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HEADER HYDROLASE 25-SEP-18 6IGQ
TITLE CRYSTAL STRUCTURE OF INACTIVE STATE OF S9 PEPTIDASE FROM DEINOCOCCUS
TITLE 2 RADIODURANS R1 (PMSF TREATED)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PEPTIDE HYDROLASE, PUTATIVE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS STR. R1;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1;
SOURCE 5 GENE: DR_0165;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PST50TR
KEYWDS SERINE PEPTIDASE, MEROPS S9, POP FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.YADAV,V.D.GOYAL,A.KUMAR,R.D.MAKDE
REVDAT 1 14-NOV-18 6IGQ 0
JRNL AUTH P.YADAV,V.D.GOYAL,A.KUMAR,R.D.MAKDE
JRNL TITL CRYSTAL STRUCTURE OF INACTIVE STATE OF S9 PEPTIDASE FROM
JRNL TITL 2 DEINOCOCCUS RADIODURANS R1 IN AMMONIUM SULPHATE CONDITION
JRNL TITL 3 (CONDITION 3)
JRNL REF J.BIOL.CHEM. 2018
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 134499
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6737
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.8782 - 7.1334 0.98 4480 232 0.1724 0.1945
REMARK 3 2 7.1334 - 5.6672 1.00 4373 223 0.1833 0.2150
REMARK 3 3 5.6672 - 4.9524 1.00 4346 232 0.1540 0.1878
REMARK 3 4 4.9524 - 4.5002 1.00 4277 272 0.1478 0.1808
REMARK 3 5 4.5002 - 4.1780 1.00 4277 244 0.1488 0.1743
REMARK 3 6 4.1780 - 3.9319 1.00 4242 265 0.1640 0.2023
REMARK 3 7 3.9319 - 3.7352 1.00 4264 235 0.1786 0.1951
REMARK 3 8 3.7352 - 3.5727 1.00 4272 246 0.1749 0.1935
REMARK 3 9 3.5727 - 3.4352 1.00 4263 223 0.1878 0.2318
REMARK 3 10 3.4352 - 3.3168 1.00 4269 206 0.1971 0.2261
REMARK 3 11 3.3168 - 3.2131 1.00 4243 233 0.2049 0.2364
REMARK 3 12 3.2131 - 3.1213 1.00 4251 229 0.1995 0.2539
REMARK 3 13 3.1213 - 3.0391 1.00 4252 217 0.1985 0.2461
REMARK 3 14 3.0391 - 2.9650 1.00 4257 206 0.2031 0.2262
REMARK 3 15 2.9650 - 2.8976 1.00 4223 222 0.2022 0.2670
REMARK 3 16 2.8976 - 2.8360 1.00 4257 220 0.2061 0.2211
REMARK 3 17 2.8360 - 2.7793 1.00 4276 182 0.2177 0.2510
REMARK 3 18 2.7793 - 2.7268 1.00 4221 217 0.2098 0.2565
REMARK 3 19 2.7268 - 2.6781 1.00 4261 215 0.2199 0.2567
REMARK 3 20 2.6781 - 2.6328 1.00 4263 199 0.2254 0.2544
REMARK 3 21 2.6328 - 2.5903 1.00 4216 217 0.2214 0.2612
REMARK 3 22 2.5903 - 2.5505 1.00 4192 224 0.2248 0.2686
REMARK 3 23 2.5505 - 2.5130 1.00 4254 236 0.2252 0.2908
REMARK 3 24 2.5130 - 2.4776 1.00 4201 226 0.2282 0.2556
REMARK 3 25 2.4776 - 2.4441 1.00 4232 207 0.2273 0.2494
REMARK 3 26 2.4441 - 2.4123 1.00 4262 216 0.2343 0.2654
REMARK 3 27 2.4123 - 2.3822 1.00 4220 203 0.2434 0.2768
REMARK 3 28 2.3822 - 2.3535 1.00 4205 208 0.2454 0.2902
REMARK 3 29 2.3535 - 2.3261 1.00 4202 235 0.2491 0.3009
REMARK 3 30 2.3261 - 2.3000 1.00 4211 247 0.2549 0.2763
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
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 : 0.006 18795
REMARK 3 ANGLE : 0.810 25645
REMARK 3 CHIRALITY : 0.051 2695
REMARK 3 PLANARITY : 0.006 3389
REMARK 3 DIHEDRAL : 3.692 12788
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7989 -22.0786 48.3392
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.1981
REMARK 3 T33: 0.2607 T12: -0.0080
REMARK 3 T13: 0.0030 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: -0.0280 L22: -0.0243
REMARK 3 L33: 0.1716 L12: -0.0160
REMARK 3 L13: 0.0483 L23: 0.0061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: -0.0022 S13: -0.0173
REMARK 3 S21: -0.0025 S22: -0.0126 S23: -0.0024
REMARK 3 S31: 0.0222 S32: -0.0393 S33: 0.0353
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 6IGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1300009158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8-5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : RRCAT INDUS-2
REMARK 200 BEAMLINE : PX-BL21
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97947
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : MIRRORS
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 : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134697
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 39.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.99700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5YZM
REMARK 200
REMARK 200 REMARK: CUBIOD CRYSTALS (150-200 MICRON)
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M AMMONIUM SULPHATE, 25.5% PEG
REMARK 280 4000, 15% GLYCEROL, PH 5.31, MICROBATCH, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 59.82900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 97.06500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.99450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 97.06500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.82900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.99450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 82820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 SER A 40
REMARK 465 GLU A 41
REMARK 465 GLU A 42
REMARK 465 ASP A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 LYS A 46
REMARK 465 PRO A 47
REMARK 465 ASP A 48
REMARK 465 LYS A 49
REMARK 465 ASP A 50
REMARK 465 PHE A 51
REMARK 465 ALA A 52
REMARK 465 ARG A 53
REMARK 465 GLY A 99
REMARK 465 GLU A 100
REMARK 465 THR A 145
REMARK 465 GLU A 146
REMARK 465 ASP A 147
REMARK 465 LYS A 148
REMARK 465 ARG A 149
REMARK 465 ASP A 150
REMARK 465 GLU A 151
REMARK 465 ARG A 152
REMARK 465 GLY A 153
REMARK 465 GLU A 154
REMARK 465 ALA A 155
REMARK 465 ARG A 156
REMARK 465 VAL A 157
REMARK 465 LEU A 158
REMARK 465 THR A 159
REMARK 465 ARG A 160
REMARK 465 PRO A 161
REMARK 465 VAL A 162
REMARK 465 TYR A 163
REMARK 465 ARG A 164
REMARK 465 ALA A 165
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 ALA A 168
REMARK 465 ASP A 169
REMARK 465 TRP A 170
REMARK 465 LEU A 171
REMARK 465 PRO A 172
REMARK 465 GLU A 173
REMARK 465 ARG A 174
REMARK 465 ALA A 236
REMARK 465 ASP A 237
REMARK 465 ALA A 238
REMARK 465 PRO A 239
REMARK 465 ALA A 240
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 ASN B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 THR B 6
REMARK 465 SER B 40
REMARK 465 GLU B 41
REMARK 465 GLU B 42
REMARK 465 ASP B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 LYS B 46
REMARK 465 PRO B 47
REMARK 465 ASP B 48
REMARK 465 LYS B 49
REMARK 465 ASP B 50
REMARK 465 PHE B 51
REMARK 465 ALA B 52
REMARK 465 ARG B 53
REMARK 465 ALA B 98
REMARK 465 GLY B 99
REMARK 465 GLU B 100
REMARK 465 ALA B 143
REMARK 465 ASP B 144
REMARK 465 THR B 145
REMARK 465 GLU B 146
REMARK 465 ASP B 147
REMARK 465 LYS B 148
REMARK 465 ARG B 149
REMARK 465 ASP B 150
REMARK 465 GLU B 151
REMARK 465 ARG B 152
REMARK 465 GLY B 153
REMARK 465 GLU B 154
REMARK 465 ALA B 155
REMARK 465 ARG B 156
REMARK 465 VAL B 157
REMARK 465 LEU B 158
REMARK 465 THR B 159
REMARK 465 ARG B 160
REMARK 465 PRO B 161
REMARK 465 VAL B 162
REMARK 465 TYR B 163
REMARK 465 ARG B 164
REMARK 465 ALA B 165
REMARK 465 ASN B 166
REMARK 465 GLY B 167
REMARK 465 ALA B 168
REMARK 465 ASP B 169
REMARK 465 TRP B 170
REMARK 465 LEU B 171
REMARK 465 PRO B 172
REMARK 465 GLU B 173
REMARK 465 ARG B 174
REMARK 465 ALA B 236
REMARK 465 ASP B 237
REMARK 465 ALA B 238
REMARK 465 PRO B 239
REMARK 465 ALA B 240
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 ASN C 2
REMARK 465 ASN C 3
REMARK 465 SER C 4
REMARK 465 GLU C 5
REMARK 465 THR C 6
REMARK 465 SER C 40
REMARK 465 GLU C 41
REMARK 465 GLU C 42
REMARK 465 ASP C 43
REMARK 465 PRO C 44
REMARK 465 ALA C 45
REMARK 465 LYS C 46
REMARK 465 PRO C 47
REMARK 465 ASP C 48
REMARK 465 LYS C 49
REMARK 465 ASP C 50
REMARK 465 PHE C 51
REMARK 465 ALA C 52
REMARK 465 ARG C 53
REMARK 465 ALA C 98
REMARK 465 GLY C 99
REMARK 465 GLU C 100
REMARK 465 VAL C 101
REMARK 465 PHE C 121
REMARK 465 LYS C 122
REMARK 465 ASN C 123
REMARK 465 THR C 142
REMARK 465 ALA C 143
REMARK 465 ASP C 144
REMARK 465 THR C 145
REMARK 465 GLU C 146
REMARK 465 ASP C 147
REMARK 465 LYS C 148
REMARK 465 ARG C 149
REMARK 465 ASP C 150
REMARK 465 GLU C 151
REMARK 465 ARG C 152
REMARK 465 GLY C 153
REMARK 465 GLU C 154
REMARK 465 ALA C 155
REMARK 465 ARG C 156
REMARK 465 VAL C 157
REMARK 465 LEU C 158
REMARK 465 THR C 159
REMARK 465 ARG C 160
REMARK 465 PRO C 161
REMARK 465 VAL C 162
REMARK 465 TYR C 163
REMARK 465 ARG C 164
REMARK 465 ALA C 165
REMARK 465 ASN C 166
REMARK 465 GLY C 167
REMARK 465 ALA C 168
REMARK 465 ASP C 169
REMARK 465 TRP C 170
REMARK 465 LEU C 171
REMARK 465 PRO C 172
REMARK 465 GLU C 173
REMARK 465 ARG C 174
REMARK 465 PRO C 175
REMARK 465 GLU C 216
REMARK 465 ASP C 217
REMARK 465 GLU C 218
REMARK 465 TRP C 219
REMARK 465 GLN C 220
REMARK 465 ALA C 236
REMARK 465 ASP C 237
REMARK 465 ALA C 238
REMARK 465 PRO C 239
REMARK 465 ALA C 240
REMARK 465 ALA C 241
REMARK 465 GLY D 0
REMARK 465 SER D 1
REMARK 465 ASN D 2
REMARK 465 ASN D 3
REMARK 465 SER D 4
REMARK 465 GLU D 5
REMARK 465 THR D 6
REMARK 465 SER D 40
REMARK 465 GLU D 41
REMARK 465 GLU D 42
REMARK 465 ASP D 43
REMARK 465 PRO D 44
REMARK 465 ALA D 45
REMARK 465 LYS D 46
REMARK 465 PRO D 47
REMARK 465 ASP D 48
REMARK 465 LYS D 49
REMARK 465 ASP D 50
REMARK 465 PHE D 51
REMARK 465 ALA D 52
REMARK 465 ARG D 53
REMARK 465 ALA D 98
REMARK 465 GLY D 99
REMARK 465 GLU D 100
REMARK 465 VAL D 101
REMARK 465 HIS D 120
REMARK 465 PHE D 121
REMARK 465 LYS D 122
REMARK 465 ASN D 123
REMARK 465 THR D 142
REMARK 465 ALA D 143
REMARK 465 ASP D 144
REMARK 465 THR D 145
REMARK 465 GLU D 146
REMARK 465 ASP D 147
REMARK 465 LYS D 148
REMARK 465 ARG D 149
REMARK 465 ASP D 150
REMARK 465 GLU D 151
REMARK 465 ARG D 152
REMARK 465 GLY D 153
REMARK 465 GLU D 154
REMARK 465 ALA D 155
REMARK 465 ARG D 156
REMARK 465 VAL D 157
REMARK 465 LEU D 158
REMARK 465 THR D 159
REMARK 465 ARG D 160
REMARK 465 PRO D 161
REMARK 465 VAL D 162
REMARK 465 TYR D 163
REMARK 465 ARG D 164
REMARK 465 ALA D 165
REMARK 465 ASN D 166
REMARK 465 GLY D 167
REMARK 465 ALA D 168
REMARK 465 ASP D 169
REMARK 465 TRP D 170
REMARK 465 LEU D 171
REMARK 465 PRO D 172
REMARK 465 GLU D 173
REMARK 465 ARG D 174
REMARK 465 PRO D 175
REMARK 465 THR D 235
REMARK 465 ALA D 236
REMARK 465 ASP D 237
REMARK 465 ALA D 238
REMARK 465 PRO D 239
REMARK 465 ALA D 240
REMARK 465 ALA D 241
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 LYS A 30 CG CD CE NZ
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 GLN A 223 CG CD OE1 NE2
REMARK 470 TRP A 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 224 CZ3 CH2
REMARK 470 GLN A 243 CG CD OE1 NE2
REMARK 470 LYS A 347 CG CD CE NZ
REMARK 470 GLU A 421 CG CD OE1 OE2
REMARK 470 ARG A 554 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 75 CG CD OE1 OE2
REMARK 470 ARG B 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 LYS B 187 CG CD CE NZ
REMARK 470 GLU B 195 CG CD OE1 OE2
REMARK 470 GLU B 216 CG CD OE1 OE2
REMARK 470 GLU B 218 CG CD OE1 OE2
REMARK 470 GLN B 220 CG CD OE1 NE2
REMARK 470 TRP B 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 224 CZ3 CH2
REMARK 470 ARG B 225 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 243 CG CD OE1 NE2
REMARK 470 LYS B 273 CG CD CE NZ
REMARK 470 LYS B 347 CG CD CE NZ
REMARK 470 GLU B 421 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 LYS B 507 CG CD CE NZ
REMARK 470 LYS C 30 CD CE NZ
REMARK 470 ARG C 69 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 102 CG CD CE NZ
REMARK 470 ARG C 116 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 120 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 135 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 184 CG CD OE1 OE2
REMARK 470 LYS C 187 CG CD CE NZ
REMARK 470 GLU C 195 CG CD OE1 OE2
REMARK 470 GLN C 223 CG CD OE1 NE2
REMARK 470 TRP C 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 224 CZ3 CH2
REMARK 470 ARG C 225 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 243 CG CD OE1 NE2
REMARK 470 LYS C 244 CG CD CE NZ
REMARK 470 LEU C 245 CG CD1 CD2
REMARK 470 ASP C 247 CG OD1 OD2
REMARK 470 ARG C 290 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 323 CG OD1 OD2
REMARK 470 LYS C 347 CE NZ
REMARK 470 GLU C 364 CG CD OE1 OE2
REMARK 470 ARG C 376 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 421 CG CD OE1 OE2
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 GLU D 64 CG CD OE1 OE2
REMARK 470 ARG D 69 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 75 CG CD OE1 OE2
REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 102 CG CD CE NZ
REMARK 470 LYS D 111 CG CD CE NZ
REMARK 470 ARG D 116 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 135 CG CD NE CZ NH1 NH2
REMARK 470 THR D 141 OG1 CG2
REMARK 470 TRP D 179 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 179 CZ3 CH2
REMARK 470 GLU D 184 CG CD OE1 OE2
REMARK 470 LYS D 187 CG CD CE NZ
REMARK 470 ARG D 189 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 190 CG CD OE1 OE2
REMARK 470 GLU D 195 CG CD OE1 OE2
REMARK 470 ILE D 196 CG1 CG2 CD1
REMARK 470 GLU D 216 CG CD OE1 OE2
REMARK 470 GLU D 218 CG CD OE1 OE2
REMARK 470 TRP D 219 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 219 CZ3 CH2
REMARK 470 GLN D 220 CG CD OE1 NE2
REMARK 470 GLN D 223 CG CD OE1 NE2
REMARK 470 TRP D 224 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 224 CZ3 CH2
REMARK 470 ARG D 225 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 243 CG CD OE1 NE2
REMARK 470 LEU D 245 CG CD1 CD2
REMARK 470 ASP D 247 CG OD1 OD2
REMARK 470 GLN D 262 CG CD OE1 NE2
REMARK 470 LYS D 273 CG CD CE NZ
REMARK 470 ASN D 286 CG OD1 ND2
REMARK 470 LYS D 347 CE NZ
REMARK 470 ARG D 376 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 399 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 421 CG CD OE1 OE2
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 ALA A 103 87.13 -160.77
REMARK 500 ALA A 143 -130.97 70.35
REMARK 500 GLN A 262 -51.89 -122.03
REMARK 500 ARG A 480 47.68 -150.07
REMARK 500 THR A 483 -91.11 -109.45
REMARK 500 SER A 514 -119.09 60.51
REMARK 500 ALA B 103 88.06 -161.69
REMARK 500 GLN B 262 -54.27 -121.82
REMARK 500 ASP B 293 59.68 -92.13
REMARK 500 ARG B 480 46.66 -149.90
REMARK 500 THR B 483 -92.94 -106.60
REMARK 500 SER B 514 -116.57 60.59
REMARK 500 ALA C 103 89.39 -163.95
REMARK 500 GLN C 262 -55.08 -121.75
REMARK 500 ARG C 480 47.49 -150.66
REMARK 500 THR C 483 -93.89 -107.22
REMARK 500 SER C 514 -117.86 59.36
REMARK 500 ALA D 103 88.33 -168.13
REMARK 500 GLN D 262 -52.44 -120.88
REMARK 500 ARG D 480 47.91 -151.91
REMARK 500 THR D 483 -93.98 -106.21
REMARK 500 SER D 514 -118.46 59.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C1040 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH C1041 DISTANCE = 6.77 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5YZM RELATED DB: PDB
REMARK 900 5YZM CONTAINS THE SAME PROTEIN CRYSTALLIZED IN DIFFERENT
REMARK 900 CRYSTALLIZATION CONDITION
DBREF 6IGQ A 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IGQ B 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IGQ C 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
DBREF 6IGQ D 2 655 UNP Q9RXY9 Q9RXY9_DEIRA 2 655
SEQADV 6IGQ GLY A 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ SER A 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ GLY B 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ SER B 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ GLY C 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ SER C 1 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ GLY D 0 UNP Q9RXY9 EXPRESSION TAG
SEQADV 6IGQ SER D 1 UNP Q9RXY9 EXPRESSION TAG
SEQRES 1 A 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 A 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 A 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 A 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 A 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 A 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 A 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 A 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 A 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 A 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 A 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 A 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 A 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 A 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 A 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 A 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 A 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 A 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 A 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 A 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 A 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 A 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 A 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 A 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 A 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 A 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 A 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 A 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 A 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 A 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 A 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 A 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 A 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 A 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 A 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 A 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 A 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 A 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 A 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 A 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 A 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 A 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 A 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 A 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 A 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 A 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 A 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 A 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 A 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 A 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 A 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 B 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 B 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 B 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 B 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 B 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 B 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 B 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 B 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 B 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 B 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 B 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 B 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 B 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 B 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 B 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 B 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 B 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 B 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 B 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 B 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 B 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 B 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 B 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 B 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 B 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 B 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 B 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 B 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 B 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 B 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 B 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 B 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 B 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 B 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 B 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 B 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 B 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 B 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 B 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 B 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 B 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 B 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 B 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 B 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 B 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 B 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 B 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 B 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 B 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 B 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 B 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 C 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 C 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 C 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 C 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 C 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 C 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 C 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 C 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 C 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 C 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 C 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 C 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 C 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 C 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 C 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 C 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 C 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 C 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 C 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 C 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 C 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 C 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 C 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 C 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 C 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 C 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 C 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 C 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 C 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 C 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 C 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 C 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 C 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 C 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 C 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 C 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 C 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 C 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 C 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 C 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 C 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 C 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 C 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 C 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 C 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 C 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 C 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 C 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 C 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 C 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 C 656 TRP LEU GLU ARG TRP LEU
SEQRES 1 D 656 GLY SER ASN ASN SER GLU THR PRO ALA PRO GLY PRO ASP
SEQRES 2 D 656 SER LEU LEU ALA LEU ALA PHE PRO SER ASP PRO GLN VAL
SEQRES 3 D 656 SER PRO ASP GLY LYS GLN VAL ALA PHE VAL LEU ALA GLN
SEQRES 4 D 656 ILE SER GLU GLU ASP PRO ALA LYS PRO ASP LYS ASP PHE
SEQRES 5 D 656 ALA ARG PRO ARG TYR ARG SER GLY LEU TRP LEU SER GLU
SEQRES 6 D 656 GLY GLY ALA ALA ARG PRO LEU THR HIS ALA GLU THR GLY
SEQRES 7 D 656 ARG GLY ASP SER ALA PRO ARG TRP SER PRO ASP GLY GLN
SEQRES 8 D 656 ASN LEU ALA PHE VAL ARG SER ALA GLY GLU VAL LYS ALA
SEQRES 9 D 656 ALA LEU MET LEU LEU PRO LEU LYS GLY GLY GLU ALA ARG
SEQRES 10 D 656 ARG VAL THR HIS PHE LYS ASN GLY VAL SER GLY PRO GLN
SEQRES 11 D 656 TRP SER PRO ASP GLY ARG PHE ILE ALA PHE THR THR THR
SEQRES 12 D 656 ALA ASP THR GLU ASP LYS ARG ASP GLU ARG GLY GLU ALA
SEQRES 13 D 656 ARG VAL LEU THR ARG PRO VAL TYR ARG ALA ASN GLY ALA
SEQRES 14 D 656 ASP TRP LEU PRO GLU ARG PRO ALA ALA LEU TRP LEU TYR
SEQRES 15 D 656 ASP VAL GLU ALA ASP LYS LEU ARG GLU TRP TYR ALA PRO
SEQRES 16 D 656 GLU ILE GLY ILE GLY ALA LEU SER TRP TRP PRO ASP SER
SEQRES 17 D 656 ARG GLY VAL LEU ILE VAL GLN SER GLU ASP GLU TRP GLN
SEQRES 18 D 656 ALA SER GLN TRP ARG GLN ASP VAL TYR ASP LEU PRO LEU
SEQRES 19 D 656 PRO THR ALA ASP ALA PRO ALA ALA PRO GLN LYS LEU LEU
SEQRES 20 D 656 ASP TRP ASN SER ALA ALA HIS GLY LEU ALA PRO HIS PRO
SEQRES 21 D 656 ASP GLY GLN ARG PHE ALA LEU ILE GLY ARG PRO ALA GLY
SEQRES 22 D 656 LYS GLY ASN THR GLU HIS ALA HIS LEU TYR LEU ILE GLU
SEQRES 23 D 656 ASN GLY GLN HIS ARG ARG LEU ASP THR GLY HIS ASP HIS
SEQRES 24 D 656 PRO VAL GLY ASP ALA VAL GLY GLY ASP CYS HIS VAL GLY
SEQRES 25 D 656 ALA PHE PRO GLU GLY PRO ARG TRP LEU ASP GLY ASP THR
SEQRES 26 D 656 LEU LEU PHE SER SER THR VAL ARG GLY SER VAL GLY LEU
SEQRES 27 D 656 PHE THR ALA HIS ILE GLY GLY GLY VAL LYS ALA TYR ASP
SEQRES 28 D 656 HIS ASP PRO GLN GLY VAL ILE SER ALA PHE THR ALA ASN
SEQRES 29 D 656 GLU HIS GLY VAL ALA LEU ILE ARG GLU SER ALA THR ARG
SEQRES 30 D 656 PHE PRO GLU VAL GLU LEU ASN GLY GLN ARG VAL THR ASP
SEQRES 31 D 656 LEU HIS ALA ARG PHE PRO PHE PRO VAL ARG GLU PRO GLN
SEQRES 32 D 656 ARG VAL THR PHE GLU THR GLU LEU GLY GLU GLY GLU GLY
SEQRES 33 D 656 TRP VAL LEU LEU PRO GLU GLY GLU GLN LYS VAL PRO ALA
SEQRES 34 D 656 LEU LEU ASN ILE HIS GLY GLY PRO HIS THR ASP TYR GLY
SEQRES 35 D 656 HIS GLY PHE THR HIS GLU PHE GLN LEU MET ALA ALA ARG
SEQRES 36 D 656 GLY TYR GLY VAL CYS TYR SER ASN PRO ARG GLY SER VAL
SEQRES 37 D 656 GLY TYR GLY GLN ALA TRP VAL ASP ALA ILE TYR GLY ARG
SEQRES 38 D 656 TRP GLY THR VAL ASP ALA ASP ASP LEU LEU ASN PHE PHE
SEQRES 39 D 656 ASP ARG CYS LEU GLU ALA VAL PRO ARG LEU ASP ALA ALA
SEQRES 40 D 656 LYS THR ALA VAL MET GLY GLY SER TYR GLY GLY PHE MET
SEQRES 41 D 656 THR ASN TRP ILE THR GLY HIS THR THR ARG PHE GLN ALA
SEQRES 42 D 656 ALA ILE THR ASP ARG CYS ILE SER ASN LEU ILE SER PHE
SEQRES 43 D 656 GLY GLY THR SER ASP ILE GLY LEU ARG PHE TRP ASP ASP
SEQRES 44 D 656 GLU LEU GLY LEU ASP PHE SER ARG ARG ALA ASP ALA LEU
SEQRES 45 D 656 LYS LEU TRP ASP LEU SER PRO LEU GLN TYR VAL GLU ASN
SEQRES 46 D 656 VAL LYS THR PRO THR LEU ILE VAL HIS SER VAL LEU ASP
SEQRES 47 D 656 HIS ARG CYS PRO VAL GLU GLN ALA GLU GLN TRP TYR ALA
SEQRES 48 D 656 ALA LEU HIS LYS HIS GLN VAL PRO VAL ARG PHE VAL ARG
SEQRES 49 D 656 PHE PRO GLU GLU ASN HIS GLU LEU SER ARG SER GLY ARG
SEQRES 50 D 656 PRO ASP ARG ARG LEU THR ARG LEU ASN GLU TYR PHE ALA
SEQRES 51 D 656 TRP LEU GLU ARG TRP LEU
HET GOL A 701 6
HET GOL A 702 6
HET GOL A 703 6
HET SO4 A 704 5
HET GOL B 701 6
HET GOL B 702 6
HET GOL B 703 6
HET SO4 B 704 5
HET GOL C 701 6
HET GOL C 702 6
HET SO4 C 703 5
HET GOL D 701 6
HET GOL D 702 6
HET GOL D 703 6
HET SO4 D 704 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 11(C3 H8 O3)
FORMUL 8 SO4 4(O4 S 2-)
FORMUL 20 HOH *992(H2 O)
HELIX 1 AA1 GLY A 10 LEU A 17 5 8
HELIX 2 AA2 ASP A 217 GLN A 223 1 7
HELIX 3 AA3 LEU A 390 PHE A 394 5 5
HELIX 4 AA4 THR A 445 ARG A 454 1 10
HELIX 5 AA5 GLY A 470 ALA A 476 1 7
HELIX 6 AA6 THR A 483 VAL A 500 1 18
HELIX 7 AA7 SER A 514 GLY A 525 1 12
HELIX 8 AA8 ASN A 541 SER A 549 1 9
HELIX 9 AA9 ILE A 551 GLY A 561 1 11
HELIX 10 AB1 ARG A 566 LEU A 576 1 11
HELIX 11 AB2 SER A 577 VAL A 585 5 9
HELIX 12 AB3 VAL A 602 HIS A 615 1 14
HELIX 13 AB4 HIS A 629 GLY A 635 1 7
HELIX 14 AB5 PRO A 637 LEU A 655 1 19
HELIX 15 AB6 GLY B 10 LEU B 17 5 8
HELIX 16 AB7 ASP B 217 GLN B 223 1 7
HELIX 17 AB8 LEU B 390 PHE B 394 5 5
HELIX 18 AB9 THR B 445 ARG B 454 1 10
HELIX 19 AC1 GLY B 470 ALA B 476 1 7
HELIX 20 AC2 THR B 483 VAL B 500 1 18
HELIX 21 AC3 SER B 514 GLY B 525 1 12
HELIX 22 AC4 ASN B 541 SER B 549 1 9
HELIX 23 AC5 ILE B 551 GLY B 561 1 11
HELIX 24 AC6 ARG B 566 LEU B 576 1 11
HELIX 25 AC7 SER B 577 VAL B 585 5 9
HELIX 26 AC8 VAL B 602 HIS B 615 1 14
HELIX 27 AC9 HIS B 629 GLY B 635 1 7
HELIX 28 AD1 PRO B 637 LEU B 655 1 19
HELIX 29 AD2 GLY C 10 LEU C 17 5 8
HELIX 30 AD3 LEU C 390 PHE C 394 5 5
HELIX 31 AD4 THR C 445 ARG C 454 1 10
HELIX 32 AD5 GLY C 470 ALA C 476 1 7
HELIX 33 AD6 THR C 483 VAL C 500 1 18
HELIX 34 AD7 SER C 514 GLY C 525 1 12
HELIX 35 AD8 ASN C 541 SER C 549 1 9
HELIX 36 AD9 ILE C 551 GLY C 561 1 11
HELIX 37 AE1 ARG C 566 LEU C 576 1 11
HELIX 38 AE2 SER C 577 VAL C 585 5 9
HELIX 39 AE3 VAL C 602 HIS C 615 1 14
HELIX 40 AE4 HIS C 629 GLY C 635 1 7
HELIX 41 AE5 PRO C 637 LEU C 655 1 19
HELIX 42 AE6 GLY D 10 LEU D 17 5 8
HELIX 43 AE7 ASP D 217 GLN D 223 1 7
HELIX 44 AE8 LEU D 390 PHE D 394 5 5
HELIX 45 AE9 THR D 445 ARG D 454 1 10
HELIX 46 AF1 GLY D 470 ALA D 476 1 7
HELIX 47 AF2 THR D 483 VAL D 500 1 18
HELIX 48 AF3 SER D 514 GLY D 525 1 12
HELIX 49 AF4 ASN D 541 SER D 549 1 9
HELIX 50 AF5 ILE D 551 GLY D 561 1 11
HELIX 51 AF6 ARG D 566 LEU D 576 1 11
HELIX 52 AF7 SER D 577 VAL D 585 5 9
HELIX 53 AF8 VAL D 602 HIS D 615 1 14
HELIX 54 AF9 HIS D 629 GLY D 635 1 7
HELIX 55 AG1 PRO D 637 LEU D 655 1 19
SHEET 1 AA1 4 PHE A 19 VAL A 25 0
SHEET 2 AA1 4 VAL A 32 GLN A 38 -1 O VAL A 35 N SER A 21
SHEET 3 AA1 4 ARG A 57 SER A 63 -1 O TRP A 61 N PHE A 34
SHEET 4 AA1 4 ARG A 69 PRO A 70 -1 O ARG A 69 N LEU A 62
SHEET 1 AA2 4 GLY A 79 TRP A 85 0
SHEET 2 AA2 4 ASN A 91 SER A 97 -1 O VAL A 95 N SER A 81
SHEET 3 AA2 4 ALA A 104 PRO A 109 -1 O MET A 106 N PHE A 94
SHEET 4 AA2 4 ARG A 116 ARG A 117 -1 O ARG A 116 N LEU A 107
SHEET 1 AA3 4 VAL A 125 TRP A 130 0
SHEET 2 AA3 4 PHE A 136 THR A 141 -1 O ALA A 138 N GLN A 129
SHEET 3 AA3 4 ALA A 177 ASP A 182 -1 O TRP A 179 N PHE A 139
SHEET 4 AA3 4 LYS A 187 TYR A 192 -1 O LYS A 187 N ASP A 182
SHEET 1 AA4 4 LEU A 201 TRP A 203 0
SHEET 2 AA4 4 GLY A 209 GLN A 214 -1 O LEU A 211 N SER A 202
SHEET 3 AA4 4 GLN A 226 PRO A 232 -1 O TYR A 229 N ILE A 212
SHEET 4 AA4 4 GLN A 243 SER A 250 -1 O GLN A 243 N ASP A 230
SHEET 1 AA5 4 ALA A 252 PRO A 257 0
SHEET 2 AA5 4 PHE A 264 GLY A 268 -1 O ALA A 265 N ALA A 256
SHEET 3 AA5 4 HIS A 280 GLU A 285 -1 O ILE A 284 N PHE A 264
SHEET 4 AA5 4 GLN A 288 ARG A 291 -1 O ARG A 290 N LEU A 283
SHEET 1 AA6 4 ARG A 318 TRP A 319 0
SHEET 2 AA6 4 THR A 324 VAL A 331 -1 O LEU A 326 N ARG A 318
SHEET 3 AA6 4 SER A 334 HIS A 341 -1 O PHE A 338 N PHE A 327
SHEET 4 AA6 4 GLY A 344 ASP A 350 -1 O ASP A 350 N LEU A 337
SHEET 1 AA7 4 GLY A 355 ASN A 363 0
SHEET 2 AA7 4 GLY A 366 SER A 373 -1 O GLU A 372 N VAL A 356
SHEET 3 AA7 4 ARG A 376 LEU A 382 -1 O GLU A 381 N LEU A 369
SHEET 4 AA7 4 GLN A 385 ARG A 386 -1 O GLN A 385 N LEU A 382
SHEET 1 AA8 8 GLN A 402 PHE A 406 0
SHEET 2 AA8 8 GLY A 413 LEU A 418 -1 O GLY A 413 N PHE A 406
SHEET 3 AA8 8 GLY A 457 SER A 461 -1 O TYR A 460 N TRP A 416
SHEET 4 AA8 8 VAL A 426 ILE A 432 1 N PRO A 427 O GLY A 457
SHEET 5 AA8 8 LEU A 503 GLY A 513 1 O ALA A 509 N LEU A 430
SHEET 6 AA8 8 ALA A 532 ASP A 536 1 O ASP A 536 N GLY A 512
SHEET 7 AA8 8 THR A 589 SER A 594 1 O LEU A 590 N THR A 535
SHEET 8 AA8 8 VAL A 619 PHE A 624 1 O ARG A 620 N ILE A 591
SHEET 1 AA9 4 PHE B 19 VAL B 25 0
SHEET 2 AA9 4 VAL B 32 GLN B 38 -1 O ALA B 33 N GLN B 24
SHEET 3 AA9 4 ARG B 57 SER B 63 -1 O TRP B 61 N PHE B 34
SHEET 4 AA9 4 ARG B 69 PRO B 70 -1 O ARG B 69 N LEU B 62
SHEET 1 AB1 4 GLY B 79 TRP B 85 0
SHEET 2 AB1 4 ASN B 91 SER B 97 -1 O ALA B 93 N ARG B 84
SHEET 3 AB1 4 ALA B 104 PRO B 109 -1 O MET B 106 N PHE B 94
SHEET 4 AB1 4 ARG B 116 ARG B 117 -1 O ARG B 116 N LEU B 107
SHEET 1 AB2 4 VAL B 125 TRP B 130 0
SHEET 2 AB2 4 PHE B 136 THR B 141 -1 O ALA B 138 N GLN B 129
SHEET 3 AB2 4 ALA B 177 ASP B 182 -1 O TRP B 179 N PHE B 139
SHEET 4 AB2 4 LYS B 187 TYR B 192 -1 O TYR B 192 N LEU B 178
SHEET 1 AB3 4 LEU B 201 TRP B 203 0
SHEET 2 AB3 4 GLY B 209 GLN B 214 -1 O LEU B 211 N SER B 202
SHEET 3 AB3 4 GLN B 226 PRO B 232 -1 O TYR B 229 N ILE B 212
SHEET 4 AB3 4 GLN B 243 SER B 250 -1 O GLN B 243 N ASP B 230
SHEET 1 AB4 4 ALA B 252 PRO B 257 0
SHEET 2 AB4 4 PHE B 264 GLY B 268 -1 O ILE B 267 N HIS B 253
SHEET 3 AB4 4 HIS B 280 GLU B 285 -1 O ILE B 284 N PHE B 264
SHEET 4 AB4 4 GLN B 288 ARG B 291 -1 O ARG B 290 N LEU B 283
SHEET 1 AB5 4 ARG B 318 TRP B 319 0
SHEET 2 AB5 4 THR B 324 VAL B 331 -1 O LEU B 326 N ARG B 318
SHEET 3 AB5 4 SER B 334 HIS B 341 -1 O PHE B 338 N PHE B 327
SHEET 4 AB5 4 VAL B 346 ASP B 350 -1 O ASP B 350 N LEU B 337
SHEET 1 AB6 4 VAL B 356 ALA B 362 0
SHEET 2 AB6 4 VAL B 367 SER B 373 -1 O GLU B 372 N VAL B 356
SHEET 3 AB6 4 ARG B 376 LEU B 382 -1 O GLU B 381 N LEU B 369
SHEET 4 AB6 4 GLN B 385 ARG B 386 -1 O GLN B 385 N LEU B 382
SHEET 1 AB7 8 GLN B 402 PHE B 406 0
SHEET 2 AB7 8 GLY B 413 LEU B 418 -1 O GLY B 413 N PHE B 406
SHEET 3 AB7 8 GLY B 457 SER B 461 -1 O TYR B 460 N TRP B 416
SHEET 4 AB7 8 VAL B 426 ILE B 432 1 N PRO B 427 O GLY B 457
SHEET 5 AB7 8 LEU B 503 GLY B 513 1 O ALA B 509 N LEU B 430
SHEET 6 AB7 8 ALA B 532 ASP B 536 1 O ASP B 536 N GLY B 512
SHEET 7 AB7 8 THR B 589 SER B 594 1 O LEU B 590 N THR B 535
SHEET 8 AB7 8 VAL B 619 PHE B 624 1 O VAL B 622 N ILE B 591
SHEET 1 AB8 4 PHE C 19 VAL C 25 0
SHEET 2 AB8 4 VAL C 32 GLN C 38 -1 O ALA C 33 N GLN C 24
SHEET 3 AB8 4 ARG C 57 SER C 63 -1 O TRP C 61 N PHE C 34
SHEET 4 AB8 4 ARG C 69 PRO C 70 -1 O ARG C 69 N LEU C 62
SHEET 1 AB9 4 GLY C 79 TRP C 85 0
SHEET 2 AB9 4 ASN C 91 SER C 97 -1 O ALA C 93 N ARG C 84
SHEET 3 AB9 4 ALA C 104 PRO C 109 -1 O MET C 106 N PHE C 94
SHEET 4 AB9 4 ARG C 116 ARG C 117 -1 O ARG C 116 N LEU C 107
SHEET 1 AC1 4 SER C 126 TRP C 130 0
SHEET 2 AC1 4 PHE C 136 THR C 140 -1 O ALA C 138 N GLN C 129
SHEET 3 AC1 4 LEU C 178 ASP C 182 -1 O TRP C 179 N PHE C 139
SHEET 4 AC1 4 LYS C 187 TYR C 192 -1 O TYR C 192 N LEU C 178
SHEET 1 AC2 4 LEU C 201 TRP C 203 0
SHEET 2 AC2 4 GLY C 209 GLN C 214 -1 O LEU C 211 N SER C 202
SHEET 3 AC2 4 GLN C 226 PRO C 232 -1 O TYR C 229 N ILE C 212
SHEET 4 AC2 4 GLN C 243 SER C 250 -1 O GLN C 243 N ASP C 230
SHEET 1 AC3 4 ALA C 252 PRO C 257 0
SHEET 2 AC3 4 PHE C 264 GLY C 268 -1 O ILE C 267 N HIS C 253
SHEET 3 AC3 4 HIS C 280 GLU C 285 -1 O ILE C 284 N PHE C 264
SHEET 4 AC3 4 GLN C 288 ARG C 291 -1 O GLN C 288 N GLU C 285
SHEET 1 AC4 4 ARG C 318 TRP C 319 0
SHEET 2 AC4 4 THR C 324 VAL C 331 -1 O LEU C 326 N ARG C 318
SHEET 3 AC4 4 SER C 334 HIS C 341 -1 O PHE C 338 N PHE C 327
SHEET 4 AC4 4 VAL C 346 ASP C 350 -1 O ASP C 350 N LEU C 337
SHEET 1 AC5 4 GLY C 355 ALA C 362 0
SHEET 2 AC5 4 VAL C 367 SER C 373 -1 O GLU C 372 N VAL C 356
SHEET 3 AC5 4 ARG C 376 LEU C 382 -1 O GLU C 381 N LEU C 369
SHEET 4 AC5 4 GLN C 385 ARG C 386 -1 O GLN C 385 N LEU C 382
SHEET 1 AC6 8 GLN C 402 THR C 408 0
SHEET 2 AC6 8 GLY C 411 LEU C 418 -1 O GLY C 413 N PHE C 406
SHEET 3 AC6 8 GLY C 457 SER C 461 -1 O TYR C 460 N TRP C 416
SHEET 4 AC6 8 VAL C 426 ILE C 432 1 N PRO C 427 O GLY C 457
SHEET 5 AC6 8 LEU C 503 GLY C 513 1 O ALA C 509 N LEU C 430
SHEET 6 AC6 8 ALA C 532 ASP C 536 1 O ASP C 536 N GLY C 512
SHEET 7 AC6 8 THR C 589 SER C 594 1 O LEU C 590 N THR C 535
SHEET 8 AC6 8 VAL C 619 PHE C 624 1 O ARG C 620 N ILE C 591
SHEET 1 AC7 4 PHE D 19 VAL D 25 0
SHEET 2 AC7 4 VAL D 32 GLN D 38 -1 O ALA D 33 N GLN D 24
SHEET 3 AC7 4 ARG D 57 SER D 63 -1 O ARG D 57 N GLN D 38
SHEET 4 AC7 4 ARG D 69 PRO D 70 -1 O ARG D 69 N LEU D 62
SHEET 1 AC8 4 ASP D 80 TRP D 85 0
SHEET 2 AC8 4 ASN D 91 ARG D 96 -1 O ALA D 93 N ARG D 84
SHEET 3 AC8 4 ALA D 104 PRO D 109 -1 O MET D 106 N PHE D 94
SHEET 4 AC8 4 ARG D 116 ARG D 117 -1 O ARG D 116 N LEU D 107
SHEET 1 AC9 4 SER D 126 TRP D 130 0
SHEET 2 AC9 4 PHE D 136 THR D 140 -1 O ALA D 138 N GLN D 129
SHEET 3 AC9 4 LEU D 178 ASP D 182 -1 O TRP D 179 N PHE D 139
SHEET 4 AC9 4 LYS D 187 TYR D 192 -1 O ARG D 189 N LEU D 180
SHEET 1 AD1 4 LEU D 201 TRP D 203 0
SHEET 2 AD1 4 GLY D 209 GLN D 214 -1 O LEU D 211 N SER D 202
SHEET 3 AD1 4 GLN D 226 PRO D 232 -1 O TYR D 229 N ILE D 212
SHEET 4 AD1 4 GLN D 243 SER D 250 -1 O GLN D 243 N ASP D 230
SHEET 1 AD2 4 ALA D 252 PRO D 257 0
SHEET 2 AD2 4 PHE D 264 GLY D 268 -1 O ALA D 265 N ALA D 256
SHEET 3 AD2 4 HIS D 280 GLU D 285 -1 O ILE D 284 N PHE D 264
SHEET 4 AD2 4 GLN D 288 ARG D 291 -1 O GLN D 288 N GLU D 285
SHEET 1 AD3 4 ARG D 318 TRP D 319 0
SHEET 2 AD3 4 THR D 324 VAL D 331 -1 O LEU D 326 N ARG D 318
SHEET 3 AD3 4 SER D 334 HIS D 341 -1 O PHE D 338 N PHE D 327
SHEET 4 AD3 4 VAL D 346 ASP D 350 -1 O ASP D 350 N LEU D 337
SHEET 1 AD4 4 GLY D 355 ALA D 362 0
SHEET 2 AD4 4 VAL D 367 SER D 373 -1 O GLU D 372 N VAL D 356
SHEET 3 AD4 4 ARG D 376 LEU D 382 -1 O GLU D 381 N LEU D 369
SHEET 4 AD4 4 GLN D 385 ARG D 386 -1 O GLN D 385 N LEU D 382
SHEET 1 AD5 8 GLN D 402 THR D 408 0
SHEET 2 AD5 8 GLY D 411 LEU D 418 -1 O GLY D 413 N PHE D 406
SHEET 3 AD5 8 GLY D 457 SER D 461 -1 O TYR D 460 N TRP D 416
SHEET 4 AD5 8 VAL D 426 ILE D 432 1 N PRO D 427 O GLY D 457
SHEET 5 AD5 8 LEU D 503 GLY D 513 1 O ALA D 509 N LEU D 430
SHEET 6 AD5 8 ALA D 532 ASP D 536 1 O ASP D 536 N GLY D 512
SHEET 7 AD5 8 THR D 589 SER D 594 1 O LEU D 590 N THR D 535
SHEET 8 AD5 8 VAL D 619 PHE D 624 1 O ARG D 620 N ILE D 591
CISPEP 1 GLY A 435 PRO A 436 0 7.83
CISPEP 2 GLY B 435 PRO B 436 0 7.56
CISPEP 3 GLY C 435 PRO C 436 0 5.98
CISPEP 4 GLY D 435 PRO D 436 0 7.15
SITE 1 AC1 7 TYR A 349 ASP A 350 GLU A 381 ASN A 383
SITE 2 AC1 7 GLY A 384 HOH A 815 HOH D 803
SITE 1 AC2 6 ALA A 374 GLY A 443 THR A 445 PHE A 448
SITE 2 AC2 6 GLN A 449 TYR A 460
SITE 1 AC3 6 GLY A 435 SER A 514 ARG A 537 PHE A 555
SITE 2 AC3 6 ARG A 599 CYS A 600
SITE 1 AC4 10 ASN A 628 HIS A 629 GLU A 630 LEU A 631
SITE 2 AC4 10 ARG A 639 ARG A 640 HOH A 820 HOH A 881
SITE 3 AC4 10 HOH A 948 HOH A 974
SITE 1 AC5 9 TYR B 349 ASP B 350 VAL B 367 LEU B 369
SITE 2 AC5 9 GLU B 381 ASN B 383 GLY B 384 HOH B 808
SITE 3 AC5 9 ARG C 566
SITE 1 AC6 6 GLU B 400 VAL B 417 LEU B 419 HOH B 809
SITE 2 AC6 6 GLU C 409 ARG C 480
SITE 1 AC7 6 ALA B 374 GLY B 443 THR B 445 PHE B 448
SITE 2 AC7 6 GLN B 449 TYR B 460
SITE 1 AC8 9 HIS B 629 GLU B 630 LEU B 631 ARG B 639
SITE 2 AC8 9 ARG B 640 HOH B 816 HOH B 826 HOH B 848
SITE 3 AC8 9 HOH B 882
SITE 1 AC9 7 ALA C 374 GLY C 441 GLY C 443 THR C 445
SITE 2 AC9 7 PHE C 448 GLN C 449 TYR C 460
SITE 1 AD1 5 ARG C 332 LEU C 410 GLU C 412 TYR C 469
SITE 2 AD1 5 TRP C 473
SITE 1 AD2 8 HIS C 629 GLU C 630 LEU C 631 ARG C 640
SITE 2 AD2 8 HOH C 812 HOH C 871 HOH C 896 HOH C 948
SITE 1 AD3 7 ARG A 399 GLU A 400 VAL A 417 LEU A 418
SITE 2 AD3 7 LEU A 419 GLU D 409 ARG D 480
SITE 1 AD4 4 GLY A 411 GLU A 412 TYR D 282 ARG D 291
SITE 1 AD5 6 LEU A 571 LEU D 571 ASP D 575 GLN D 580
SITE 2 AD5 6 HOH D 820 HOH D 828
SITE 1 AD6 7 HIS D 629 GLU D 630 LEU D 631 ARG D 640
SITE 2 AD6 7 HOH D 812 HOH D 870 HOH D 890
CRYST1 119.658 129.989 194.130 90.00 90.00 90.00 P 21 21 21 16
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 0.008357 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005151 0.00000
TER 4650 LEU A 655
TER 9261 LEU B 655
TER 13729 LEU C 655
TER 18176 LEU D 655
MASTER 724 0 15 55 144 0 32 619224 4 86 204
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