HEADER HYDROLASE/STRUCTURAL PROTEIN 17-SEP-14 4V0N
TITLE CRYSTAL STRUCTURE OF BBS1N IN COMPLEX WITH ARL6DN, SOAKED WITH MERCURY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARF-LIKE SMALL GTPASE;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: GTPASE, RESIDUES 16-180;
COMPND 5 SYNONYM: ARL6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BARDET-BIEDL SYNDROME 1 PROTEIN;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: WD40, RESIDUES 1-425;
COMPND 11 SYNONYM: BBS1;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 3 ORGANISM_TAXID: 3055;
SOURCE 4 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 10 ORGANISM_TAXID: 3055;
SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 12 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE
KEYWDS HYDROLASE-STRUCTURAL PROTEIN COMPLEX, BBSOME, GTP, COAT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MOURAO,E.LORENTZEN
REVDAT 4 03-APR-19 4V0N 1 SOURCE
REVDAT 3 17-DEC-14 4V0N 1 JRNL
REVDAT 2 26-NOV-14 4V0N 1 JRNL
REVDAT 1 19-NOV-14 4V0N 0
JRNL AUTH A.MOURAO,A.R.NAGER,M.V.NACHURY,E.LORENTZEN
JRNL TITL STRUCTURAL BASIS FOR MEMBRANE TARGETING OF THE BBSOME BY
JRNL TITL 2 ARL6
JRNL REF NAT.STRUCT.MOL.BIOL. V. 21 1035 2014
JRNL REFN ISSN 1545-9993
JRNL PMID 25402481
JRNL DOI 10.1038/NSMB.2920
REMARK 2
REMARK 2 RESOLUTION. 3.13 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) : 3.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.880
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 70096
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6643
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 96.5437 - 9.7263 0.99 4220 223 0.2176 0.2514
REMARK 3 2 9.7263 - 7.7211 1.00 4217 225 0.1891 0.1876
REMARK 3 3 7.7211 - 6.7454 1.00 4267 219 0.2106 0.2332
REMARK 3 4 6.7454 - 6.1287 1.00 4232 217 0.1936 0.2520
REMARK 3 5 6.1287 - 5.6895 1.00 4246 224 0.1892 0.2407
REMARK 3 6 5.6895 - 5.3541 1.00 4222 222 0.1850 0.2117
REMARK 3 7 5.3541 - 5.0860 1.00 4272 221 0.1803 0.2147
REMARK 3 8 5.0860 - 4.8646 1.00 4243 224 0.1884 0.2304
REMARK 3 9 4.8646 - 4.6773 1.00 4219 224 0.1860 0.2412
REMARK 3 10 4.6773 - 4.5159 1.00 4280 219 0.1733 0.2140
REMARK 3 11 4.5159 - 4.3747 1.00 4189 223 0.1818 0.2399
REMARK 3 12 4.3747 - 4.2497 1.00 4207 223 0.1959 0.2301
REMARK 3 13 4.2497 - 4.1378 1.00 4213 224 0.1962 0.2491
REMARK 3 14 4.1378 - 4.0368 1.00 4302 224 0.2052 0.2554
REMARK 3 15 4.0368 - 3.9451 1.00 4245 227 0.2108 0.2749
REMARK 3 16 3.9451 - 3.8611 1.00 4165 222 0.2211 0.2550
REMARK 3 17 3.8611 - 3.7839 1.00 4284 232 0.2266 0.2997
REMARK 3 18 3.7839 - 3.7125 1.00 4247 231 0.2351 0.2610
REMARK 3 19 3.7125 - 3.6462 1.00 4196 216 0.2344 0.2820
REMARK 3 20 3.6462 - 3.5844 1.00 4295 228 0.2359 0.2596
REMARK 3 21 3.5844 - 3.5265 1.00 4169 222 0.2412 0.3117
REMARK 3 22 3.5265 - 3.4723 1.00 4309 230 0.2500 0.2593
REMARK 3 23 3.4723 - 3.4212 1.00 4201 225 0.2631 0.2884
REMARK 3 24 3.4212 - 3.3730 1.00 4205 215 0.2754 0.3474
REMARK 3 25 3.3730 - 3.3274 1.00 4282 230 0.2998 0.3127
REMARK 3 26 3.3274 - 3.2842 1.00 4227 226 0.3124 0.3174
REMARK 3 27 3.2842 - 3.2432 1.00 4118 221 0.3333 0.3485
REMARK 3 28 3.2432 - 3.2041 1.00 4303 220 0.3403 0.3918
REMARK 3 29 3.2041 - 3.1668 1.00 4262 224 0.3542 0.3788
REMARK 3 30 3.1668 - 3.1312 0.73 3105 162 0.4107 0.4022
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 104.0
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 : 0.011 14775
REMARK 3 ANGLE : 1.476 20201
REMARK 3 CHIRALITY : 0.084 2394
REMARK 3 PLANARITY : 0.008 2555
REMARK 3 DIHEDRAL : 16.976 5234
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 4V0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1290061732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2MF
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70112
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.130
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 11.30
REMARK 200 R MERGE FOR SHELL (I) : 0.79000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% PEG400, 0.1M TRIS PH 8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.90300
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 295.80600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 295.80600
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 147.90300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.1 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 350
REMARK 350 BIOMOLECULE: 4
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: 3300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -194.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 HIS B 3
REMARK 465 GLU B 4
REMARK 465 SER B 5
REMARK 465 ASN B 6
REMARK 465 PRO B 7
REMARK 465 ASN B 8
REMARK 465 ASP B 9
REMARK 465 TYR B 10
REMARK 465 ALA B 11
REMARK 465 ALA B 12
REMARK 465 GLY B 13
REMARK 465 ASP B 14
REMARK 465 ALA B 15
REMARK 465 GLY B 16
REMARK 465 ASN B 17
REMARK 465 ALA B 18
REMARK 465 SER B 19
REMARK 465 GLY B 20
REMARK 465 ARG B 21
REMARK 465 TYR B 22
REMARK 465 THR B 23
REMARK 465 THR B 24
REMARK 465 GLY B 25
REMARK 465 SER B 26
REMARK 465 ASN B 27
REMARK 465 GLY B 28
REMARK 465 ILE B 29
REMARK 465 PRO B 30
REMARK 465 PRO B 31
REMARK 465 MET B 32
REMARK 465 LEU B 33
REMARK 465 PRO B 34
REMARK 465 SER B 35
REMARK 465 ASP B 149
REMARK 465 ILE B 150
REMARK 465 TRP B 151
REMARK 465 GLN B 152
REMARK 465 LYS B 153
REMARK 465 VAL B 154
REMARK 465 MET B 155
REMARK 465 GLU B 156
REMARK 465 GLY B 157
REMARK 465 GLU B 158
REMARK 465 ILE B 159
REMARK 465 VAL B 160
REMARK 465 ILE B 161
REMARK 465 GLY B 162
REMARK 465 GLU B 163
REMARK 465 ALA B 164
REMARK 465 VAL B 165
REMARK 465 ALA B 166
REMARK 465 GLN B 167
REMARK 465 LEU B 168
REMARK 465 THR B 169
REMARK 465 ARG B 170
REMARK 465 LEU B 171
REMARK 465 GLN B 172
REMARK 465 VAL B 173
REMARK 465 ARG B 174
REMARK 465 ALA B 175
REMARK 465 GLY B 176
REMARK 465 ASP B 177
REMARK 465 ALA B 178
REMARK 465 GLY B 179
REMARK 465 VAL B 180
REMARK 465 VAL B 181
REMARK 465 LEU B 182
REMARK 465 GLN B 183
REMARK 465 THR B 184
REMARK 465 ARG B 185
REMARK 465 SER B 186
REMARK 465 LEU B 187
REMARK 465 GLN B 188
REMARK 465 LEU B 189
REMARK 465 MET B 190
REMARK 465 ASN B 191
REMARK 465 ILE B 192
REMARK 465 GLY B 193
REMARK 465 ASP B 194
REMARK 465 PRO B 195
REMARK 465 ASP B 196
REMARK 465 ALA B 197
REMARK 465 LYS B 198
REMARK 465 MET B 199
REMARK 465 ALA B 200
REMARK 465 PHE B 201
REMARK 465 VAL B 202
REMARK 465 GLU B 203
REMARK 465 HIS B 204
REMARK 465 TRP B 205
REMARK 465 GLN B 206
REMARK 465 GLY B 207
REMARK 465 GLN B 208
REMARK 465 GLY C 12
REMARK 465 ALA C 13
REMARK 465 ALA C 14
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 HIS D 3
REMARK 465 GLU D 4
REMARK 465 SER D 5
REMARK 465 ASN D 6
REMARK 465 PRO D 7
REMARK 465 ASN D 8
REMARK 465 ASP D 9
REMARK 465 TYR D 10
REMARK 465 ALA D 11
REMARK 465 ALA D 12
REMARK 465 GLY D 13
REMARK 465 ASP D 14
REMARK 465 ALA D 15
REMARK 465 GLY D 16
REMARK 465 ASN D 17
REMARK 465 ALA D 18
REMARK 465 SER D 19
REMARK 465 GLY D 20
REMARK 465 ARG D 21
REMARK 465 TYR D 22
REMARK 465 THR D 23
REMARK 465 THR D 24
REMARK 465 GLY D 25
REMARK 465 SER D 26
REMARK 465 ASN D 27
REMARK 465 GLY D 28
REMARK 465 ILE D 29
REMARK 465 PRO D 30
REMARK 465 PRO D 31
REMARK 465 MET D 32
REMARK 465 LEU D 33
REMARK 465 PRO D 34
REMARK 465 SER D 35
REMARK 465 SER D 106
REMARK 465 GLU D 107
REMARK 465 ASN D 108
REMARK 465 THR D 109
REMARK 465 ALA D 110
REMARK 465 PRO D 111
REMARK 465 ARG D 112
REMARK 465 ASN D 142
REMARK 465 VAL D 143
REMARK 465 ASN D 144
REMARK 465 THR D 145
REMARK 465 GLU D 146
REMARK 465 GLU D 147
REMARK 465 GLN D 148
REMARK 465 ASP D 149
REMARK 465 ILE D 150
REMARK 465 TRP D 151
REMARK 465 GLN D 152
REMARK 465 LYS D 153
REMARK 465 VAL D 154
REMARK 465 MET D 155
REMARK 465 GLU D 156
REMARK 465 GLY D 157
REMARK 465 GLU D 158
REMARK 465 ILE D 159
REMARK 465 VAL D 160
REMARK 465 ILE D 161
REMARK 465 GLY D 162
REMARK 465 GLU D 163
REMARK 465 ALA D 164
REMARK 465 VAL D 165
REMARK 465 ALA D 166
REMARK 465 GLN D 167
REMARK 465 LEU D 168
REMARK 465 THR D 169
REMARK 465 ARG D 170
REMARK 465 LEU D 171
REMARK 465 GLN D 172
REMARK 465 VAL D 173
REMARK 465 ARG D 174
REMARK 465 ALA D 175
REMARK 465 GLY D 176
REMARK 465 ASP D 177
REMARK 465 ALA D 178
REMARK 465 GLY D 179
REMARK 465 VAL D 180
REMARK 465 VAL D 181
REMARK 465 LEU D 182
REMARK 465 GLN D 183
REMARK 465 THR D 184
REMARK 465 ARG D 185
REMARK 465 SER D 186
REMARK 465 LEU D 187
REMARK 465 GLN D 188
REMARK 465 LEU D 189
REMARK 465 MET D 190
REMARK 465 ASN D 191
REMARK 465 ILE D 192
REMARK 465 GLY D 193
REMARK 465 ASP D 194
REMARK 465 PRO D 195
REMARK 465 ASP D 196
REMARK 465 ALA D 197
REMARK 465 LYS D 198
REMARK 465 MET D 199
REMARK 465 ALA D 200
REMARK 465 PHE D 201
REMARK 465 VAL D 202
REMARK 465 GLU D 203
REMARK 465 HIS D 204
REMARK 465 TRP D 205
REMARK 465 GLN D 206
REMARK 465 GLY D 207
REMARK 465 GLN D 208
REMARK 465 PRO D 209
REMARK 465 LEU D 210
REMARK 465 VAL D 211
REMARK 465 ALA D 212
REMARK 465 THR D 213
REMARK 465 ASP D 227
REMARK 465 GLU D 228
REMARK 465 PRO D 229
REMARK 465 ASP D 230
REMARK 465 ALA D 231
REMARK 465 GLY D 251
REMARK 465 THR D 252
REMARK 465 GLY E 12
REMARK 465 ALA E 13
REMARK 465 ALA E 14
REMARK 465 MET F 1
REMARK 465 VAL F 2
REMARK 465 HIS F 3
REMARK 465 GLU F 4
REMARK 465 SER F 5
REMARK 465 ASN F 6
REMARK 465 PRO F 7
REMARK 465 ASN F 8
REMARK 465 ASP F 9
REMARK 465 TYR F 10
REMARK 465 ALA F 11
REMARK 465 ALA F 12
REMARK 465 GLY F 13
REMARK 465 ASP F 14
REMARK 465 ALA F 15
REMARK 465 GLY F 16
REMARK 465 ASN F 17
REMARK 465 ALA F 18
REMARK 465 SER F 19
REMARK 465 GLY F 20
REMARK 465 ARG F 21
REMARK 465 TYR F 22
REMARK 465 THR F 23
REMARK 465 THR F 24
REMARK 465 GLY F 25
REMARK 465 SER F 26
REMARK 465 ASN F 27
REMARK 465 GLY F 28
REMARK 465 ILE F 29
REMARK 465 PRO F 30
REMARK 465 PRO F 31
REMARK 465 MET F 32
REMARK 465 LEU F 33
REMARK 465 PRO F 34
REMARK 465 SER F 35
REMARK 465 ILE F 105
REMARK 465 SER F 106
REMARK 465 GLU F 107
REMARK 465 ASN F 108
REMARK 465 THR F 109
REMARK 465 ALA F 110
REMARK 465 PRO F 111
REMARK 465 ARG F 112
REMARK 465 LEU F 113
REMARK 465 ASN F 142
REMARK 465 VAL F 143
REMARK 465 ASN F 144
REMARK 465 THR F 145
REMARK 465 GLU F 146
REMARK 465 GLU F 147
REMARK 465 GLN F 148
REMARK 465 ASP F 149
REMARK 465 ILE F 150
REMARK 465 TRP F 151
REMARK 465 GLN F 152
REMARK 465 LYS F 153
REMARK 465 VAL F 154
REMARK 465 MET F 155
REMARK 465 GLU F 156
REMARK 465 GLY F 157
REMARK 465 GLU F 158
REMARK 465 ILE F 159
REMARK 465 VAL F 160
REMARK 465 ILE F 161
REMARK 465 GLY F 162
REMARK 465 GLU F 163
REMARK 465 ALA F 164
REMARK 465 VAL F 165
REMARK 465 ALA F 166
REMARK 465 GLN F 167
REMARK 465 LEU F 168
REMARK 465 THR F 169
REMARK 465 ARG F 170
REMARK 465 LEU F 171
REMARK 465 GLN F 172
REMARK 465 VAL F 173
REMARK 465 ARG F 174
REMARK 465 ALA F 175
REMARK 465 GLY F 176
REMARK 465 ASP F 177
REMARK 465 ALA F 178
REMARK 465 GLY F 179
REMARK 465 VAL F 180
REMARK 465 VAL F 181
REMARK 465 LEU F 182
REMARK 465 GLN F 183
REMARK 465 THR F 184
REMARK 465 ARG F 185
REMARK 465 SER F 186
REMARK 465 LEU F 187
REMARK 465 GLN F 188
REMARK 465 LEU F 189
REMARK 465 MET F 190
REMARK 465 ASN F 191
REMARK 465 ILE F 192
REMARK 465 GLY F 193
REMARK 465 ASP F 194
REMARK 465 PRO F 195
REMARK 465 ASP F 196
REMARK 465 ALA F 197
REMARK 465 LYS F 198
REMARK 465 MET F 199
REMARK 465 ALA F 200
REMARK 465 PHE F 201
REMARK 465 VAL F 202
REMARK 465 GLU F 203
REMARK 465 HIS F 204
REMARK 465 TRP F 205
REMARK 465 GLN F 206
REMARK 465 GLY F 207
REMARK 465 GLN F 208
REMARK 465 PRO F 209
REMARK 465 LEU F 210
REMARK 465 VAL F 211
REMARK 465 ALA F 212
REMARK 465 THR F 213
REMARK 465 ASP F 227
REMARK 465 GLU F 228
REMARK 465 PRO F 229
REMARK 465 ASP F 230
REMARK 465 ALA F 231
REMARK 465 GLY G 12
REMARK 465 ALA G 13
REMARK 465 ALA G 14
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 HIS H 3
REMARK 465 GLU H 4
REMARK 465 SER H 5
REMARK 465 ASN H 6
REMARK 465 PRO H 7
REMARK 465 ASN H 8
REMARK 465 ASP H 9
REMARK 465 TYR H 10
REMARK 465 ALA H 11
REMARK 465 ALA H 12
REMARK 465 GLY H 13
REMARK 465 ASP H 14
REMARK 465 ALA H 15
REMARK 465 GLY H 16
REMARK 465 ASN H 17
REMARK 465 ALA H 18
REMARK 465 SER H 19
REMARK 465 GLY H 20
REMARK 465 ARG H 21
REMARK 465 TYR H 22
REMARK 465 THR H 23
REMARK 465 THR H 24
REMARK 465 GLY H 25
REMARK 465 SER H 26
REMARK 465 ASN H 27
REMARK 465 GLY H 28
REMARK 465 ILE H 29
REMARK 465 PRO H 30
REMARK 465 PRO H 31
REMARK 465 MET H 32
REMARK 465 LEU H 33
REMARK 465 PRO H 34
REMARK 465 SER H 35
REMARK 465 GLN H 148
REMARK 465 ASP H 149
REMARK 465 ILE H 150
REMARK 465 TRP H 151
REMARK 465 GLN H 152
REMARK 465 LYS H 153
REMARK 465 VAL H 154
REMARK 465 MET H 155
REMARK 465 GLU H 156
REMARK 465 GLY H 157
REMARK 465 GLU H 158
REMARK 465 ILE H 159
REMARK 465 VAL H 160
REMARK 465 ILE H 161
REMARK 465 GLY H 162
REMARK 465 GLU H 163
REMARK 465 ALA H 164
REMARK 465 VAL H 165
REMARK 465 ALA H 166
REMARK 465 GLN H 167
REMARK 465 LEU H 168
REMARK 465 THR H 169
REMARK 465 ARG H 170
REMARK 465 LEU H 171
REMARK 465 GLN H 172
REMARK 465 VAL H 173
REMARK 465 ARG H 174
REMARK 465 ALA H 175
REMARK 465 GLY H 176
REMARK 465 ASP H 177
REMARK 465 ALA H 178
REMARK 465 GLY H 179
REMARK 465 VAL H 180
REMARK 465 VAL H 181
REMARK 465 LEU H 182
REMARK 465 GLN H 183
REMARK 465 THR H 184
REMARK 465 ARG H 185
REMARK 465 SER H 186
REMARK 465 LEU H 187
REMARK 465 GLN H 188
REMARK 465 LEU H 189
REMARK 465 MET H 190
REMARK 465 ASN H 191
REMARK 465 ILE H 192
REMARK 465 GLY H 193
REMARK 465 ASP H 194
REMARK 465 PRO H 195
REMARK 465 ASP H 196
REMARK 465 ALA H 197
REMARK 465 LYS H 198
REMARK 465 MET H 199
REMARK 465 ALA H 200
REMARK 465 PHE H 201
REMARK 465 VAL H 202
REMARK 465 GLU H 203
REMARK 465 HIS H 204
REMARK 465 TRP H 205
REMARK 465 GLN H 206
REMARK 465 GLY H 207
REMARK 465 GLN H 208
REMARK 465 PRO H 209
REMARK 465 LEU H 210
REMARK 465 VAL H 211
REMARK 465 ALA H 212
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 15 OG
REMARK 470 LYS A 17 CG CD CE NZ
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 46 CG CD OE1 OE2
REMARK 470 ASP A 56 CG OD1 OD2
REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 VAL A 134 CG1 CG2
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 VAL B 36 CG1 CG2
REMARK 470 ARG B 37 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 75 CG OD1 OD2
REMARK 470 LEU B 95 CG CD1 CD2
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 THR B 109 OG1 CG2
REMARK 470 ARG B 112 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 113 CG CD1 CD2
REMARK 470 GLU B 141 CG CD OE1 OE2
REMARK 470 ASN B 142 CG OD1 ND2
REMARK 470 VAL B 143 CG1 CG2
REMARK 470 ASN B 144 CG OD1 ND2
REMARK 470 THR B 145 OG1 CG2
REMARK 470 GLU B 146 CG CD OE1 OE2
REMARK 470 VAL B 211 CG1 CG2
REMARK 470 GLN B 224 CG CD OE1 NE2
REMARK 470 ASP B 227 CG OD1 OD2
REMARK 470 ASP B 230 CG OD1 OD2
REMARK 470 ARG B 243 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 248 CG OD1 ND2
REMARK 470 VAL B 275 CG1 CG2
REMARK 470 ARG B 278 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 295 CG CD OE1 OE2
REMARK 470 GLN B 298 CG CD OE1 NE2
REMARK 470 THR B 299 OG1 CG2
REMARK 470 LEU B 303 CG CD1 CD2
REMARK 470 LYS B 315 CG CD CE NZ
REMARK 470 SER C 15 OG
REMARK 470 LYS C 17 CG CD CE NZ
REMARK 470 ARG C 40 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 46 CG CD OE1 OE2
REMARK 470 LYS C 114 CG CD CE NZ
REMARK 470 VAL D 36 CG1 CG2
REMARK 470 ARG D 37 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 64 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 79 CG CD CE NZ
REMARK 470 LYS D 84 CG CD CE NZ
REMARK 470 GLN D 87 CG CD OE1 NE2
REMARK 470 TYR D 104 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE D 105 CG1 CG2 CD1
REMARK 470 LEU D 113 CG CD1 CD2
REMARK 470 LEU D 116 CG CD1 CD2
REMARK 470 HIS D 123 CG ND1 CD2 CE1 NE2
REMARK 470 LEU D 130 CG CD1 CD2
REMARK 470 ARG D 131 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 138 CG CD1 CD2
REMARK 470 GLU D 141 CG CD OE1 OE2
REMARK 470 THR D 214 OG1 CG2
REMARK 470 VAL D 215 CG1 CG2
REMARK 470 CYS D 218 SG
REMARK 470 LYS D 223 CG CD CE NZ
REMARK 470 GLN D 224 CG CD OE1 NE2
REMARK 470 ILE D 226 CG1 CG2 CD1
REMARK 470 ARG D 243 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 245 CG CD1 CD2
REMARK 470 ASN D 248 CG OD1 ND2
REMARK 470 ILE D 254 CG1 CG2 CD1
REMARK 470 VAL D 255 CG1 CG2
REMARK 470 LYS D 256 CG CD CE NZ
REMARK 470 ASN D 257 CG OD1 ND2
REMARK 470 ILE D 262 CG1 CG2 CD1
REMARK 470 VAL D 269 CG1 CG2
REMARK 470 GLN D 270 CG CD OE1 NE2
REMARK 470 GLU D 272 CG CD OE1 OE2
REMARK 470 LEU D 273 CG CD1 CD2
REMARK 470 ASP D 274 CG OD1 OD2
REMARK 470 VAL D 275 CG1 CG2
REMARK 470 ARG D 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 295 CG CD OE1 OE2
REMARK 470 LEU D 296 CG CD1 CD2
REMARK 470 SER D 297 OG
REMARK 470 GLN D 298 CG CD OE1 NE2
REMARK 470 LYS D 315 CG CD CE NZ
REMARK 470 SER E 15 OG
REMARK 470 ARG E 40 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 46 CG CD OE1 OE2
REMARK 470 LYS E 99 CG CD CE NZ
REMARK 470 ASP E 169 CG OD1 OD2
REMARK 470 VAL F 36 CG1 CG2
REMARK 470 ARG F 37 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 79 CG CD CE NZ
REMARK 470 LYS F 84 CG CD CE NZ
REMARK 470 LEU F 95 CG CD1 CD2
REMARK 470 TYR F 104 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU F 116 CG CD1 CD2
REMARK 470 HIS F 123 CG ND1 CD2 CE1 NE2
REMARK 470 ARG F 128 CG CD NE CZ NH1 NH2
REMARK 470 ASN F 129 CG OD1 ND2
REMARK 470 ARG F 131 CG CD NE CZ NH1 NH2
REMARK 470 LEU F 138 CG CD1 CD2
REMARK 470 GLU F 141 CG CD OE1 OE2
REMARK 470 THR F 214 OG1 CG2
REMARK 470 LYS F 223 CG CD CE NZ
REMARK 470 GLN F 224 CG CD OE1 NE2
REMARK 470 ILE F 226 CG1 CG2 CD1
REMARK 470 VAL F 232 CG1 CG2
REMARK 470 SER F 233 OG
REMARK 470 ARG F 243 CG CD NE CZ NH1 NH2
REMARK 470 ASN F 248 CG OD1 ND2
REMARK 470 THR F 252 OG1 CG2
REMARK 470 ILE F 262 CG1 CG2 CD1
REMARK 470 VAL F 269 CG1 CG2
REMARK 470 GLN F 270 CG CD OE1 NE2
REMARK 470 GLU F 272 CG CD OE1 OE2
REMARK 470 LEU F 273 CG CD1 CD2
REMARK 470 ASP F 274 CG OD1 OD2
REMARK 470 VAL F 275 CG1 CG2
REMARK 470 TYR F 277 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG F 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 295 CG CD OE1 OE2
REMARK 470 GLN F 298 CG CD OE1 NE2
REMARK 470 ILE F 301 CG1 CG2 CD1
REMARK 470 LYS F 315 CG CD CE NZ
REMARK 470 ARG F 350 CG CD NE CZ NH1 NH2
REMARK 470 SER G 15 OG
REMARK 470 ARG G 40 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 42 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 46 CG CD OE1 OE2
REMARK 470 ASP G 169 CG OD1 OD2
REMARK 470 VAL H 36 CG1 CG2
REMARK 470 ARG H 37 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 77 CG OD1 OD2
REMARK 470 LYS H 79 CG CD CE NZ
REMARK 470 LYS H 84 CG CD CE NZ
REMARK 470 GLU H 107 CG CD OE1 OE2
REMARK 470 THR H 109 OG1 CG2
REMARK 470 ARG H 112 CG CD NE CZ NH1 NH2
REMARK 470 LEU H 113 CG CD1 CD2
REMARK 470 ARG H 131 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 141 CG CD OE1 OE2
REMARK 470 ASN H 142 CG OD1 ND2
REMARK 470 ASN H 144 CG OD1 ND2
REMARK 470 GLU H 147 CG CD OE1 OE2
REMARK 470 GLN H 224 CG CD OE1 NE2
REMARK 470 ILE H 226 CG1 CG2 CD1
REMARK 470 ASP H 227 CG OD1 OD2
REMARK 470 ASP H 230 CG OD1 OD2
REMARK 470 VAL H 232 CG1 CG2
REMARK 470 ARG H 243 CG CD NE CZ NH1 NH2
REMARK 470 ASN H 248 CG OD1 ND2
REMARK 470 VAL H 269 CG1 CG2
REMARK 470 GLN H 270 CG CD OE1 NE2
REMARK 470 LEU H 273 CG CD1 CD2
REMARK 470 ASP H 274 CG OD1 OD2
REMARK 470 VAL H 275 CG1 CG2
REMARK 470 ARG H 278 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 292 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 295 CG CD OE1 OE2
REMARK 470 GLN H 298 CG CD OE1 NE2
REMARK 470 LYS H 315 CG CD CE NZ
REMARK 470 ASN H 423 CG OD1 ND2
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 OG SER D 385 O ASN D 387 2.12
REMARK 500 NH2 ARG B 350 OE1 GLU B 352 2.12
REMARK 500 OG1 THR E 31 O2B GTP E 600 2.13
REMARK 500 OG1 THR C 31 O2B GTP C 600 2.15
REMARK 500 NH2 ARG H 350 OE1 GLU H 352 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 80 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 LEU H 80 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
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 ARG A 36 1.17 -61.42
REMARK 500 ALA A 45 -75.45 -77.74
REMARK 500 PRO A 62 2.79 -68.30
REMARK 500 ASN B 62 67.92 -104.49
REMARK 500 ASP B 77 -13.48 -49.63
REMARK 500 LEU B 113 -48.80 -174.20
REMARK 500 LEU B 130 -8.39 41.04
REMARK 500 TYR B 133 -30.62 -130.90
REMARK 500 PRO B 139 -175.55 -65.11
REMARK 500 VAL B 143 -153.55 -113.56
REMARK 500 ASN B 144 35.68 -153.20
REMARK 500 GLU B 304 -77.57 -67.09
REMARK 500 ALA B 305 -166.29 -79.48
REMARK 500 VAL B 308 -24.67 -142.23
REMARK 500 LEU B 313 -163.40 -110.21
REMARK 500 ASN B 323 30.47 -83.86
REMARK 500 CYS B 343 -162.35 -124.16
REMARK 500 ASN B 358 59.09 30.31
REMARK 500 GLU B 376 -115.76 53.99
REMARK 500 ASN B 402 79.65 -108.94
REMARK 500 PRO B 419 152.24 -48.65
REMARK 500 ARG C 36 2.65 -59.71
REMARK 500 ALA C 45 -79.29 -76.31
REMARK 500 PRO C 62 3.09 -68.38
REMARK 500 LYS C 120 49.09 -80.44
REMARK 500 ASN D 62 65.29 -106.93
REMARK 500 PHE D 64 24.76 -79.40
REMARK 500 LEU D 130 -37.01 63.34
REMARK 500 TYR D 133 -33.75 -132.27
REMARK 500 PRO D 249 -2.93 -56.48
REMARK 500 GLU D 304 -75.58 -65.66
REMARK 500 ALA D 305 -165.76 -79.61
REMARK 500 VAL D 308 -28.64 -141.55
REMARK 500 LEU D 313 -160.49 -109.66
REMARK 500 ALA D 314 -73.04 -61.86
REMARK 500 ASN D 323 32.44 -84.22
REMARK 500 CYS D 343 -159.73 -119.55
REMARK 500 ASN D 358 59.86 30.28
REMARK 500 GLU D 376 -111.14 54.21
REMARK 500 ASN D 402 75.64 -105.80
REMARK 500 PRO D 419 155.25 -48.54
REMARK 500 ALA E 45 -78.69 -78.10
REMARK 500 PRO E 62 2.95 -68.57
REMARK 500 LYS E 120 49.60 -78.80
REMARK 500 ASN F 62 66.08 -106.86
REMARK 500 LEU F 130 -49.08 58.03
REMARK 500 TYR F 133 -33.48 -133.95
REMARK 500 GLU F 304 -73.87 -66.56
REMARK 500 ALA F 305 -168.53 -79.56
REMARK 500 VAL F 308 -28.94 -143.62
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE B 226 ASP B 227 129.93
REMARK 500 THR H 145 GLU H 146 -149.37
REMARK 500 ILE H 226 ASP H 227 131.94
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 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP A 600 O1G
REMARK 620 2 GTP A 600 O2B 88.2
REMARK 620 3 THR A 31 OG1 151.1 94.7
REMARK 620 4 THR A 50 OG1 92.5 167.5 90.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1426 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 99 O
REMARK 620 2 THR B 217 O 120.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1427 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 57 SG
REMARK 620 2 VAL B 99 O 97.3
REMARK 620 3 HG B1438 HG 159.7 62.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1430 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 LEU B 247 O 99.1
REMARK 620 3 HG B1433 HG 157.4 68.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1431 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 61 SG
REMARK 620 2 HG B1434 HG 141.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1435 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 61 SG
REMARK 620 2 SER B 103 OG 76.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1436 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 265 O
REMARK 620 2 CYS B 218 SG 84.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG B1437 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 325 O
REMARK 620 2 HIS B 327 NE2 155.8
REMARK 620 3 CYS B 321 SG 79.5 116.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP C 600 O1G
REMARK 620 2 GTP C 600 O2B 63.6
REMARK 620 3 THR C 50 OG1 72.8 111.3
REMARK 620 4 THR C 31 OG1 89.7 58.5 71.7
REMARK 620 5 ASP C 69 OD1 169.5 126.9 101.2 96.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D1426 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HG D1432 HG
REMARK 620 2 CYS D 321 SG 165.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D1429 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D 99 O
REMARK 620 2 CYS D 57 SG 84.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D1430 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 61 SG
REMARK 620 2 SER D 103 OG 77.3
REMARK 620 3 HG D1434 HG 77.2 153.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D1431 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 234 SG
REMARK 620 2 HG D1437 HG 72.1
REMARK 620 3 HG D1435 HG 120.9 54.5
REMARK 620 4 LEU D 247 O 123.1 101.0 55.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D1433 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO D 98 O
REMARK 620 2 CYS D 57 SG 93.5
REMARK 620 3 ALA D 74 O 148.5 83.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG D1435 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU D 247 O
REMARK 620 2 HG D1437 HG 93.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP E 600 O2B
REMARK 620 2 GTP E 600 O1G 64.6
REMARK 620 3 ASP E 69 OD1 129.6 162.4
REMARK 620 4 THR E 50 OG1 116.7 71.0 105.1
REMARK 620 5 THR E 31 OG1 58.8 82.1 113.6 73.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG E1181 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 421 OG1
REMARK 620 2 HIS E 111 NE2 77.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1426 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 321 SG
REMARK 620 2 HG F1432 HG 154.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1427 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA F 265 O
REMARK 620 2 HG F1438 HG 96.3
REMARK 620 3 THR F 217 O 135.7 91.2
REMARK 620 4 HG F1439 HG 85.4 167.5 96.2
REMARK 620 5 CYS F 218 SG 129.2 94.6 93.3 74.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1429 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL F 99 O
REMARK 620 2 CYS F 57 SG 88.1
REMARK 620 3 HG F1435 HG 155.3 68.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1430 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HG F1436 HG
REMARK 620 2 SER F 103 OG 140.1
REMARK 620 3 CYS F 61 SG 68.5 89.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1431 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HG F1437 HG
REMARK 620 2 HG F1434 HG 124.7
REMARK 620 3 HG F1433 HG 67.6 167.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1433 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HG F1437 HG
REMARK 620 2 LEU F 247 O 52.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG F1437 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 234 SG
REMARK 620 2 LEU F 247 O 114.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GTP G 600 O1G
REMARK 620 2 GTP G 600 O2B 80.4
REMARK 620 3 THR G 31 OG1 160.1 87.0
REMARK 620 4 THR G 50 OG1 105.3 159.6 91.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG H1426 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HG H1433 HG
REMARK 620 2 CYS H 57 SG 57.4
REMARK 620 3 HG H1437 HG 146.8 152.7
REMARK 620 4 VAL H 99 O 138.5 93.3 59.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG H1427 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HG H1438 HG
REMARK 620 2 ALA H 265 O 109.2
REMARK 620 3 THR H 217 O 74.0 137.9
REMARK 620 4 HG H1439 HG 156.6 92.6 95.9
REMARK 620 5 CYS H 218 SG 82.3 119.9 102.3 79.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG H1428 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 234 SG
REMARK 620 2 HG H1432 HG 152.9
REMARK 620 3 LEU H 247 O 91.6 68.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG H1431 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER H 103 OG
REMARK 620 2 HG H1435 HG 161.7
REMARK 620 3 HG H1436 HG 72.8 104.9
REMARK 620 4 CYS H 61 SG 86.3 98.7 155.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG H1433 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA H 74 O
REMARK 620 2 CYS H 57 SG 81.3
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 GTP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP G 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1426
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1427
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1426
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1427
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1428
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1429
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1428
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1429
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1430
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1430
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1426
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1426
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1431
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1427
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1427
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1431
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1428
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1428
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1429
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1429
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1430
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1430
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG E 1181
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1431
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG C 1181
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1431
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG G 1181
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 1181
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1432
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1433
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1432
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1433
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1434
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1432
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1432
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1434
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1437
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1433
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1434
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1438
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG H 1439
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1433
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1434
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1435
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1437
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1438
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1436
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG D 1437
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1437
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG F 1439
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 1438
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4V0K RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CRARL6DN IN THE GDP BOUND FORM
REMARK 900 RELATED ID: 4V0M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BBS1N IN COMPLEX WITH ARL6DN
REMARK 900 RELATED ID: 4V0O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BBS1N IN COMPLEX WITH ARL6DN, SOAKED WITH LEAD
DBREF 4V0N A 16 180 UNP A8JF99 A8JF99_CHLRE 16 180
DBREF 4V0N B 1 425 UNP A8JEA1 A8JEA1_CHLRE 1 425
DBREF 4V0N C 16 180 UNP A8JF99 A8JF99_CHLRE 16 180
DBREF 4V0N D 1 425 UNP A8JEA1 A8JEA1_CHLRE 1 425
DBREF 4V0N E 16 180 UNP A8JF99 A8JF99_CHLRE 16 180
DBREF 4V0N F 1 425 UNP A8JEA1 A8JEA1_CHLRE 1 425
DBREF 4V0N G 16 180 UNP A8JF99 A8JF99_CHLRE 16 180
DBREF 4V0N H 1 425 UNP A8JEA1 A8JEA1_CHLRE 1 425
SEQADV 4V0N GLY A 12 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA A 13 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA A 14 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N SER A 15 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ARG B 37 UNP A8JEA1 LYS 37 CONFLICT
SEQADV 4V0N GLY C 12 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA C 13 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA C 14 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N SER C 15 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ARG D 37 UNP A8JEA1 LYS 37 CONFLICT
SEQADV 4V0N GLY E 12 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA E 13 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA E 14 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N SER E 15 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ARG F 37 UNP A8JEA1 LYS 37 CONFLICT
SEQADV 4V0N GLY G 12 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA G 13 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ALA G 14 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N SER G 15 UNP A8JF99 EXPRESSION TAG
SEQADV 4V0N ARG H 37 UNP A8JEA1 LYS 37 CONFLICT
SEQRES 1 A 169 GLY ALA ALA SER LYS LYS VAL ASN VAL LEU VAL VAL GLY
SEQRES 2 A 169 LEU ASP ASN SER GLY LYS THR THR ILE ILE GLU ARG LEU
SEQRES 3 A 169 LYS PRO ARG PRO ARG GLN ALA ALA GLU VAL ALA PRO THR
SEQRES 4 A 169 VAL GLY PHE THR VAL ASP GLU VAL GLU LYS GLY PRO LEU
SEQRES 5 A 169 THR PHE THR VAL PHE ASP MET SER GLY ALA GLY ARG TYR
SEQRES 6 A 169 ARG THR LEU TRP GLU GLN TYR TYR ARG GLU ALA ASP ALA
SEQRES 7 A 169 VAL VAL PHE VAL VAL ASP SER ALA ASP LYS LEU ARG MET
SEQRES 8 A 169 VAL VAL ALA ARG ASP GLU MET GLU HIS MET LEU LYS HIS
SEQRES 9 A 169 SER ASN MET ARG LYS VAL PRO ILE LEU TYR PHE ALA ASN
SEQRES 10 A 169 LYS LYS ASP LEU PRO VAL ALA MET PRO PRO VAL GLU ILE
SEQRES 11 A 169 ALA GLN ALA LEU GLY LEU ASP ASP ILE LYS ASP ARG PRO
SEQRES 12 A 169 TRP GLN ILE VAL PRO SER ASN GLY LEU THR GLY GLU GLY
SEQRES 13 A 169 VAL ASP LYS GLY ILE ASP TRP LEU ALA GLU ARG LEU SER
SEQRES 1 B 425 MET VAL HIS GLU SER ASN PRO ASN ASP TYR ALA ALA GLY
SEQRES 2 B 425 ASP ALA GLY ASN ALA SER GLY ARG TYR THR THR GLY SER
SEQRES 3 B 425 ASN GLY ILE PRO PRO MET LEU PRO SER VAL ARG SER VAL
SEQRES 4 B 425 TRP LEU ASP ALA PHE ASN ASP PRO VAL ALA GLY ILE SER
SEQRES 5 B 425 ALA TYR THR PRO CYS VAL HIS THR CYS ASN LEU PHE GLY
SEQRES 6 B 425 ASP GLY GLU ASN ARG LEU VAL ILE ALA ASP GLU ASP ARG
SEQRES 7 B 425 LYS LEU LYS ILE TRP LYS GLY THR GLN LYS ALA SER GLU
SEQRES 8 B 425 HIS PRO LEU LEU ASP THR PRO VAL ALA ILE CYS SER TYR
SEQRES 9 B 425 ILE SER GLU ASN THR ALA PRO ARG LEU PRO ALA LEU ALA
SEQRES 10 B 425 VAL ALA ALA GLY SER HIS ILE TYR ILE TYR ARG ASN LEU
SEQRES 11 B 425 ARG PRO TYR TYR LYS PHE VAL LEU PRO PRO GLU ASN VAL
SEQRES 12 B 425 ASN THR GLU GLU GLN ASP ILE TRP GLN LYS VAL MET GLU
SEQRES 13 B 425 GLY GLU ILE VAL ILE GLY GLU ALA VAL ALA GLN LEU THR
SEQRES 14 B 425 ARG LEU GLN VAL ARG ALA GLY ASP ALA GLY VAL VAL LEU
SEQRES 15 B 425 GLN THR ARG SER LEU GLN LEU MET ASN ILE GLY ASP PRO
SEQRES 16 B 425 ASP ALA LYS MET ALA PHE VAL GLU HIS TRP GLN GLY GLN
SEQRES 17 B 425 PRO LEU VAL ALA THR THR VAL ILE THR CYS MET ASP VAL
SEQRES 18 B 425 VAL LYS GLN ALA ILE ASP GLU PRO ASP ALA VAL SER CYS
SEQRES 19 B 425 LEU VAL VAL GLY THR GLU SER GLY ARG ILE LEU ILE LEU
SEQRES 20 B 425 ASN PRO ALA GLY THR ALA ILE VAL LYS ASN ILE TRP VAL
SEQRES 21 B 425 GLY ILE THR PRO ALA MET ILE ALA VAL GLN GLY GLU LEU
SEQRES 22 B 425 ASP VAL GLY TYR ARG ILE THR VAL ALA GLY ARG ASP GLY
SEQRES 23 B 425 LYS LEU TYR HIS ILE ARG ASN GLY GLU LEU SER GLN THR
SEQRES 24 B 425 ILE ILE GLN LEU GLU ALA GLN PRO VAL GLY LEU VAL ARG
SEQRES 25 B 425 LEU ALA LYS HIS VAL ALA VAL GLY CYS MET ASN ASP VAL
SEQRES 26 B 425 VAL HIS ALA TYR THR PRO THR GLY HIS LYS SER TRP SER
SEQRES 27 B 425 LEU TYR LEU PRO CYS HIS ILE LEU ALA MET GLN ARG MET
SEQRES 28 B 425 GLU VAL THR GLY GLN ARG ASN THR LYS ALA LEU ILE VAL
SEQRES 29 B 425 ALA LEU SER ASN GLY GLU VAL ARG VAL TYR ASN GLU LYS
SEQRES 30 B 425 LEU LEU VAL SER VAL HIS VAL SER PRO ASN PRO VAL THR
SEQRES 31 B 425 ALA LEU TRP PHE GLY ARG TYR GLY ARG GLU ASP ASN THR
SEQRES 32 B 425 LEU LEU ALA ILE THR LYS SER GLY ALA LEU ASP ILE LYS
SEQRES 33 B 425 MET LEU PRO ARG THR ALA ASN LEU GLU
SEQRES 1 C 169 GLY ALA ALA SER LYS LYS VAL ASN VAL LEU VAL VAL GLY
SEQRES 2 C 169 LEU ASP ASN SER GLY LYS THR THR ILE ILE GLU ARG LEU
SEQRES 3 C 169 LYS PRO ARG PRO ARG GLN ALA ALA GLU VAL ALA PRO THR
SEQRES 4 C 169 VAL GLY PHE THR VAL ASP GLU VAL GLU LYS GLY PRO LEU
SEQRES 5 C 169 THR PHE THR VAL PHE ASP MET SER GLY ALA GLY ARG TYR
SEQRES 6 C 169 ARG THR LEU TRP GLU GLN TYR TYR ARG GLU ALA ASP ALA
SEQRES 7 C 169 VAL VAL PHE VAL VAL ASP SER ALA ASP LYS LEU ARG MET
SEQRES 8 C 169 VAL VAL ALA ARG ASP GLU MET GLU HIS MET LEU LYS HIS
SEQRES 9 C 169 SER ASN MET ARG LYS VAL PRO ILE LEU TYR PHE ALA ASN
SEQRES 10 C 169 LYS LYS ASP LEU PRO VAL ALA MET PRO PRO VAL GLU ILE
SEQRES 11 C 169 ALA GLN ALA LEU GLY LEU ASP ASP ILE LYS ASP ARG PRO
SEQRES 12 C 169 TRP GLN ILE VAL PRO SER ASN GLY LEU THR GLY GLU GLY
SEQRES 13 C 169 VAL ASP LYS GLY ILE ASP TRP LEU ALA GLU ARG LEU SER
SEQRES 1 D 425 MET VAL HIS GLU SER ASN PRO ASN ASP TYR ALA ALA GLY
SEQRES 2 D 425 ASP ALA GLY ASN ALA SER GLY ARG TYR THR THR GLY SER
SEQRES 3 D 425 ASN GLY ILE PRO PRO MET LEU PRO SER VAL ARG SER VAL
SEQRES 4 D 425 TRP LEU ASP ALA PHE ASN ASP PRO VAL ALA GLY ILE SER
SEQRES 5 D 425 ALA TYR THR PRO CYS VAL HIS THR CYS ASN LEU PHE GLY
SEQRES 6 D 425 ASP GLY GLU ASN ARG LEU VAL ILE ALA ASP GLU ASP ARG
SEQRES 7 D 425 LYS LEU LYS ILE TRP LYS GLY THR GLN LYS ALA SER GLU
SEQRES 8 D 425 HIS PRO LEU LEU ASP THR PRO VAL ALA ILE CYS SER TYR
SEQRES 9 D 425 ILE SER GLU ASN THR ALA PRO ARG LEU PRO ALA LEU ALA
SEQRES 10 D 425 VAL ALA ALA GLY SER HIS ILE TYR ILE TYR ARG ASN LEU
SEQRES 11 D 425 ARG PRO TYR TYR LYS PHE VAL LEU PRO PRO GLU ASN VAL
SEQRES 12 D 425 ASN THR GLU GLU GLN ASP ILE TRP GLN LYS VAL MET GLU
SEQRES 13 D 425 GLY GLU ILE VAL ILE GLY GLU ALA VAL ALA GLN LEU THR
SEQRES 14 D 425 ARG LEU GLN VAL ARG ALA GLY ASP ALA GLY VAL VAL LEU
SEQRES 15 D 425 GLN THR ARG SER LEU GLN LEU MET ASN ILE GLY ASP PRO
SEQRES 16 D 425 ASP ALA LYS MET ALA PHE VAL GLU HIS TRP GLN GLY GLN
SEQRES 17 D 425 PRO LEU VAL ALA THR THR VAL ILE THR CYS MET ASP VAL
SEQRES 18 D 425 VAL LYS GLN ALA ILE ASP GLU PRO ASP ALA VAL SER CYS
SEQRES 19 D 425 LEU VAL VAL GLY THR GLU SER GLY ARG ILE LEU ILE LEU
SEQRES 20 D 425 ASN PRO ALA GLY THR ALA ILE VAL LYS ASN ILE TRP VAL
SEQRES 21 D 425 GLY ILE THR PRO ALA MET ILE ALA VAL GLN GLY GLU LEU
SEQRES 22 D 425 ASP VAL GLY TYR ARG ILE THR VAL ALA GLY ARG ASP GLY
SEQRES 23 D 425 LYS LEU TYR HIS ILE ARG ASN GLY GLU LEU SER GLN THR
SEQRES 24 D 425 ILE ILE GLN LEU GLU ALA GLN PRO VAL GLY LEU VAL ARG
SEQRES 25 D 425 LEU ALA LYS HIS VAL ALA VAL GLY CYS MET ASN ASP VAL
SEQRES 26 D 425 VAL HIS ALA TYR THR PRO THR GLY HIS LYS SER TRP SER
SEQRES 27 D 425 LEU TYR LEU PRO CYS HIS ILE LEU ALA MET GLN ARG MET
SEQRES 28 D 425 GLU VAL THR GLY GLN ARG ASN THR LYS ALA LEU ILE VAL
SEQRES 29 D 425 ALA LEU SER ASN GLY GLU VAL ARG VAL TYR ASN GLU LYS
SEQRES 30 D 425 LEU LEU VAL SER VAL HIS VAL SER PRO ASN PRO VAL THR
SEQRES 31 D 425 ALA LEU TRP PHE GLY ARG TYR GLY ARG GLU ASP ASN THR
SEQRES 32 D 425 LEU LEU ALA ILE THR LYS SER GLY ALA LEU ASP ILE LYS
SEQRES 33 D 425 MET LEU PRO ARG THR ALA ASN LEU GLU
SEQRES 1 E 169 GLY ALA ALA SER LYS LYS VAL ASN VAL LEU VAL VAL GLY
SEQRES 2 E 169 LEU ASP ASN SER GLY LYS THR THR ILE ILE GLU ARG LEU
SEQRES 3 E 169 LYS PRO ARG PRO ARG GLN ALA ALA GLU VAL ALA PRO THR
SEQRES 4 E 169 VAL GLY PHE THR VAL ASP GLU VAL GLU LYS GLY PRO LEU
SEQRES 5 E 169 THR PHE THR VAL PHE ASP MET SER GLY ALA GLY ARG TYR
SEQRES 6 E 169 ARG THR LEU TRP GLU GLN TYR TYR ARG GLU ALA ASP ALA
SEQRES 7 E 169 VAL VAL PHE VAL VAL ASP SER ALA ASP LYS LEU ARG MET
SEQRES 8 E 169 VAL VAL ALA ARG ASP GLU MET GLU HIS MET LEU LYS HIS
SEQRES 9 E 169 SER ASN MET ARG LYS VAL PRO ILE LEU TYR PHE ALA ASN
SEQRES 10 E 169 LYS LYS ASP LEU PRO VAL ALA MET PRO PRO VAL GLU ILE
SEQRES 11 E 169 ALA GLN ALA LEU GLY LEU ASP ASP ILE LYS ASP ARG PRO
SEQRES 12 E 169 TRP GLN ILE VAL PRO SER ASN GLY LEU THR GLY GLU GLY
SEQRES 13 E 169 VAL ASP LYS GLY ILE ASP TRP LEU ALA GLU ARG LEU SER
SEQRES 1 F 425 MET VAL HIS GLU SER ASN PRO ASN ASP TYR ALA ALA GLY
SEQRES 2 F 425 ASP ALA GLY ASN ALA SER GLY ARG TYR THR THR GLY SER
SEQRES 3 F 425 ASN GLY ILE PRO PRO MET LEU PRO SER VAL ARG SER VAL
SEQRES 4 F 425 TRP LEU ASP ALA PHE ASN ASP PRO VAL ALA GLY ILE SER
SEQRES 5 F 425 ALA TYR THR PRO CYS VAL HIS THR CYS ASN LEU PHE GLY
SEQRES 6 F 425 ASP GLY GLU ASN ARG LEU VAL ILE ALA ASP GLU ASP ARG
SEQRES 7 F 425 LYS LEU LYS ILE TRP LYS GLY THR GLN LYS ALA SER GLU
SEQRES 8 F 425 HIS PRO LEU LEU ASP THR PRO VAL ALA ILE CYS SER TYR
SEQRES 9 F 425 ILE SER GLU ASN THR ALA PRO ARG LEU PRO ALA LEU ALA
SEQRES 10 F 425 VAL ALA ALA GLY SER HIS ILE TYR ILE TYR ARG ASN LEU
SEQRES 11 F 425 ARG PRO TYR TYR LYS PHE VAL LEU PRO PRO GLU ASN VAL
SEQRES 12 F 425 ASN THR GLU GLU GLN ASP ILE TRP GLN LYS VAL MET GLU
SEQRES 13 F 425 GLY GLU ILE VAL ILE GLY GLU ALA VAL ALA GLN LEU THR
SEQRES 14 F 425 ARG LEU GLN VAL ARG ALA GLY ASP ALA GLY VAL VAL LEU
SEQRES 15 F 425 GLN THR ARG SER LEU GLN LEU MET ASN ILE GLY ASP PRO
SEQRES 16 F 425 ASP ALA LYS MET ALA PHE VAL GLU HIS TRP GLN GLY GLN
SEQRES 17 F 425 PRO LEU VAL ALA THR THR VAL ILE THR CYS MET ASP VAL
SEQRES 18 F 425 VAL LYS GLN ALA ILE ASP GLU PRO ASP ALA VAL SER CYS
SEQRES 19 F 425 LEU VAL VAL GLY THR GLU SER GLY ARG ILE LEU ILE LEU
SEQRES 20 F 425 ASN PRO ALA GLY THR ALA ILE VAL LYS ASN ILE TRP VAL
SEQRES 21 F 425 GLY ILE THR PRO ALA MET ILE ALA VAL GLN GLY GLU LEU
SEQRES 22 F 425 ASP VAL GLY TYR ARG ILE THR VAL ALA GLY ARG ASP GLY
SEQRES 23 F 425 LYS LEU TYR HIS ILE ARG ASN GLY GLU LEU SER GLN THR
SEQRES 24 F 425 ILE ILE GLN LEU GLU ALA GLN PRO VAL GLY LEU VAL ARG
SEQRES 25 F 425 LEU ALA LYS HIS VAL ALA VAL GLY CYS MET ASN ASP VAL
SEQRES 26 F 425 VAL HIS ALA TYR THR PRO THR GLY HIS LYS SER TRP SER
SEQRES 27 F 425 LEU TYR LEU PRO CYS HIS ILE LEU ALA MET GLN ARG MET
SEQRES 28 F 425 GLU VAL THR GLY GLN ARG ASN THR LYS ALA LEU ILE VAL
SEQRES 29 F 425 ALA LEU SER ASN GLY GLU VAL ARG VAL TYR ASN GLU LYS
SEQRES 30 F 425 LEU LEU VAL SER VAL HIS VAL SER PRO ASN PRO VAL THR
SEQRES 31 F 425 ALA LEU TRP PHE GLY ARG TYR GLY ARG GLU ASP ASN THR
SEQRES 32 F 425 LEU LEU ALA ILE THR LYS SER GLY ALA LEU ASP ILE LYS
SEQRES 33 F 425 MET LEU PRO ARG THR ALA ASN LEU GLU
SEQRES 1 G 169 GLY ALA ALA SER LYS LYS VAL ASN VAL LEU VAL VAL GLY
SEQRES 2 G 169 LEU ASP ASN SER GLY LYS THR THR ILE ILE GLU ARG LEU
SEQRES 3 G 169 LYS PRO ARG PRO ARG GLN ALA ALA GLU VAL ALA PRO THR
SEQRES 4 G 169 VAL GLY PHE THR VAL ASP GLU VAL GLU LYS GLY PRO LEU
SEQRES 5 G 169 THR PHE THR VAL PHE ASP MET SER GLY ALA GLY ARG TYR
SEQRES 6 G 169 ARG THR LEU TRP GLU GLN TYR TYR ARG GLU ALA ASP ALA
SEQRES 7 G 169 VAL VAL PHE VAL VAL ASP SER ALA ASP LYS LEU ARG MET
SEQRES 8 G 169 VAL VAL ALA ARG ASP GLU MET GLU HIS MET LEU LYS HIS
SEQRES 9 G 169 SER ASN MET ARG LYS VAL PRO ILE LEU TYR PHE ALA ASN
SEQRES 10 G 169 LYS LYS ASP LEU PRO VAL ALA MET PRO PRO VAL GLU ILE
SEQRES 11 G 169 ALA GLN ALA LEU GLY LEU ASP ASP ILE LYS ASP ARG PRO
SEQRES 12 G 169 TRP GLN ILE VAL PRO SER ASN GLY LEU THR GLY GLU GLY
SEQRES 13 G 169 VAL ASP LYS GLY ILE ASP TRP LEU ALA GLU ARG LEU SER
SEQRES 1 H 425 MET VAL HIS GLU SER ASN PRO ASN ASP TYR ALA ALA GLY
SEQRES 2 H 425 ASP ALA GLY ASN ALA SER GLY ARG TYR THR THR GLY SER
SEQRES 3 H 425 ASN GLY ILE PRO PRO MET LEU PRO SER VAL ARG SER VAL
SEQRES 4 H 425 TRP LEU ASP ALA PHE ASN ASP PRO VAL ALA GLY ILE SER
SEQRES 5 H 425 ALA TYR THR PRO CYS VAL HIS THR CYS ASN LEU PHE GLY
SEQRES 6 H 425 ASP GLY GLU ASN ARG LEU VAL ILE ALA ASP GLU ASP ARG
SEQRES 7 H 425 LYS LEU LYS ILE TRP LYS GLY THR GLN LYS ALA SER GLU
SEQRES 8 H 425 HIS PRO LEU LEU ASP THR PRO VAL ALA ILE CYS SER TYR
SEQRES 9 H 425 ILE SER GLU ASN THR ALA PRO ARG LEU PRO ALA LEU ALA
SEQRES 10 H 425 VAL ALA ALA GLY SER HIS ILE TYR ILE TYR ARG ASN LEU
SEQRES 11 H 425 ARG PRO TYR TYR LYS PHE VAL LEU PRO PRO GLU ASN VAL
SEQRES 12 H 425 ASN THR GLU GLU GLN ASP ILE TRP GLN LYS VAL MET GLU
SEQRES 13 H 425 GLY GLU ILE VAL ILE GLY GLU ALA VAL ALA GLN LEU THR
SEQRES 14 H 425 ARG LEU GLN VAL ARG ALA GLY ASP ALA GLY VAL VAL LEU
SEQRES 15 H 425 GLN THR ARG SER LEU GLN LEU MET ASN ILE GLY ASP PRO
SEQRES 16 H 425 ASP ALA LYS MET ALA PHE VAL GLU HIS TRP GLN GLY GLN
SEQRES 17 H 425 PRO LEU VAL ALA THR THR VAL ILE THR CYS MET ASP VAL
SEQRES 18 H 425 VAL LYS GLN ALA ILE ASP GLU PRO ASP ALA VAL SER CYS
SEQRES 19 H 425 LEU VAL VAL GLY THR GLU SER GLY ARG ILE LEU ILE LEU
SEQRES 20 H 425 ASN PRO ALA GLY THR ALA ILE VAL LYS ASN ILE TRP VAL
SEQRES 21 H 425 GLY ILE THR PRO ALA MET ILE ALA VAL GLN GLY GLU LEU
SEQRES 22 H 425 ASP VAL GLY TYR ARG ILE THR VAL ALA GLY ARG ASP GLY
SEQRES 23 H 425 LYS LEU TYR HIS ILE ARG ASN GLY GLU LEU SER GLN THR
SEQRES 24 H 425 ILE ILE GLN LEU GLU ALA GLN PRO VAL GLY LEU VAL ARG
SEQRES 25 H 425 LEU ALA LYS HIS VAL ALA VAL GLY CYS MET ASN ASP VAL
SEQRES 26 H 425 VAL HIS ALA TYR THR PRO THR GLY HIS LYS SER TRP SER
SEQRES 27 H 425 LEU TYR LEU PRO CYS HIS ILE LEU ALA MET GLN ARG MET
SEQRES 28 H 425 GLU VAL THR GLY GLN ARG ASN THR LYS ALA LEU ILE VAL
SEQRES 29 H 425 ALA LEU SER ASN GLY GLU VAL ARG VAL TYR ASN GLU LYS
SEQRES 30 H 425 LEU LEU VAL SER VAL HIS VAL SER PRO ASN PRO VAL THR
SEQRES 31 H 425 ALA LEU TRP PHE GLY ARG TYR GLY ARG GLU ASP ASN THR
SEQRES 32 H 425 LEU LEU ALA ILE THR LYS SER GLY ALA LEU ASP ILE LYS
SEQRES 33 H 425 MET LEU PRO ARG THR ALA ASN LEU GLU
HET GTP A 600 32
HET MG A 601 1
HET HG A1181 1
HET HG B1426 1
HET HG B1427 1
HET HG B1428 1
HET HG B1429 1
HET HG B1430 1
HET HG B1431 1
HET HG B1432 1
HET HG B1433 1
HET HG B1434 1
HET HG B1435 1
HET HG B1436 1
HET HG B1437 1
HET HG B1438 1
HET GTP C 600 32
HET MG C 601 1
HET HG C1181 1
HET HG D1426 1
HET HG D1427 1
HET HG D1428 1
HET HG D1429 1
HET HG D1430 1
HET HG D1431 1
HET HG D1432 1
HET HG D1433 1
HET HG D1434 1
HET HG D1435 1
HET HG D1436 1
HET HG D1437 1
HET GTP E 600 32
HET MG E 601 1
HET HG E1181 1
HET HG F1426 1
HET HG F1427 1
HET HG F1428 1
HET HG F1429 1
HET HG F1430 1
HET HG F1431 1
HET HG F1432 1
HET HG F1433 1
HET HG F1434 1
HET HG F1435 1
HET HG F1436 1
HET HG F1437 1
HET HG F1438 1
HET HG F1439 1
HET GTP G 600 32
HET MG G 601 1
HET HG G1181 1
HET HG H1426 1
HET HG H1427 1
HET HG H1428 1
HET HG H1429 1
HET HG H1430 1
HET HG H1431 1
HET HG H1432 1
HET HG H1433 1
HET HG H1434 1
HET HG H1435 1
HET HG H1436 1
HET HG H1437 1
HET HG H1438 1
HET HG H1439 1
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM HG MERCURY (II) ION
FORMUL 9 GTP 4(C10 H16 N5 O14 P3)
FORMUL 10 MG 4(MG 2+)
FORMUL 11 HG 57(HG 2+)
HELIX 1 1 GLY A 29 ARG A 36 1 8
HELIX 2 2 ALA A 73 TYR A 84 5 12
HELIX 3 3 ARG A 101 HIS A 115 1 15
HELIX 4 4 PRO A 137 GLY A 146 1 10
HELIX 5 5 LEU A 147 ILE A 150 5 4
HELIX 6 6 GLY A 167 LEU A 179 1 13
HELIX 7 7 TYR B 54 PRO B 56 5 3
HELIX 8 8 GLY C 29 ARG C 36 1 8
HELIX 9 9 ALA C 73 LEU C 79 5 7
HELIX 10 10 TRP C 80 ARG C 85 1 6
HELIX 11 11 ARG C 101 HIS C 115 1 15
HELIX 12 12 PRO C 137 LEU C 145 1 9
HELIX 13 13 GLY C 146 ILE C 150 5 5
HELIX 14 14 GLY C 167 LEU C 179 1 13
HELIX 15 15 TYR D 54 PRO D 56 5 3
HELIX 16 16 GLY E 29 ARG E 36 1 8
HELIX 17 17 ALA E 73 TYR E 84 5 12
HELIX 18 18 ARG E 101 HIS E 115 1 15
HELIX 19 19 PRO E 137 LEU E 145 1 9
HELIX 20 20 GLY E 146 ILE E 150 5 5
HELIX 21 21 GLY E 167 LEU E 179 1 13
HELIX 22 22 TYR F 54 PRO F 56 5 3
HELIX 23 23 GLY G 29 ARG G 36 1 8
HELIX 24 24 ALA G 73 TYR G 84 5 12
HELIX 25 25 ARG G 101 HIS G 115 1 15
HELIX 26 26 PRO G 137 LEU G 145 1 9
HELIX 27 27 GLY G 146 ILE G 150 5 5
HELIX 28 28 GLY G 167 LEU G 179 1 13
HELIX 29 29 TYR H 54 PRO H 56 5 3
SHEET 1 AA 6 PHE A 53 LYS A 60 0
SHEET 2 AA 6 LEU A 63 MET A 70 -1 O LEU A 63 N LYS A 60
SHEET 3 AA 6 LYS A 16 GLY A 24 1 O LYS A 16 N THR A 64
SHEET 4 AA 6 ALA A 89 ASP A 95 1 O ALA A 89 N LEU A 21
SHEET 5 AA 6 ILE A 123 ASN A 128 1 O LEU A 124 N PHE A 92
SHEET 6 AA 6 TRP A 155 PRO A 159 1 O GLN A 156 N TYR A 125
SHEET 1 BA 4 LEU B 41 ASP B 46 0
SHEET 2 BA 4 LEU B 413 MET B 417 -1 O LEU B 413 N ASP B 46
SHEET 3 BA 4 GLU B 400 THR B 408 -1 O LEU B 404 N LYS B 416
SHEET 4 BA 4 VAL B 389 TYR B 397 -1 N THR B 390 O ILE B 407
SHEET 1 BB 4 VAL B 58 CYS B 61 0
SHEET 2 BB 4 ARG B 70 ALA B 74 -1 O ARG B 70 N CYS B 61
SHEET 3 BB 4 LYS B 79 LYS B 84 -1 O LYS B 81 N ILE B 73
SHEET 4 BB 4 GLN B 87 PRO B 93 -1 O GLN B 87 N LYS B 84
SHEET 1 BC 4 ALA B 100 TYR B 104 0
SHEET 2 BC 4 ALA B 115 ALA B 120 -1 O ALA B 115 N TYR B 104
SHEET 3 BC 4 HIS B 123 ARG B 128 -1 O HIS B 123 N ALA B 120
SHEET 4 BC 4 ARG B 131 VAL B 137 -1 O ARG B 131 N ARG B 128
SHEET 1 BD 4 ILE B 216 LYS B 223 0
SHEET 2 BD 4 SER B 233 THR B 239 -1 O CYS B 234 N VAL B 222
SHEET 3 BD 4 ARG B 243 LEU B 247 -1 O ARG B 243 N THR B 239
SHEET 4 BD 4 ILE B 254 TRP B 259 -1 N VAL B 255 O ILE B 246
SHEET 1 BE 4 PRO B 264 GLU B 272 0
SHEET 2 BE 4 GLY B 276 GLY B 283 -1 O GLY B 276 N GLU B 272
SHEET 3 BE 4 LYS B 287 ARG B 292 -1 O LYS B 287 N GLY B 283
SHEET 4 BE 4 GLU B 295 LEU B 296 1 O GLU B 295 N ARG B 292
SHEET 1 BF 4 PRO B 264 GLU B 272 0
SHEET 2 BF 4 GLY B 276 GLY B 283 -1 O GLY B 276 N GLU B 272
SHEET 3 BF 4 LYS B 287 ARG B 292 -1 O LYS B 287 N GLY B 283
SHEET 4 BF 4 ILE B 301 GLN B 302 -1 O ILE B 301 N LEU B 288
SHEET 1 BG 2 GLU B 295 LEU B 296 0
SHEET 2 BG 2 LYS B 287 ARG B 292 1 O ARG B 292 N GLU B 295
SHEET 1 BH 4 PRO B 307 ARG B 312 0
SHEET 2 BH 4 VAL B 317 CYS B 321 -1 O ALA B 318 N VAL B 311
SHEET 3 BH 4 VAL B 325 TYR B 329 -1 O VAL B 325 N CYS B 321
SHEET 4 BH 4 LYS B 335 TYR B 340 -1 N SER B 336 O ALA B 328
SHEET 1 BI 4 ILE B 345 VAL B 353 0
SHEET 2 BI 4 THR B 359 LEU B 366 -1 O THR B 359 N VAL B 353
SHEET 3 BI 4 GLU B 370 ASN B 375 -1 O GLU B 370 N LEU B 366
SHEET 4 BI 4 LEU B 378 VAL B 384 -1 O LEU B 378 N ASN B 375
SHEET 1 CA 6 PHE C 53 LYS C 60 0
SHEET 2 CA 6 LEU C 63 MET C 70 -1 O LEU C 63 N LYS C 60
SHEET 3 CA 6 LYS C 16 GLY C 24 1 O LYS C 16 N THR C 64
SHEET 4 CA 6 ALA C 89 ASP C 95 1 O ALA C 89 N LEU C 21
SHEET 5 CA 6 ILE C 123 ASN C 128 1 O LEU C 124 N PHE C 92
SHEET 6 CA 6 TRP C 155 PRO C 159 1 O GLN C 156 N TYR C 125
SHEET 1 DA 4 LEU D 41 ASP D 46 0
SHEET 2 DA 4 LEU D 413 MET D 417 -1 O LEU D 413 N ASP D 46
SHEET 3 DA 4 GLU D 400 THR D 408 -1 O LEU D 404 N LYS D 416
SHEET 4 DA 4 VAL D 389 TYR D 397 -1 N THR D 390 O ILE D 407
SHEET 1 DB 4 VAL D 58 CYS D 61 0
SHEET 2 DB 4 ARG D 70 ALA D 74 -1 O ARG D 70 N CYS D 61
SHEET 3 DB 4 LYS D 79 LYS D 84 -1 O LYS D 81 N ILE D 73
SHEET 4 DB 4 GLN D 87 PRO D 93 -1 O GLN D 87 N LYS D 84
SHEET 1 DC 4 ALA D 100 TYR D 104 0
SHEET 2 DC 4 ALA D 115 ALA D 120 -1 O ALA D 115 N TYR D 104
SHEET 3 DC 4 HIS D 123 ARG D 128 -1 O HIS D 123 N ALA D 120
SHEET 4 DC 4 ARG D 131 PRO D 132 1 O ARG D 131 N ARG D 128
SHEET 1 DD 4 ALA D 100 TYR D 104 0
SHEET 2 DD 4 ALA D 115 ALA D 120 -1 O ALA D 115 N TYR D 104
SHEET 3 DD 4 HIS D 123 ARG D 128 -1 O HIS D 123 N ALA D 120
SHEET 4 DD 4 PHE D 136 VAL D 137 -1 O PHE D 136 N ILE D 124
SHEET 1 DE 2 ARG D 131 PRO D 132 0
SHEET 2 DE 2 HIS D 123 ARG D 128 1 O ARG D 128 N ARG D 131
SHEET 1 DF 4 ILE D 216 LYS D 223 0
SHEET 2 DF 4 SER D 233 THR D 239 -1 O CYS D 234 N VAL D 222
SHEET 3 DF 4 ARG D 243 LEU D 247 -1 O ARG D 243 N THR D 239
SHEET 4 DF 4 ILE D 254 TRP D 259 -1 O LYS D 256 N ILE D 246
SHEET 1 DG 4 PRO D 264 GLU D 272 0
SHEET 2 DG 4 GLY D 276 GLY D 283 -1 O GLY D 276 N GLU D 272
SHEET 3 DG 4 LYS D 287 ARG D 292 -1 O LYS D 287 N GLY D 283
SHEET 4 DG 4 GLU D 295 LEU D 296 1 O GLU D 295 N ARG D 292
SHEET 1 DH 4 PRO D 264 GLU D 272 0
SHEET 2 DH 4 GLY D 276 GLY D 283 -1 O GLY D 276 N GLU D 272
SHEET 3 DH 4 LYS D 287 ARG D 292 -1 O LYS D 287 N GLY D 283
SHEET 4 DH 4 ILE D 301 GLN D 302 -1 O ILE D 301 N LEU D 288
SHEET 1 DI 2 GLU D 295 LEU D 296 0
SHEET 2 DI 2 LYS D 287 ARG D 292 1 O ARG D 292 N GLU D 295
SHEET 1 DJ 4 PRO D 307 ARG D 312 0
SHEET 2 DJ 4 VAL D 317 CYS D 321 -1 O ALA D 318 N VAL D 311
SHEET 3 DJ 4 VAL D 325 TYR D 329 -1 O VAL D 325 N CYS D 321
SHEET 4 DJ 4 LYS D 335 TYR D 340 -1 N SER D 336 O ALA D 328
SHEET 1 DK 4 ILE D 345 VAL D 353 0
SHEET 2 DK 4 THR D 359 LEU D 366 -1 O THR D 359 N VAL D 353
SHEET 3 DK 4 GLU D 370 ASN D 375 -1 O GLU D 370 N LEU D 366
SHEET 4 DK 4 LEU D 378 VAL D 384 -1 O LEU D 378 N ASN D 375
SHEET 1 EA 6 PHE E 53 LYS E 60 0
SHEET 2 EA 6 LEU E 63 MET E 70 -1 O LEU E 63 N LYS E 60
SHEET 3 EA 6 LYS E 16 GLY E 24 1 O LYS E 16 N THR E 64
SHEET 4 EA 6 ALA E 89 ASP E 95 1 O ALA E 89 N LEU E 21
SHEET 5 EA 6 ILE E 123 ASN E 128 1 O LEU E 124 N PHE E 92
SHEET 6 EA 6 TRP E 155 PRO E 159 1 O GLN E 156 N TYR E 125
SHEET 1 FA 4 LEU F 41 ASP F 46 0
SHEET 2 FA 4 LEU F 413 MET F 417 -1 O LEU F 413 N ASP F 46
SHEET 3 FA 4 GLU F 400 THR F 408 -1 O LEU F 404 N LYS F 416
SHEET 4 FA 4 VAL F 389 TYR F 397 -1 N THR F 390 O ILE F 407
SHEET 1 FB 4 VAL F 58 CYS F 61 0
SHEET 2 FB 4 ARG F 70 ALA F 74 -1 O ARG F 70 N CYS F 61
SHEET 3 FB 4 LYS F 79 LYS F 84 -1 O LYS F 81 N ILE F 73
SHEET 4 FB 4 GLN F 87 PRO F 93 -1 O GLN F 87 N LYS F 84
SHEET 1 FC 4 ALA F 100 SER F 103 0
SHEET 2 FC 4 LEU F 116 ALA F 120 -1 O ALA F 117 N CYS F 102
SHEET 3 FC 4 HIS F 123 TYR F 127 -1 O HIS F 123 N ALA F 120
SHEET 4 FC 4 PRO F 132 VAL F 137 -1 N TYR F 133 O ILE F 126
SHEET 1 FD 4 ILE F 216 LYS F 223 0
SHEET 2 FD 4 SER F 233 THR F 239 -1 O CYS F 234 N VAL F 222
SHEET 3 FD 4 ARG F 243 LEU F 247 -1 O ARG F 243 N THR F 239
SHEET 4 FD 4 ILE F 254 TRP F 259 -1 N VAL F 255 O ILE F 246
SHEET 1 FE 4 PRO F 264 GLU F 272 0
SHEET 2 FE 4 GLY F 276 GLY F 283 -1 O GLY F 276 N GLU F 272
SHEET 3 FE 4 LYS F 287 ARG F 292 -1 O LYS F 287 N GLY F 283
SHEET 4 FE 4 GLU F 295 LEU F 296 1 O GLU F 295 N ARG F 292
SHEET 1 FF 4 PRO F 264 GLU F 272 0
SHEET 2 FF 4 GLY F 276 GLY F 283 -1 O GLY F 276 N GLU F 272
SHEET 3 FF 4 LYS F 287 ARG F 292 -1 O LYS F 287 N GLY F 283
SHEET 4 FF 4 ILE F 301 GLN F 302 -1 O ILE F 301 N LEU F 288
SHEET 1 FG 2 GLU F 295 LEU F 296 0
SHEET 2 FG 2 LYS F 287 ARG F 292 1 O ARG F 292 N GLU F 295
SHEET 1 FH 4 PRO F 307 ARG F 312 0
SHEET 2 FH 4 VAL F 317 CYS F 321 -1 O ALA F 318 N VAL F 311
SHEET 3 FH 4 VAL F 325 TYR F 329 -1 O VAL F 325 N CYS F 321
SHEET 4 FH 4 LYS F 335 TYR F 340 -1 N SER F 336 O ALA F 328
SHEET 1 FI 4 ILE F 345 VAL F 353 0
SHEET 2 FI 4 THR F 359 LEU F 366 -1 O THR F 359 N VAL F 353
SHEET 3 FI 4 GLU F 370 ASN F 375 -1 O GLU F 370 N LEU F 366
SHEET 4 FI 4 LEU F 378 VAL F 384 -1 O LEU F 378 N ASN F 375
SHEET 1 GA 6 PHE G 53 LYS G 60 0
SHEET 2 GA 6 LEU G 63 MET G 70 -1 O LEU G 63 N LYS G 60
SHEET 3 GA 6 LYS G 16 GLY G 24 1 O LYS G 16 N THR G 64
SHEET 4 GA 6 ALA G 89 ASP G 95 1 O ALA G 89 N LEU G 21
SHEET 5 GA 6 ILE G 123 ASN G 128 1 O LEU G 124 N PHE G 92
SHEET 6 GA 6 TRP G 155 PRO G 159 1 O GLN G 156 N TYR G 125
SHEET 1 HA 4 LEU H 41 ASP H 46 0
SHEET 2 HA 4 LEU H 413 MET H 417 -1 O LEU H 413 N ASP H 46
SHEET 3 HA 4 GLU H 400 THR H 408 -1 O LEU H 404 N LYS H 416
SHEET 4 HA 4 VAL H 389 TYR H 397 -1 N THR H 390 O ILE H 407
SHEET 1 HB 4 VAL H 58 CYS H 61 0
SHEET 2 HB 4 ARG H 70 ALA H 74 -1 O ARG H 70 N CYS H 61
SHEET 3 HB 4 LYS H 79 LYS H 84 -1 O LYS H 81 N ILE H 73
SHEET 4 HB 4 GLN H 87 PRO H 93 -1 O GLN H 87 N LYS H 84
SHEET 1 HC 4 ALA H 100 TYR H 104 0
SHEET 2 HC 4 ALA H 115 ALA H 120 -1 O ALA H 115 N TYR H 104
SHEET 3 HC 4 HIS H 123 TYR H 127 -1 O HIS H 123 N ALA H 120
SHEET 4 HC 4 PRO H 132 VAL H 137 -1 N TYR H 133 O ILE H 126
SHEET 1 HD 4 ILE H 216 LYS H 223 0
SHEET 2 HD 4 SER H 233 THR H 239 -1 O CYS H 234 N VAL H 222
SHEET 3 HD 4 ARG H 243 LEU H 247 -1 O ARG H 243 N THR H 239
SHEET 4 HD 4 ILE H 254 TRP H 259 -1 N VAL H 255 O ILE H 246
SHEET 1 HE 4 PRO H 264 GLU H 272 0
SHEET 2 HE 4 GLY H 276 GLY H 283 -1 O GLY H 276 N GLU H 272
SHEET 3 HE 4 LYS H 287 ARG H 292 -1 O LYS H 287 N GLY H 283
SHEET 4 HE 4 GLU H 295 LEU H 296 1 O GLU H 295 N ARG H 292
SHEET 1 HF 4 PRO H 264 GLU H 272 0
SHEET 2 HF 4 GLY H 276 GLY H 283 -1 O GLY H 276 N GLU H 272
SHEET 3 HF 4 LYS H 287 ARG H 292 -1 O LYS H 287 N GLY H 283
SHEET 4 HF 4 ILE H 301 GLN H 302 -1 O ILE H 301 N LEU H 288
SHEET 1 HG 2 GLU H 295 LEU H 296 0
SHEET 2 HG 2 LYS H 287 ARG H 292 1 O ARG H 292 N GLU H 295
SHEET 1 HH 4 PRO H 307 ARG H 312 0
SHEET 2 HH 4 VAL H 317 CYS H 321 -1 O ALA H 318 N VAL H 311
SHEET 3 HH 4 VAL H 325 TYR H 329 -1 O VAL H 325 N CYS H 321
SHEET 4 HH 4 LYS H 335 TYR H 340 -1 N SER H 336 O ALA H 328
SHEET 1 HI 4 ILE H 345 VAL H 353 0
SHEET 2 HI 4 THR H 359 LEU H 366 -1 O THR H 359 N VAL H 353
SHEET 3 HI 4 GLU H 370 ASN H 375 -1 O GLU H 370 N LEU H 366
SHEET 4 HI 4 LEU H 378 VAL H 384 -1 O LEU H 378 N ASN H 375
SSBOND 1 CYS B 343 CYS D 343 1555 1555 2.08
SSBOND 2 CYS F 343 CYS H 343 1555 1555 2.09
LINK O1G GTP A 600 MG MG A 601 1555 1555 1.97
LINK O2B GTP A 600 MG MG A 601 1555 1555 1.95
LINK MG MG A 601 OG1 THR A 31 1555 1555 1.98
LINK MG MG A 601 OG1 THR A 50 1555 1555 1.89
LINK HG HG A1181 NE2 HIS A 111 1555 1555 2.57
LINK HG HG B1426 O VAL B 99 1555 1555 2.81
LINK HG HG B1426 O THR B 217 1555 1555 2.66
LINK HG HG B1427 SG CYS B 57 1555 1555 2.32
LINK HG HG B1427 O VAL B 99 1555 1555 3.06
LINK HG HG B1427 HG HG B1438 1555 1555 2.12
LINK HG HG B1428 SG CYS B 321 1555 1555 2.60
LINK HG HG B1429 SG CYS B 102 1555 1555 2.42
LINK HG HG B1430 SG CYS B 234 1555 1555 2.50
LINK HG HG B1430 O LEU B 247 1555 1555 3.01
LINK HG HG B1430 HG HG B1433 1555 1555 2.13
LINK HG HG B1431 SG CYS B 61 1555 1555 2.57
LINK HG HG B1431 HG HG B1434 1555 1555 2.26
LINK HG HG B1433 O LEU B 247 1555 1555 2.98
LINK HG HG B1434 O SER B 103 1555 1555 3.00
LINK HG HG B1435 SG CYS B 61 1555 1555 2.68
LINK HG HG B1435 OG SER B 103 1555 1555 3.18
LINK HG HG B1436 O ALA B 265 1555 1555 2.99
LINK HG HG B1436 SG CYS B 218 1555 1555 2.46
LINK HG HG B1437 O VAL B 325 1555 1555 2.94
LINK HG HG B1437 NE2 HIS B 327 1555 1555 2.68
LINK HG HG B1437 SG CYS B 321 1555 1555 3.12
LINK HG HG B1438 O VAL B 99 1555 1555 2.80
LINK O1G GTP C 600 MG MG C 601 1555 1555 2.49
LINK O2B GTP C 600 MG MG C 601 1555 1555 2.28
LINK MG MG C 601 OG1 THR C 50 1555 1555 2.17
LINK MG MG C 601 OG1 THR C 31 1555 1555 2.11
LINK MG MG C 601 OD1 ASP C 69 1555 1555 2.97
LINK HG HG D1426 HG HG D1432 1555 1555 2.34
LINK HG HG D1426 SG CYS D 321 1555 1555 2.49
LINK HG HG D1427 O ALA D 265 1555 1555 2.90
LINK HG HG D1428 SG CYS D 102 1555 1555 2.50
LINK HG HG D1429 O VAL D 99 1555 1555 2.75
LINK HG HG D1429 SG CYS D 57 1555 1555 2.52
LINK HG HG D1430 SG CYS D 61 1555 1555 2.52
LINK HG HG D1430 OG SER D 103 1555 1555 3.01
LINK HG HG D1430 HG HG D1434 1555 1555 2.49
LINK HG HG D1431 SG CYS D 234 1555 1555 2.74
LINK HG HG D1431 HG HG D1437 1555 1555 2.56
LINK HG HG D1431 HG HG D1435 1555 1555 3.15
LINK HG HG D1431 O LEU D 247 1555 1555 2.48
LINK HG HG D1433 O PRO D 98 1555 1555 2.67
LINK HG HG D1433 SG CYS D 57 1555 1555 2.82
LINK HG HG D1433 O ALA D 74 1555 1555 2.84
LINK HG HG D1434 SG CYS D 61 1555 1555 3.12
LINK HG HG D1435 O LEU D 247 1555 1555 2.69
LINK HG HG D1435 HG HG D1437 1555 1555 2.67
LINK HG HG D1436 HG HG D1437 1555 1555 3.27
LINK HG HG D1437 SG CYS D 234 1555 1555 3.12
LINK O2B GTP E 600 MG MG E 601 1555 1555 2.26
LINK O1G GTP E 600 MG MG E 601 1555 1555 2.59
LINK MG MG E 601 OD1 ASP E 69 1555 1555 2.89
LINK MG MG E 601 OG1 THR E 50 1555 1555 1.89
LINK MG MG E 601 OG1 THR E 31 1555 1555 2.08
LINK HG HG E1181 OG1 THR F 421 1555 1555 2.95
LINK HG HG E1181 NE2 HIS E 111 1555 1555 2.50
LINK HG HG F1426 SG CYS F 321 1555 1555 2.59
LINK HG HG F1426 HG HG F1432 1555 1555 2.57
LINK HG HG F1427 O ALA F 265 1555 1555 2.90
LINK HG HG F1427 HG HG F1438 1555 1555 2.59
LINK HG HG F1427 O THR F 217 1555 1555 3.20
LINK HG HG F1427 HG HG F1439 1555 1555 1.84
LINK HG HG F1427 SG CYS F 218 1555 1555 2.86
LINK HG HG F1428 SG CYS F 102 1555 1555 2.47
LINK HG HG F1429 O VAL F 99 1555 1555 2.77
LINK HG HG F1429 SG CYS F 57 1555 1555 2.57
LINK HG HG F1429 HG HG F1435 1555 1555 2.93
LINK HG HG F1430 HG HG F1436 1555 1555 2.24
LINK HG HG F1430 OG SER F 103 1555 1555 2.94
LINK HG HG F1430 SG CYS F 61 1555 1555 2.52
LINK HG HG F1431 HG HG F1437 1555 1555 2.09
LINK HG HG F1431 HG HG F1434 1555 1555 3.20
LINK HG HG F1431 HG HG F1433 1555 1555 2.52
LINK HG HG F1433 HG HG F1437 1555 1555 2.59
LINK HG HG F1433 O LEU F 247 1555 1555 2.60
LINK HG HG F1434 O GLN F 224 1555 1555 2.89
LINK HG HG F1435 SG CYS F 57 1555 1555 3.11
LINK HG HG F1436 SG CYS F 61 1555 1555 2.69
LINK HG HG F1437 SG CYS F 234 1555 1555 2.87
LINK HG HG F1437 O LEU F 247 1555 1555 2.30
LINK HG HG F1438 OG1 THR F 217 1555 1555 3.11
LINK HG HG F1439 SG CYS F 218 1555 1555 2.97
LINK O1G GTP G 600 MG MG G 601 1555 1555 1.92
LINK O2B GTP G 600 MG MG G 601 1555 1555 2.16
LINK MG MG G 601 OG1 THR G 31 1555 1555 1.86
LINK MG MG G 601 OG1 THR G 50 1555 1555 1.74
LINK HG HG G1181 NE2 HIS G 111 1555 1555 2.52
LINK HG HG H1426 HG HG H1433 1555 1555 3.30
LINK HG HG H1426 SG CYS H 57 1555 1555 2.37
LINK HG HG H1426 HG HG H1437 1555 1555 2.16
LINK HG HG H1426 O VAL H 99 1555 1555 3.01
LINK HG HG H1427 HG HG H1438 1555 1555 1.94
LINK HG HG H1427 O ALA H 265 1555 1555 2.60
LINK HG HG H1427 O THR H 217 1555 1555 3.18
LINK HG HG H1427 HG HG H1439 1555 1555 2.99
LINK HG HG H1427 SG CYS H 218 1555 1555 2.45
LINK HG HG H1428 SG CYS H 234 1555 1555 2.39
LINK HG HG H1428 HG HG H1432 1555 1555 2.15
LINK HG HG H1428 O LEU H 247 1555 1555 2.99
LINK HG HG H1429 SG CYS H 321 1555 1555 2.61
LINK HG HG H1430 SG CYS H 102 1555 1555 2.42
LINK HG HG H1431 OG SER H 103 1555 1555 3.02
LINK HG HG H1431 HG HG H1435 1555 1555 3.21
LINK HG HG H1431 HG HG H1436 1555 1555 2.09
LINK HG HG H1431 SG CYS H 61 1555 1555 2.37
LINK HG HG H1432 O LEU H 247 1555 1555 2.98
LINK HG HG H1433 O ALA H 74 1555 1555 2.64
LINK HG HG H1433 SG CYS H 57 1555 1555 2.84
LINK HG HG H1436 OG SER H 103 1555 1555 3.12
LINK HG HG H1437 O VAL H 99 1555 1555 2.68
LINK HG HG H1438 SG CYS H 218 1555 1555 2.91
CISPEP 1 ARG B 112 LEU B 113 0 5.12
CISPEP 2 ARG H 112 LEU H 113 0 1.49
CISPEP 3 ARG H 128 ASN H 129 0 -4.77
CISPEP 4 ASN H 129 LEU H 130 0 5.93
SITE 1 AC1 18 ASP A 26 ASN A 27 SER A 28 GLY A 29
SITE 2 AC1 18 LYS A 30 THR A 31 THR A 32 ALA A 48
SITE 3 AC1 18 THR A 50 SER A 71 GLY A 72 ASN A 128
SITE 4 AC1 18 LYS A 129 ASP A 131 ASN A 161 GLY A 162
SITE 5 AC1 18 LEU A 163 MG A 601
SITE 1 AC2 3 THR A 31 THR A 50 GTP A 600
SITE 1 AC3 16 ASN C 27 SER C 28 GLY C 29 LYS C 30
SITE 2 AC3 16 THR C 31 THR C 32 THR C 50 SER C 71
SITE 3 AC3 16 GLY C 72 ASN C 128 LYS C 129 ASP C 131
SITE 4 AC3 16 LEU C 132 ASN C 161 GLY C 162 MG C 601
SITE 1 AC4 5 THR C 31 THR C 50 ASP C 69 MET C 70
SITE 2 AC4 5 GTP C 600
SITE 1 AC5 17 ASN E 27 SER E 28 GLY E 29 LYS E 30
SITE 2 AC5 17 THR E 31 THR E 32 PRO E 49 THR E 50
SITE 3 AC5 17 SER E 71 GLY E 72 ASN E 128 LYS E 129
SITE 4 AC5 17 ASP E 131 ASN E 161 GLY E 162 LEU E 163
SITE 5 AC5 17 MG E 601
SITE 1 AC6 5 LYS E 30 THR E 31 THR E 50 ASP E 69
SITE 2 AC6 5 GTP E 600
SITE 1 AC7 17 ASN G 27 SER G 28 GLY G 29 LYS G 30
SITE 2 AC7 17 THR G 31 THR G 32 ALA G 48 THR G 50
SITE 3 AC7 17 SER G 71 GLY G 72 ASN G 128 LYS G 129
SITE 4 AC7 17 ASP G 131 ASN G 161 GLY G 162 LEU G 163
SITE 5 AC7 17 MG G 601
SITE 1 AC8 3 THR G 31 THR G 50 GTP G 600
SITE 1 AC9 4 VAL B 99 ALA B 100 THR B 217 CYS B 218
SITE 1 BC1 3 CYS B 57 VAL B 99 HG B1438
SITE 1 BC2 4 CYS H 57 VAL H 99 HG H1433 HG H1437
SITE 1 BC3 6 THR H 217 CYS H 218 ALA H 265 MET H 266
SITE 2 BC3 6 HG H1438 HG H1439
SITE 1 BC4 2 LEU B 303 CYS B 321
SITE 1 BC5 3 ILE B 101 CYS B 102 ASP B 220
SITE 1 BC6 4 CYS H 234 LEU H 247 PRO H 249 HG H1432
SITE 1 BC7 4 LEU H 303 ALA H 305 GLN H 306 CYS H 321
SITE 1 BC8 3 CYS B 234 LEU B 247 HG B1433
SITE 1 BC9 2 CYS H 102 ASP H 220
SITE 1 CC1 4 LEU D 303 GLN D 306 CYS D 321 HG D1432
SITE 1 CC2 5 LEU F 303 ALA F 305 GLN F 306 CYS F 321
SITE 2 CC2 5 HG F1432
SITE 1 CC3 6 CYS H 61 ASN H 62 SER H 103 PRO H 114
SITE 2 CC3 6 HG H1435 HG H1436
SITE 1 CC4 4 THR D 217 CYS D 218 ALA D 265 MET D 266
SITE 1 CC5 6 THR F 217 CYS F 218 ALA F 265 MET F 266
SITE 2 CC5 6 HG F1438 HG F1439
SITE 1 CC6 4 CYS B 61 SER B 103 PRO B 114 HG B1434
SITE 1 CC7 5 HIS F 59 ILE F 101 CYS F 102 MET F 219
SITE 2 CC7 5 ASP F 220
SITE 1 CC8 2 CYS D 102 ASP D 220
SITE 1 CC9 2 CYS D 57 VAL D 99
SITE 1 DC1 3 CYS F 57 VAL F 99 HG F1435
SITE 1 DC2 3 CYS F 61 SER F 103 HG F1436
SITE 1 DC3 3 CYS D 61 SER D 103 HG D1434
SITE 1 DC4 3 HIS E 111 LYS E 114 THR F 421
SITE 1 DC5 6 CYS D 234 LEU D 247 ASN D 248 PRO D 249
SITE 2 DC5 6 HG D1435 HG D1437
SITE 1 DC6 1 HIS C 111
SITE 1 DC7 4 CYS F 234 HG F1433 HG F1434 HG F1437
SITE 1 DC8 2 HIS G 111 THR H 421
SITE 1 DC9 3 HIS A 111 LYS A 114 THR B 421
SITE 1 EC1 2 GLN B 224 VAL B 232
SITE 1 EC2 2 LEU B 247 HG B1430
SITE 1 EC3 2 LEU H 247 HG H1428
SITE 1 EC4 3 CYS H 57 ALA H 74 HG H1426
SITE 1 EC5 3 GLN H 224 VAL H 232 PRO H 249
SITE 1 EC6 3 LEU D 303 PRO D 307 HG D1426
SITE 1 EC7 4 CYS H 61 ASN H 62 ASN H 69 HG H1431
SITE 1 EC8 3 GLY F 286 LEU F 303 HG F1426
SITE 1 EC9 2 SER H 103 HG H1431
SITE 1 FC1 2 SER B 103 HG B1431
SITE 1 FC2 3 PRO H 56 VAL H 99 HG H1426
SITE 1 FC3 3 CYS B 61 LEU B 63 SER B 103
SITE 1 FC4 4 LEU F 247 VAL F 255 HG F1431 HG F1437
SITE 1 FC5 3 GLN F 224 LEU F 273 HG F1431
SITE 1 FC6 3 THR H 217 CYS H 218 HG H1427
SITE 1 FC7 6 THR H 217 CYS H 218 PRO H 264 MET H 266
SITE 2 FC7 6 ILE H 267 HG H1427
SITE 1 FC8 4 ALA F 53 TYR F 54 CYS F 57 HG F1429
SITE 1 FC9 3 CYS D 57 ALA D 74 PRO D 98
SITE 1 GC1 3 CYS D 61 ASN D 62 HG D1430
SITE 1 GC2 5 ILE D 246 LEU D 247 VAL D 255 HG D1431
SITE 2 GC2 5 HG D1437
SITE 1 GC3 3 CYS F 61 ASN F 62 HG F1430
SITE 1 GC4 6 CYS F 234 LEU F 247 ASN F 248 PRO F 249
SITE 2 GC4 6 HG F1431 HG F1433
SITE 1 GC5 5 LYS D 223 GLN D 224 CYS D 234 LEU D 273
SITE 2 GC5 5 HG D1437
SITE 1 GC6 4 THR F 217 CYS F 218 PRO F 264 HG F1427
SITE 1 GC7 3 THR B 217 CYS B 218 ALA B 265
SITE 1 GC8 4 CYS D 234 HG D1431 HG D1435 HG D1436
SITE 1 GC9 4 CYS B 321 VAL B 325 VAL B 326 HIS B 327
SITE 1 HC1 3 CYS F 218 ALA F 265 HG F1427
SITE 1 HC2 3 PRO B 56 VAL B 99 HG B1427
CRYST1 123.745 123.745 443.709 90.00 90.00 120.00 P 31 2 1 24
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 0.008081 0.004666 0.000000 0.00000
SCALE2 0.000000 0.009331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002254 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
