HEADER SIGNALING PROTEIN 25-NOV-13 4NQI
TITLE STRUCTURE OF THE N-TERMINAL I-BAR DOMAIN (1-259) OF D.DISCOIDEUM IBARA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH3 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_COMMON: SLIME MOLD;
SOURCE 4 ORGANISM_TAXID: 44689;
SOURCE 5 GENE: DDB_G0274805;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS I-BAR DOMAIN, MEMBRANE REMODELLING, SIGNALING PROTEIN, CYTOKINESIS,
KEYWDS 2 ENDOCYTOSIS, LIPID BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR G.WITTE,J.FAIX,P.RUNGE-WOLLMANN
REVDAT 2 02-APR-14 4NQI 1 JRNL
REVDAT 1 05-FEB-14 4NQI 0
JRNL AUTH J.LINKNER,G.WITTE,H.ZHAO,A.JUNEMANN,B.NORDHOLZ,
JRNL AUTH 2 P.RUNGE-WOLLMANN,P.LAPPALAINEN,J.FAIX
JRNL TITL THE INVERSE BAR DOMAIN PROTEIN IBARA DRIVES MEMBRANE
JRNL TITL 2 REMODELING TO CONTROL OSMOREGULATION, PHAGOCYTOSIS AND
JRNL TITL 3 CYTOKINESIS.
JRNL REF J.CELL.SCI. V. 127 1279 2014
JRNL REFN ISSN 0021-9533
JRNL PMID 24463811
JRNL DOI 10.1242/JCS.140756
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.880
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 99167
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2562
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 48.4127 - 6.8499 0.97 3113 168 0.1752 0.1705
REMARK 3 2 6.8499 - 5.4393 0.99 3153 166 0.2337 0.2701
REMARK 3 3 5.4393 - 4.7524 0.99 3166 169 0.1827 0.1995
REMARK 3 4 4.7524 - 4.3182 0.99 3126 162 0.1607 0.1782
REMARK 3 5 4.3182 - 4.0089 0.99 3138 168 0.1512 0.1979
REMARK 3 6 4.0089 - 3.7726 0.99 3208 171 0.1596 0.1560
REMARK 3 7 3.7726 - 3.5837 0.99 3168 163 0.1640 0.2393
REMARK 3 8 3.5837 - 3.4278 1.00 3176 165 0.1830 0.2294
REMARK 3 9 3.4278 - 3.2959 1.00 3171 168 0.1903 0.2144
REMARK 3 10 3.2959 - 3.1821 1.00 3200 168 0.1934 0.2449
REMARK 3 11 3.1821 - 3.0827 1.00 3162 167 0.1974 0.2226
REMARK 3 12 3.0827 - 2.9946 1.00 3187 168 0.1939 0.2558
REMARK 3 13 2.9946 - 2.9157 1.00 3170 167 0.1953 0.2350
REMARK 3 14 2.9157 - 2.8446 1.00 3185 166 0.1989 0.2642
REMARK 3 15 2.8446 - 2.7799 1.00 3224 173 0.1964 0.2245
REMARK 3 16 2.7799 - 2.7208 1.00 3105 162 0.1889 0.2466
REMARK 3 17 2.7208 - 2.6664 1.00 3249 168 0.1942 0.2514
REMARK 3 18 2.6664 - 2.6161 1.00 3157 167 0.2101 0.2346
REMARK 3 19 2.6161 - 2.5693 1.00 3154 168 0.2234 0.3021
REMARK 3 20 2.5693 - 2.5258 1.00 3241 173 0.2199 0.3285
REMARK 3 21 2.5258 - 2.4850 1.00 3146 166 0.2278 0.2540
REMARK 3 22 2.4850 - 2.4468 1.00 3218 171 0.2254 0.2400
REMARK 3 23 2.4468 - 2.4108 1.00 3101 158 0.2401 0.3078
REMARK 3 24 2.4108 - 2.3769 1.00 3206 170 0.2473 0.3200
REMARK 3 25 2.3769 - 2.3448 1.00 3180 166 0.2500 0.3144
REMARK 3 26 2.3448 - 2.3143 1.00 3212 170 0.2559 0.3069
REMARK 3 27 2.3143 - 2.2854 1.00 3183 163 0.2676 0.2832
REMARK 3 28 2.2854 - 2.2578 1.00 3246 167 0.2736 0.3358
REMARK 3 29 2.2578 - 2.2316 0.99 3087 162 0.2800 0.3307
REMARK 3 30 2.2316 - 2.2065 0.68 2183 112 0.3156 0.3814
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 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 : 0.004 7351
REMARK 3 ANGLE : 0.766 9860
REMARK 3 CHIRALITY : 0.049 1142
REMARK 3 PLANARITY : 0.003 1291
REMARK 3 DIHEDRAL : 15.893 2909
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 4NQI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083529.
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 : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99218
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.48
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.25M AMMONIUM ACETATE,
REMARK 280 15% V/V GLYCEROL, PH 7, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.10500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 8070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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: 7950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 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 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 -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 SER A 2
REMARK 465 ASN A 3
REMARK 465 ALA A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 GLN A 7
REMARK 465 GLN A 8
REMARK 465 LYS A 144
REMARK 465 THR A 145
REMARK 465 THR A 146
REMARK 465 PRO A 147
REMARK 465 GLU A 148
REMARK 465 VAL A 149
REMARK 465 LEU A 150
REMARK 465 LYS A 151
REMARK 465 GLN A 152
REMARK 465 GLN A 153
REMARK 465 THR A 239
REMARK 465 LEU A 240
REMARK 465 VAL A 241
REMARK 465 GLN A 242
REMARK 465 ILE A 243
REMARK 465 GLN A 244
REMARK 465 PRO A 245
REMARK 465 GLN A 246
REMARK 465 GLY A 247
REMARK 465 ASP A 248
REMARK 465 THR A 249
REMARK 465 GLY A 250
REMARK 465 SER A 251
REMARK 465 ASP A 252
REMARK 465 ALA A 253
REMARK 465 TYR A 254
REMARK 465 ARG A 255
REMARK 465 ILE A 256
REMARK 465 SER A 257
REMARK 465 TYR A 258
REMARK 465 ALA A 259
REMARK 465 GLY B -4
REMARK 465 PRO B -3
REMARK 465 LEU B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 ALA B 4
REMARK 465 LYS B 5
REMARK 465 LYS B 6
REMARK 465 GLN B 7
REMARK 465 GLN B 8
REMARK 465 ARG B 139
REMARK 465 LYS B 140
REMARK 465 ALA B 141
REMARK 465 GLY B 142
REMARK 465 LYS B 143
REMARK 465 LYS B 144
REMARK 465 ARG B 238
REMARK 465 THR B 239
REMARK 465 LEU B 240
REMARK 465 VAL B 241
REMARK 465 GLN B 242
REMARK 465 ILE B 243
REMARK 465 GLN B 244
REMARK 465 PRO B 245
REMARK 465 GLN B 246
REMARK 465 GLY B 247
REMARK 465 ASP B 248
REMARK 465 THR B 249
REMARK 465 GLY B 250
REMARK 465 SER B 251
REMARK 465 ASP B 252
REMARK 465 ALA B 253
REMARK 465 TYR B 254
REMARK 465 ARG B 255
REMARK 465 ILE B 256
REMARK 465 SER B 257
REMARK 465 TYR B 258
REMARK 465 ALA B 259
REMARK 465 GLY C -4
REMARK 465 PRO C -3
REMARK 465 LEU C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MSE C 1
REMARK 465 SER C 2
REMARK 465 ASN C 3
REMARK 465 ALA C 4
REMARK 465 LYS C 5
REMARK 465 LYS C 6
REMARK 465 LYS C 140
REMARK 465 ALA C 141
REMARK 465 GLY C 142
REMARK 465 LYS C 143
REMARK 465 ARG C 238
REMARK 465 THR C 239
REMARK 465 LEU C 240
REMARK 465 VAL C 241
REMARK 465 GLN C 242
REMARK 465 ILE C 243
REMARK 465 GLN C 244
REMARK 465 PRO C 245
REMARK 465 GLN C 246
REMARK 465 GLY C 247
REMARK 465 ASP C 248
REMARK 465 THR C 249
REMARK 465 GLY C 250
REMARK 465 SER C 251
REMARK 465 ASP C 252
REMARK 465 ALA C 253
REMARK 465 TYR C 254
REMARK 465 ARG C 255
REMARK 465 ILE C 256
REMARK 465 SER C 257
REMARK 465 TYR C 258
REMARK 465 ALA C 259
REMARK 465 GLY D -4
REMARK 465 PRO D -3
REMARK 465 LEU D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MSE D 1
REMARK 465 SER D 2
REMARK 465 ASN D 3
REMARK 465 ALA D 4
REMARK 465 LYS D 5
REMARK 465 LYS D 6
REMARK 465 GLN D 7
REMARK 465 LEU D 240
REMARK 465 VAL D 241
REMARK 465 GLN D 242
REMARK 465 ILE D 243
REMARK 465 GLN D 244
REMARK 465 PRO D 245
REMARK 465 GLN D 246
REMARK 465 GLY D 247
REMARK 465 ASP D 248
REMARK 465 THR D 249
REMARK 465 GLY D 250
REMARK 465 SER D 251
REMARK 465 ASP D 252
REMARK 465 ALA D 253
REMARK 465 TYR D 254
REMARK 465 ARG D 255
REMARK 465 ILE D 256
REMARK 465 SER D 257
REMARK 465 TYR D 258
REMARK 465 ALA D 259
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 11 CG1 CG2
REMARK 480 GLU A 13 CG CD OE1 OE2
REMARK 480 LYS A 39 CG CD CE NZ
REMARK 480 LYS A 74 CD CE NZ
REMARK 480 LYS A 103 CG CD CE NZ
REMARK 480 LYS A 122 CD CE NZ
REMARK 480 GLN A 126 CD OE1 NE2
REMARK 480 ARG A 128 NE NH1 NH2
REMARK 480 GLN A 129 CG CD OE1 NE2
REMARK 480 LEU A 132 CG CD1 CD2
REMARK 480 LYS A 133 CG CD CE NZ
REMARK 480 LEU A 134 CG CD1 CD2
REMARK 480 GLU A 135 CD OE1 OE2
REMARK 480 LYS A 137 CG CD CE NZ
REMARK 480 THR A 138 CB OG1 CG2
REMARK 480 LYS A 140 CD CE NZ
REMARK 480 LYS A 143 CG CD CE NZ
REMARK 480 ILE A 154 CG1 CG2 CD1
REMARK 480 THR A 155 CB OG1 CG2
REMARK 480 GLU A 156 CB CG CD OE1 OE2
REMARK 480 ASP A 159 CB CG OD1 OD2
REMARK 480 LYS A 162 CD CE NZ
REMARK 480 GLN A 166 OE1 NE2
REMARK 480 LYS A 235 CD CE NZ
REMARK 480 GLU A 237 CD OE1 OE2
REMARK 480 ILE B 12 CD1
REMARK 480 GLU B 13 CG CD OE1 OE2
REMARK 480 LEU B 16 CG CD1 CD2
REMARK 480 LYS B 17 CD CE NZ
REMARK 480 LYS B 23 CD CE NZ
REMARK 480 LYS B 35 CE NZ
REMARK 480 LYS B 39 CD CE NZ
REMARK 480 LYS B 81 CD CE NZ
REMARK 480 GLU B 107 CG CD OE1 OE2
REMARK 480 LYS B 111 CG CD CE NZ
REMARK 480 LYS B 118 CG CD CE NZ
REMARK 480 LYS B 121 CD CE NZ
REMARK 480 GLN B 126 CG CD OE1 NE2
REMARK 480 ARG B 128 CG CD NE CZ NH1 NH2
REMARK 480 GLN B 129 CB CG CD OE1 NE2
REMARK 480 ASP B 130 CB CG OD1 OD2
REMARK 480 ILE B 131 CB CG1 CG2 CD1
REMARK 480 LEU B 132 CG CD1 CD2
REMARK 480 LYS B 133 CB CG CD CE NZ
REMARK 480 LEU B 134 CG CD1 CD2
REMARK 480 GLU B 135 CG CD OE1 OE2
REMARK 480 LYS B 137 CB CG CD CE NZ
REMARK 480 THR B 138 C O CB OG1 CG2
REMARK 480 THR B 145 CB OG1 CG2
REMARK 480 GLU B 148 CB CG CD OE1 OE2
REMARK 480 LEU B 150 CD1 CD2
REMARK 480 LYS B 151 CG CD CE NZ
REMARK 480 GLN B 152 CG CD OE1 NE2
REMARK 480 ILE B 154 CG1 CG2 CD1
REMARK 480 GLU B 156 CG CD OE1 OE2
REMARK 480 LYS B 160 CE NZ
REMARK 480 LYS B 162 CD CE NZ
REMARK 480 ARG B 181 CD NE CZ NH1 NH2
REMARK 480 LEU B 227 CG CD1 CD2
REMARK 480 GLU B 228 CD OE1 OE2
REMARK 480 GLU B 230 CG CD OE1 OE2
REMARK 480 SER B 231 CB OG
REMARK 480 ILE B 233 CG1 CG2 CD1
REMARK 480 LYS B 235 CB CG CD CE NZ
REMARK 480 GLN C 7 CG CD OE1 NE2
REMARK 480 GLN C 8 CG CD OE1 NE2
REMARK 480 GLN C 42 CD OE1 NE2
REMARK 480 LYS C 74 CD CE NZ
REMARK 480 LYS C 122 CE NZ
REMARK 480 ARG C 128 NE CZ NH1 NH2
REMARK 480 LYS C 133 CD CE NZ
REMARK 480 LYS C 137 CG CD CE NZ
REMARK 480 ARG C 139 CG CD NE CZ NH1 NH2
REMARK 480 LYS C 144 CB CG CD CE NZ
REMARK 480 GLU C 148 CG CD OE1 OE2
REMARK 480 LYS C 151 CG CD CE NZ
REMARK 480 GLN C 152 CG CD OE1 NE2
REMARK 480 LYS C 162 CD CE NZ
REMARK 480 LEU C 227 CG CD1 CD2
REMARK 480 GLU C 228 CG CD OE1 OE2
REMARK 480 LYS C 235 CG CD CE NZ
REMARK 480 GLU D 71 CG CD OE1 OE2
REMARK 480 LYS D 74 CD CE NZ
REMARK 480 GLU D 107 CD
REMARK 480 LYS D 118 CD CE NZ
REMARK 480 LYS D 121 CG CD CE NZ
REMARK 480 LYS D 122 CD CE NZ
REMARK 480 LYS D 137 CE NZ
REMARK 480 LYS D 144 CB CG CD CE NZ
REMARK 480 THR D 145 CB OG1 CG2
REMARK 480 GLU D 148 CG CD OE1 OE2
REMARK 480 VAL D 149 CB CG1 CG2
REMARK 480 LYS D 151 CD CE NZ
REMARK 480 GLN D 152 CG CD OE1 NE2
REMARK 480 LEU D 227 CG CD1 CD2
REMARK 480 LYS D 235 CG CD CE NZ
REMARK 480 GLU D 237 CG CD OE1 OE2
REMARK 480 ARG D 238 CD NE CZ NH1 NH2
REMARK 480 THR D 239 CB OG1 CG2
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 NZ LYS D 207 O HOH D 471 1.82
REMARK 500 O HOH C 500 O HOH D 475 1.97
REMARK 500 O HOH A 315 O HOH A 334 1.98
REMARK 500 OD2 ASP C 108 O HOH C 485 2.01
REMARK 500 O ACT D 301 O HOH D 491 2.02
REMARK 500 NE2 GLN D 49 O HOH D 435 2.06
REMARK 500 NZ LYS C 151 O HOH C 517 2.07
REMARK 500 O HOH D 450 O HOH D 467 2.08
REMARK 500 O HOH C 497 O HOH D 406 2.11
REMARK 500 OE2 GLU D 197 O HOH D 493 2.18
REMARK 500 NH1 ARG C 216 O HOH C 432 2.19
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 LYS A 140 35.05 -92.15
REMARK 500 VAL B 24 -60.98 -104.53
REMARK 500 GLN B 129 -73.06 -61.50
REMARK 500 ASP B 130 9.12 -67.46
REMARK 500 PHE C 98 -62.57 -120.53
REMARK 500 PHE D 98 -62.63 -125.74
REMARK 500 ALA D 141 42.11 -83.73
REMARK 500 LYS D 143 -71.98 -72.87
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 PEG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 302
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS HAVE AMPLIFIED THE GENE FROM GENOMIC DNA OF D.DISCOIDEUM
REMARK 999 AX2 LABORATORY STRAIN AND THE SEQUENCE REPORTED IS PRESENT IN THE
REMARK 999 STRAINS USED IN THE PRESENT WORK. THE GENOME DATA IN THE DATABASES
REMARK 999 REFER TO LAB STRAIN AX4. (E.G. DICTYBASE)
DBREF 4NQI A 2 259 UNP C7FZZ0 C7FZZ0_DICDI 2 259
DBREF 4NQI B 2 259 UNP C7FZZ0 C7FZZ0_DICDI 2 259
DBREF 4NQI C 2 259 UNP C7FZZ0 C7FZZ0_DICDI 2 259
DBREF 4NQI D 2 259 UNP C7FZZ0 C7FZZ0_DICDI 2 259
SEQADV 4NQI GLY A -4 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI PRO A -3 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI LEU A -2 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI GLY A -1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI SER A 0 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI MSE A 1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI VAL A 11 UNP C7FZZ0 GLY 11 SEE REMARK 999
SEQADV 4NQI GLY B -4 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI PRO B -3 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI LEU B -2 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI GLY B -1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI SER B 0 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI MSE B 1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI VAL B 11 UNP C7FZZ0 GLY 11 SEE REMARK 999
SEQADV 4NQI GLY C -4 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI PRO C -3 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI LEU C -2 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI GLY C -1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI SER C 0 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI MSE C 1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI VAL C 11 UNP C7FZZ0 GLY 11 SEE REMARK 999
SEQADV 4NQI GLY D -4 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI PRO D -3 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI LEU D -2 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI GLY D -1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI SER D 0 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI MSE D 1 UNP C7FZZ0 EXPRESSION TAG
SEQADV 4NQI VAL D 11 UNP C7FZZ0 GLY 11 SEE REMARK 999
SEQRES 1 A 264 GLY PRO LEU GLY SER MSE SER ASN ALA LYS LYS GLN GLN
SEQRES 2 A 264 ASN PRO VAL ILE GLU ILE THR LEU LYS THR ILE ASN ASN
SEQRES 3 A 264 LEU LYS VAL ASN SER PRO PRO LEU PHE THR GLU VAL ILE
SEQRES 4 A 264 LYS ALA ALA ASN LYS TYR GLN GLN GLN ALA GLN ALA LEU
SEQRES 5 A 264 SER GLN ALA GLY LEU VAL LEU ALA ASP THR LEU THR ARG
SEQRES 6 A 264 LEU THR ILE HIS ASN GLY GLY ASP PHE GLY GLU GLY PHE
SEQRES 7 A 264 LYS LYS LEU ALA ASP ALA ILE LYS ASP LEU GLU ASN ARG
SEQRES 8 A 264 ARG ASP ASP VAL ALA LYS VAL LEU LEU ASN GLU PHE ILE
SEQRES 9 A 264 THR PRO ASN LYS GLN ALA ILE GLU ASP ASP GLN LYS ALA
SEQRES 10 A 264 ILE ALA THR PHE GLU LYS ASN TYR LYS LYS ASP ARG ASP
SEQRES 11 A 264 GLN MSE ARG GLN ASP ILE LEU LYS LEU GLU ALA LYS THR
SEQRES 12 A 264 ARG LYS ALA GLY LYS LYS THR THR PRO GLU VAL LEU LYS
SEQRES 13 A 264 GLN GLN ILE THR GLU LEU ASN ASP LYS ILE LYS GLU SER
SEQRES 14 A 264 GLU GLN LEU ASN ALA ASN LYS LEU ARG ASP VAL VAL LEU
SEQRES 15 A 264 MSE GLU ARG ARG LYS HIS ALA THR PHE LEU SER GLN PHE
SEQRES 16 A 264 ASN GLN PHE LEU GLU LYS GLU ILE GLU LEU SER ALA ASP
SEQRES 17 A 264 THR MSE SER LYS PHE SER THR ASN LEU ASN THR HIS ARG
SEQRES 18 A 264 ASP LEU ILE ASN SER GLN SER GLN LEU PRO LEU GLU MSE
SEQRES 19 A 264 GLU SER MSE ILE SER LYS GLN GLU ARG THR LEU VAL GLN
SEQRES 20 A 264 ILE GLN PRO GLN GLY ASP THR GLY SER ASP ALA TYR ARG
SEQRES 21 A 264 ILE SER TYR ALA
SEQRES 1 B 264 GLY PRO LEU GLY SER MSE SER ASN ALA LYS LYS GLN GLN
SEQRES 2 B 264 ASN PRO VAL ILE GLU ILE THR LEU LYS THR ILE ASN ASN
SEQRES 3 B 264 LEU LYS VAL ASN SER PRO PRO LEU PHE THR GLU VAL ILE
SEQRES 4 B 264 LYS ALA ALA ASN LYS TYR GLN GLN GLN ALA GLN ALA LEU
SEQRES 5 B 264 SER GLN ALA GLY LEU VAL LEU ALA ASP THR LEU THR ARG
SEQRES 6 B 264 LEU THR ILE HIS ASN GLY GLY ASP PHE GLY GLU GLY PHE
SEQRES 7 B 264 LYS LYS LEU ALA ASP ALA ILE LYS ASP LEU GLU ASN ARG
SEQRES 8 B 264 ARG ASP ASP VAL ALA LYS VAL LEU LEU ASN GLU PHE ILE
SEQRES 9 B 264 THR PRO ASN LYS GLN ALA ILE GLU ASP ASP GLN LYS ALA
SEQRES 10 B 264 ILE ALA THR PHE GLU LYS ASN TYR LYS LYS ASP ARG ASP
SEQRES 11 B 264 GLN MSE ARG GLN ASP ILE LEU LYS LEU GLU ALA LYS THR
SEQRES 12 B 264 ARG LYS ALA GLY LYS LYS THR THR PRO GLU VAL LEU LYS
SEQRES 13 B 264 GLN GLN ILE THR GLU LEU ASN ASP LYS ILE LYS GLU SER
SEQRES 14 B 264 GLU GLN LEU ASN ALA ASN LYS LEU ARG ASP VAL VAL LEU
SEQRES 15 B 264 MSE GLU ARG ARG LYS HIS ALA THR PHE LEU SER GLN PHE
SEQRES 16 B 264 ASN GLN PHE LEU GLU LYS GLU ILE GLU LEU SER ALA ASP
SEQRES 17 B 264 THR MSE SER LYS PHE SER THR ASN LEU ASN THR HIS ARG
SEQRES 18 B 264 ASP LEU ILE ASN SER GLN SER GLN LEU PRO LEU GLU MSE
SEQRES 19 B 264 GLU SER MSE ILE SER LYS GLN GLU ARG THR LEU VAL GLN
SEQRES 20 B 264 ILE GLN PRO GLN GLY ASP THR GLY SER ASP ALA TYR ARG
SEQRES 21 B 264 ILE SER TYR ALA
SEQRES 1 C 264 GLY PRO LEU GLY SER MSE SER ASN ALA LYS LYS GLN GLN
SEQRES 2 C 264 ASN PRO VAL ILE GLU ILE THR LEU LYS THR ILE ASN ASN
SEQRES 3 C 264 LEU LYS VAL ASN SER PRO PRO LEU PHE THR GLU VAL ILE
SEQRES 4 C 264 LYS ALA ALA ASN LYS TYR GLN GLN GLN ALA GLN ALA LEU
SEQRES 5 C 264 SER GLN ALA GLY LEU VAL LEU ALA ASP THR LEU THR ARG
SEQRES 6 C 264 LEU THR ILE HIS ASN GLY GLY ASP PHE GLY GLU GLY PHE
SEQRES 7 C 264 LYS LYS LEU ALA ASP ALA ILE LYS ASP LEU GLU ASN ARG
SEQRES 8 C 264 ARG ASP ASP VAL ALA LYS VAL LEU LEU ASN GLU PHE ILE
SEQRES 9 C 264 THR PRO ASN LYS GLN ALA ILE GLU ASP ASP GLN LYS ALA
SEQRES 10 C 264 ILE ALA THR PHE GLU LYS ASN TYR LYS LYS ASP ARG ASP
SEQRES 11 C 264 GLN MSE ARG GLN ASP ILE LEU LYS LEU GLU ALA LYS THR
SEQRES 12 C 264 ARG LYS ALA GLY LYS LYS THR THR PRO GLU VAL LEU LYS
SEQRES 13 C 264 GLN GLN ILE THR GLU LEU ASN ASP LYS ILE LYS GLU SER
SEQRES 14 C 264 GLU GLN LEU ASN ALA ASN LYS LEU ARG ASP VAL VAL LEU
SEQRES 15 C 264 MSE GLU ARG ARG LYS HIS ALA THR PHE LEU SER GLN PHE
SEQRES 16 C 264 ASN GLN PHE LEU GLU LYS GLU ILE GLU LEU SER ALA ASP
SEQRES 17 C 264 THR MSE SER LYS PHE SER THR ASN LEU ASN THR HIS ARG
SEQRES 18 C 264 ASP LEU ILE ASN SER GLN SER GLN LEU PRO LEU GLU MSE
SEQRES 19 C 264 GLU SER MSE ILE SER LYS GLN GLU ARG THR LEU VAL GLN
SEQRES 20 C 264 ILE GLN PRO GLN GLY ASP THR GLY SER ASP ALA TYR ARG
SEQRES 21 C 264 ILE SER TYR ALA
SEQRES 1 D 264 GLY PRO LEU GLY SER MSE SER ASN ALA LYS LYS GLN GLN
SEQRES 2 D 264 ASN PRO VAL ILE GLU ILE THR LEU LYS THR ILE ASN ASN
SEQRES 3 D 264 LEU LYS VAL ASN SER PRO PRO LEU PHE THR GLU VAL ILE
SEQRES 4 D 264 LYS ALA ALA ASN LYS TYR GLN GLN GLN ALA GLN ALA LEU
SEQRES 5 D 264 SER GLN ALA GLY LEU VAL LEU ALA ASP THR LEU THR ARG
SEQRES 6 D 264 LEU THR ILE HIS ASN GLY GLY ASP PHE GLY GLU GLY PHE
SEQRES 7 D 264 LYS LYS LEU ALA ASP ALA ILE LYS ASP LEU GLU ASN ARG
SEQRES 8 D 264 ARG ASP ASP VAL ALA LYS VAL LEU LEU ASN GLU PHE ILE
SEQRES 9 D 264 THR PRO ASN LYS GLN ALA ILE GLU ASP ASP GLN LYS ALA
SEQRES 10 D 264 ILE ALA THR PHE GLU LYS ASN TYR LYS LYS ASP ARG ASP
SEQRES 11 D 264 GLN MSE ARG GLN ASP ILE LEU LYS LEU GLU ALA LYS THR
SEQRES 12 D 264 ARG LYS ALA GLY LYS LYS THR THR PRO GLU VAL LEU LYS
SEQRES 13 D 264 GLN GLN ILE THR GLU LEU ASN ASP LYS ILE LYS GLU SER
SEQRES 14 D 264 GLU GLN LEU ASN ALA ASN LYS LEU ARG ASP VAL VAL LEU
SEQRES 15 D 264 MSE GLU ARG ARG LYS HIS ALA THR PHE LEU SER GLN PHE
SEQRES 16 D 264 ASN GLN PHE LEU GLU LYS GLU ILE GLU LEU SER ALA ASP
SEQRES 17 D 264 THR MSE SER LYS PHE SER THR ASN LEU ASN THR HIS ARG
SEQRES 18 D 264 ASP LEU ILE ASN SER GLN SER GLN LEU PRO LEU GLU MSE
SEQRES 19 D 264 GLU SER MSE ILE SER LYS GLN GLU ARG THR LEU VAL GLN
SEQRES 20 D 264 ILE GLN PRO GLN GLY ASP THR GLY SER ASP ALA TYR ARG
SEQRES 21 D 264 ILE SER TYR ALA
MODRES 4NQI MSE A 127 MET SELENOMETHIONINE
MODRES 4NQI MSE A 178 MET SELENOMETHIONINE
MODRES 4NQI MSE A 205 MET SELENOMETHIONINE
MODRES 4NQI MSE A 229 MET SELENOMETHIONINE
MODRES 4NQI MSE A 232 MET SELENOMETHIONINE
MODRES 4NQI MSE B 127 MET SELENOMETHIONINE
MODRES 4NQI MSE B 178 MET SELENOMETHIONINE
MODRES 4NQI MSE B 205 MET SELENOMETHIONINE
MODRES 4NQI MSE B 229 MET SELENOMETHIONINE
MODRES 4NQI MSE B 232 MET SELENOMETHIONINE
MODRES 4NQI MSE C 127 MET SELENOMETHIONINE
MODRES 4NQI MSE C 178 MET SELENOMETHIONINE
MODRES 4NQI MSE C 205 MET SELENOMETHIONINE
MODRES 4NQI MSE C 229 MET SELENOMETHIONINE
MODRES 4NQI MSE C 232 MET SELENOMETHIONINE
MODRES 4NQI MSE D 127 MET SELENOMETHIONINE
MODRES 4NQI MSE D 178 MET SELENOMETHIONINE
MODRES 4NQI MSE D 205 MET SELENOMETHIONINE
MODRES 4NQI MSE D 229 MET SELENOMETHIONINE
MODRES 4NQI MSE D 232 MET SELENOMETHIONINE
HET MSE A 127 8
HET MSE A 178 8
HET MSE A 205 8
HET MSE A 229 8
HET MSE A 232 8
HET MSE B 127 8
HET MSE B 178 8
HET MSE B 205 8
HET MSE B 229 8
HET MSE B 232 8
HET MSE C 127 8
HET MSE C 178 8
HET MSE C 205 8
HET MSE C 229 8
HET MSE C 232 8
HET MSE D 127 8
HET MSE D 178 8
HET MSE D 205 8
HET MSE D 229 8
HET MSE D 232 8
HET PEG B 301 7
HET PEG B 302 7
HET PEG C 301 7
HET ACT D 301 4
HET ACT D 302 4
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ACT ACETATE ION
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 5 PEG 3(C4 H10 O3)
FORMUL 8 ACT 2(C2 H3 O2 1-)
FORMUL 10 HOH *276(H2 O)
HELIX 1 1 ASN A 9 VAL A 24 1 16
HELIX 2 2 ASN A 25 ARG A 60 1 36
HELIX 3 3 LEU A 61 ILE A 63 5 3
HELIX 4 4 GLY A 66 PHE A 98 1 33
HELIX 5 5 PHE A 98 ALA A 136 1 39
HELIX 6 6 LYS A 137 GLY A 142 5 6
HELIX 7 7 THR A 155 SER A 221 1 67
HELIX 8 8 PRO A 226 GLU A 237 1 12
HELIX 9 9 PRO B 10 VAL B 24 1 15
HELIX 10 10 ASN B 25 ARG B 60 1 36
HELIX 11 11 LEU B 61 HIS B 64 5 4
HELIX 12 12 GLY B 66 PHE B 98 1 33
HELIX 13 13 PHE B 98 ALA B 136 1 39
HELIX 14 14 THR B 146 ASN B 220 1 75
HELIX 15 15 PRO B 226 GLN B 236 1 11
HELIX 16 16 ASN C 9 VAL C 24 1 16
HELIX 17 17 ASN C 25 ARG C 60 1 36
HELIX 18 18 LEU C 61 HIS C 64 5 4
HELIX 19 19 GLY C 66 PHE C 98 1 33
HELIX 20 20 PHE C 98 THR C 138 1 41
HELIX 21 21 THR C 146 ASN C 220 1 75
HELIX 22 22 PRO C 226 GLU C 237 1 12
HELIX 23 23 ASN D 9 VAL D 24 1 16
HELIX 24 24 ASN D 25 ARG D 60 1 36
HELIX 25 25 LEU D 61 ILE D 63 5 3
HELIX 26 26 GLY D 66 PHE D 98 1 33
HELIX 27 27 PHE D 98 LYS D 144 1 47
HELIX 28 28 THR D 146 SER D 221 1 76
HELIX 29 29 PRO D 226 GLU D 237 1 12
LINK C GLN A 126 N MSE A 127 1555 1555 1.33
LINK C MSE A 127 N ARG A 128 1555 1555 1.33
LINK C LEU A 177 N MSE A 178 1555 1555 1.33
LINK C MSE A 178 N GLU A 179 1555 1555 1.33
LINK C THR A 204 N MSE A 205 1555 1555 1.33
LINK C MSE A 205 N SER A 206 1555 1555 1.33
LINK C GLU A 228 N MSE A 229 1555 1555 1.33
LINK C MSE A 229 N GLU A 230 1555 1555 1.33
LINK C SER A 231 N MSE A 232 1555 1555 1.33
LINK C MSE A 232 N ILE A 233 1555 1555 1.33
LINK C GLN B 126 N MSE B 127 1555 1555 1.33
LINK C MSE B 127 N ARG B 128 1555 1555 1.33
LINK C LEU B 177 N MSE B 178 1555 1555 1.33
LINK C MSE B 178 N GLU B 179 1555 1555 1.33
LINK C THR B 204 N MSE B 205 1555 1555 1.33
LINK C MSE B 205 N SER B 206 1555 1555 1.33
LINK C GLU B 228 N MSE B 229 1555 1555 1.33
LINK C MSE B 229 N GLU B 230 1555 1555 1.33
LINK C SER B 231 N MSE B 232 1555 1555 1.33
LINK C MSE B 232 N ILE B 233 1555 1555 1.33
LINK C GLN C 126 N MSE C 127 1555 1555 1.33
LINK C MSE C 127 N ARG C 128 1555 1555 1.33
LINK C LEU C 177 N MSE C 178 1555 1555 1.34
LINK C MSE C 178 N GLU C 179 1555 1555 1.33
LINK C THR C 204 N MSE C 205 1555 1555 1.33
LINK C MSE C 205 N SER C 206 1555 1555 1.33
LINK C GLU C 228 N MSE C 229 1555 1555 1.33
LINK C MSE C 229 N GLU C 230 1555 1555 1.33
LINK C SER C 231 N MSE C 232 1555 1555 1.33
LINK C MSE C 232 N ILE C 233 1555 1555 1.33
LINK C GLN D 126 N MSE D 127 1555 1555 1.33
LINK C MSE D 127 N ARG D 128 1555 1555 1.33
LINK C LEU D 177 N MSE D 178 1555 1555 1.33
LINK C MSE D 178 N GLU D 179 1555 1555 1.33
LINK C THR D 204 N MSE D 205 1555 1555 1.33
LINK C MSE D 205 N SER D 206 1555 1555 1.33
LINK C GLU D 228 N MSE D 229 1555 1555 1.33
LINK C MSE D 229 N GLU D 230 1555 1555 1.33
LINK C SER D 231 N MSE D 232 1555 1555 1.33
LINK C MSE D 232 N ILE D 233 1555 1555 1.33
SITE 1 AC1 5 ARG A 87 GLU A 197 ARG B 87 GLU B 197
SITE 2 AC1 5 LEU B 200
SITE 1 AC2 7 ASN B 102 ALA B 105 ASP B 109 LYS B 182
SITE 2 AC2 7 THR B 185 PHE B 186 HOH B 408
SITE 1 AC3 6 ASN B 213 LYS C 23 VAL C 24 PRO C 27
SITE 2 AC3 6 PRO C 28 THR C 31
SITE 1 AC4 3 ARG D 60 HIS D 64 HOH D 491
SITE 1 AC5 7 HIS C 183 ASN D 65 GLY D 66 ASP D 68
SITE 2 AC5 7 PHE D 69 HOH D 423 HOH D 473
CRYST1 59.100 60.210 147.620 90.00 100.38 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.016920 0.000000 0.003100 0.00000
SCALE2 0.000000 0.016609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006887 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
