 A 371 PRO ASP ASN LEU PHE ILE MET PRO ASP GLY ARG LEU MET
SEQRES 19 A 371 LEU GLY ASP VAL SER ALA LEU TRP LYS VAL GLY THR ARG
SEQRES 20 A 371 GLY PRO ALA SER SER VAL PRO VAL THR TYR ALA PRO ARG
SEQRES 21 A 371 GLU PHE LEU ASN ALA SER THR ALA THR PHE THR HIS ALA
SEQRES 22 A 371 LEU ASN ALA TRP GLN LEU GLY LEU SER ILE TYR ARG VAL
SEQRES 23 A 371 TRP CYS LEU PHE LEU PRO PHE GLY LEU VAL THR PRO GLY
SEQRES 24 A 371 ILE LYS GLY SER TRP LYS ARG PRO SER LEU ARG VAL PRO
SEQRES 25 A 371 GLY THR ASP SER LEU ALA PHE GLY SER CYS THR PRO LEU
SEQRES 26 A 371 PRO ASP PHE VAL LYS THR LEU ILE GLY ARG PHE LEU ASN
SEQRES 27 A 371 PHE ASP ARG ARG ARG ARG LEU LEU PRO LEU GLU ALA MET
SEQRES 28 A 371 GLU THR PRO GLU PHE LEU GLN LEU GLN ASN GLU ILE SER
SEQRES 29 A 371 SER SER LEU SER THR GLY GLN
SEQRES 1 B 423 GLY SER PRO GLY ILE PRO GLY SER THR THR MET GLY GLN
SEQRES 2 B 423 LEU PHE SER SER PRO LYS SER ASP GLU ASN ASN ASP LEU
SEQRES 3 B 423 PRO SER SER PHE THR GLY TYR PHE LYS LYS PHE ASN THR
SEQRES 4 B 423 GLY ARG LYS ILE ILE SER GLN GLU ILE LEU ASN LEU ILE
SEQRES 5 B 423 GLU LEU ARG MET ARG LYS GLY ASN ILE GLN LEU THR ASN
SEQRES 6 B 423 SER ALA ILE SER ASP ALA LEU LYS GLU ILE ASP SER SER
SEQRES 7 B 423 VAL LEU ASN VAL ALA VAL THR GLY GLU THR GLY SER GLY
SEQRES 8 B 423 LYS SER SER PHE ILE ASN THR LEU ARG GLY ILE GLY ASN
SEQRES 9 B 423 GLU GLU GLU GLY ALA ALA LYS THR GLY VAL VAL GLU VAL
SEQRES 10 B 423 THR MET GLU ARG HIS PRO TYR LYS HIS PRO ASN ILE PRO
SEQRES 11 B 423 ASN VAL VAL PHE TRP ASP LEU PRO GLY ILE GLY SER THR
SEQRES 12 B 423 ASN PHE PRO PRO ASN THR TYR LEU GLU LYS MET LYS PHE
SEQRES 13 B 423 TYR GLU TYR ASP PHE PHE ILE ILE ILE SER ALA THR ARG
SEQRES 14 B 423 PHE LYS LYS ASN ASP ILE ASP ILE ALA LYS ALA ILE SER
SEQRES 15 B 423 MET MET LYS LYS GLU PHE TYR PHE VAL ARG THR LYS VAL
SEQRES 16 B 423 ASP SER ASP ILE THR ASN GLU ALA ASP GLY LYS PRO GLN
SEQRES 17 B 423 THR PHE ASP LYS GLU LYS VAL LEU GLN ASP ILE ARG LEU
SEQRES 18 B 423 ASN CYS VAL ASN THR PHE ARG GLU ASN GLY ILE ALA GLU
SEQRES 19 B 423 PRO PRO ILE PHE LEU LEU SER ASN LYS ASN VAL CYS HIS
SEQRES 20 B 423 TYR ASP PHE PRO VAL LEU MET ASP LYS LEU ILE SER ASP
SEQRES 21 B 423 LEU PRO ILE TYR LYS ARG HIS ASN PHE MET VAL SER LEU
SEQRES 22 B 423 PRO ASN ILE THR ASP SER VAL ILE GLU LYS LYS ARG GLN
SEQRES 23 B 423 PHE LEU LYS GLN ARG ILE TRP LEU GLU GLY PHE ALA ALA
SEQRES 24 B 423 ASP LEU VAL ASN ILE ILE PRO SER LEU THR PHE LEU LEU
SEQRES 25 B 423 ASP SER ASP LEU GLU THR LEU LYS LYS SER MET LYS PHE
SEQRES 26 B 423 TYR ARG THR VAL PHE GLY VAL ASP GLU THR SER LEU GLN
SEQRES 27 B 423 ARG LEU ALA ARG ASP TRP GLU ILE GLU VAL ASP GLN VAL
SEQRES 28 B 423 GLU ALA MET ILE LYS SER PRO ALA VAL PHE LYS PRO THR
SEQRES 29 B 423 ASP GLU GLU THR ILE GLN GLU ARG LEU SER ARG TYR ILE
SEQRES 30 B 423 GLN GLU PHE CYS LEU ALA ASN GLY TYR LEU LEU PRO LYS
SEQRES 31 B 423 ASN SER PHE LEU LYS GLU ILE PHE TYR LEU LYS TYR TYR
SEQRES 32 B 423 PHE LEU ASP MET VAL THR GLU ASP ALA LYS THR LEU LEU
SEQRES 33 B 423 LYS GLU ILE CYS LEU ARG ASN
HET ADP A 601 27
HET BME A 602 4
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET GDP B 501 28
HET EDO B 502 4
HET EDO B 503 4
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM BME BETA-MERCAPTOETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 BME C2 H6 O S
FORMUL 5 EDO 6(C2 H6 O2)
FORMUL 9 GDP C10 H15 N5 O11 P2
FORMUL 12 HOH *483(H2 O)
HELIX 1 1 GLU A 175 GLU A 188 1 14
HELIX 2 2 GLU A 188 GLU A 202 1 15
HELIX 3 3 PRO A 203 TRP A 215 1 13
HELIX 4 4 ASN A 271 ALA A 287 1 17
HELIX 5 5 LEU A 344 VAL A 354 1 11
HELIX 6 6 ARG A 358 LYS A 383 1 26
HELIX 7 7 THR A 391 ASP A 393 5 3
HELIX 8 8 ASP A 407 SER A 409 5 3
HELIX 9 9 SER A 421 VAL A 423 5 3
HELIX 10 10 PRO A 424 ALA A 428 5 5
HELIX 11 11 PRO A 429 LEU A 433 5 5
HELIX 12 12 THR A 441 LEU A 459 1 19
HELIX 13 13 PRO A 496 LEU A 507 1 12
HELIX 14 14 LEU A 516 GLU A 522 1 7
HELIX 15 15 THR A 523 SER A 538 1 16
HELIX 16 16 ASP B 15 LYS B 26 1 12
HELIX 17 17 SER B 35 LYS B 48 1 14
HELIX 18 18 ASN B 50 SER B 67 1 18
HELIX 19 19 GLY B 81 GLY B 91 1 11
HELIX 20 20 GLY B 103 MET B 109 1 7
HELIX 21 21 GLY B 129 THR B 133 5 5
HELIX 22 22 PRO B 136 MET B 144 1 9
HELIX 23 23 LYS B 145 TYR B 149 5 5
HELIX 24 24 LYS B 161 MET B 174 1 14
HELIX 25 25 LYS B 184 LYS B 196 1 13
HELIX 26 26 ASP B 201 ASN B 220 1 20
HELIX 27 27 ASP B 239 ASP B 250 1 12
HELIX 28 28 LEU B 251 TYR B 254 5 4
HELIX 29 29 LYS B 255 LEU B 263 1 9
HELIX 30 30 THR B 267 ALA B 289 1 23
HELIX 31 31 ILE B 295 THR B 299 5 5
HELIX 32 32 LEU B 302 PHE B 320 1 19
HELIX 33 33 ASP B 323 TRP B 334 1 12
HELIX 34 34 GLU B 337 ALA B 343 1 7
HELIX 35 35 MET B 344 ILE B 345 5 2
HELIX 36 36 LYS B 346 VAL B 350 5 5
HELIX 37 37 THR B 358 GLY B 375 1 18
HELIX 38 38 LYS B 385 CYS B 410 1 26
SHEET 1 A 7 GLU A 220 SER A 225 0
SHEET 2 A 7 GLU A 231 GLY A 243 -1 O ARG A 232 N VAL A 223
SHEET 3 A 7 SER A 246 ASP A 253 -1 O LEU A 250 N GLU A 238
SHEET 4 A 7 GLU A 258 THR A 266 -1 O PHE A 260 N VAL A 251
SHEET 5 A 7 VAL A 330 MET A 337 -1 O MET A 337 N ALA A 261
SHEET 6 A 7 ASP A 308 VAL A 312 -1 N VAL A 310 O LEU A 334
SHEET 7 A 7 GLU A 220 SER A 225 -1 N ASP A 224 O ALA A 311
SHEET 1 B 3 VAL A 342 ASP A 343 0
SHEET 2 B 3 LEU A 395 ILE A 397 -1 O ILE A 397 N VAL A 342
SHEET 3 B 3 LEU A 403 LEU A 405 -1 O MET A 404 N PHE A 396
SHEET 1 C 2 LEU A 385 HIS A 387 0
SHEET 2 C 2 LEU A 411 LYS A 413 -1 O TRP A 412 N VAL A 386
SHEET 1 D 2 ARG A 417 PRO A 419 0
SHEET 2 D 2 THR A 437 THR A 439 -1 O ALA A 438 N GLY A 418
SHEET 1 E 6 HIS B 112 LYS B 115 0
SHEET 2 E 6 VAL B 122 ASP B 126 -1 O PHE B 124 N TYR B 114
SHEET 3 E 6 LEU B 70 THR B 75 1 N VAL B 72 O TRP B 125
SHEET 4 E 6 PHE B 151 ALA B 157 1 O ILE B 155 N THR B 75
SHEET 5 E 6 TYR B 179 THR B 183 1 O TYR B 179 N ILE B 154
SHEET 6 E 6 ILE B 227 LEU B 229 1 O PHE B 228 N ARG B 182
SSBOND 1 CYS A 458 CYS A 492 1555 1555 2.05
SSBOND 2 CYS B 236 CYS B 410 1555 1555 2.03
LINK SG CYS A 195 S2 BME A 602 1555 1555 2.60
CISPEP 1 SER A 322 PRO A 323 0 1.96
SITE 1 AC1 21 ARG A 241 GLY A 243 ASP A 244 SER A 246
SITE 2 AC1 21 VAL A 248 ALA A 261 LYS A 263 LEU A 304
SITE 3 AC1 21 MET A 337 PRO A 338 ALA A 340 ASP A 343
SITE 4 AC1 21 ASP A 393 PHE A 396 HOH A 714 HOH A 732
SITE 5 AC1 21 HOH A 773 HOH A 837 HOH A 854 HOH A 868
SITE 6 AC1 21 HOH A 895
SITE 1 AC2 4 CYS A 195 ALA A 199 SER A 349 HOH A 887
SITE 1 AC3 5 LEU A 304 PRO A 306 ASP A 407 VAL A 408
SITE 2 AC3 5 HOH A 714
SITE 1 AC4 8 ASN A 218 ALA A 219 ALA A 443 ARG A 511
SITE 2 AC4 8 ARG A 512 ARG A 513 ARG A 514 HOH A 850
SITE 1 AC5 7 TYR A 454 PHE A 460 LEU A 461 PRO A 462
SITE 2 AC5 7 PHE A 463 GLY A 464 HOH A 704
SITE 1 AC6 4 LYS A 263 LEU A 279 LEU A 335 HOH A 854
SITE 1 AC7 16 GLY B 79 SER B 80 GLY B 81 LYS B 82
SITE 2 AC7 16 SER B 83 SER B 84 THR B 102 LYS B 184
SITE 3 AC7 16 ASP B 186 SER B 187 SER B 231 ASN B 232
SITE 4 AC7 16 LYS B 233 HOH B 700 HOH B 709 HOH B 822
SITE 1 AC8 3 TYR B 23 LYS B 279 HOH B 833
SITE 1 AC9 4 GLU A 277 PHE A 318 ILE B 294 HOH B 796
CRYST1 52.600 54.700 85.600 99.00 106.60 106.90 P 1 1
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 0.019011 0.005776 0.007434 0.00000
SCALE2 0.000000 0.019107 0.005170 0.00000
SCALE3 0.000000 0.000000 0.012629 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
