HEADER TRANSFERASE 22-MAY-14 4QG6
TITLE CRYSTAL STRUCTURE OF PKM2-Y105E MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE PKM;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CYTOSOLIC THYROID HORMONE-BINDING PROTEIN, CTHBP, OPA-
COMPND 5 INTERACTING PROTEIN 3, OIP-3, PYRUVATE KINASE 2/3, PYRUVATE KINASE
COMPND 6 MUSCLE ISOZYME, THYROID HORMONE-BINDING PROTEIN 1, THBP1, TUMOR M2-
COMPND 7 PK, P58;
COMPND 8 EC: 2.7.1.40;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PKM, OIP3, PK2, PK3, PKM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TETRAMER, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.WANG,C.SUN,T.ZHU,Y.XU
REVDAT 3 24-AUG-22 4QG6 1 JRNL REMARK SEQADV
REVDAT 2 25-MAR-15 4QG6 1 TITLE
REVDAT 1 25-FEB-15 4QG6 0
JRNL AUTH P.WANG,C.SUN,T.ZHU,Y.XU
JRNL TITL STRUCTURAL INSIGHT INTO MECHANISMS FOR DYNAMIC REGULATION OF
JRNL TITL 2 PKM2.
JRNL REF PROTEIN CELL V. 6 275 2015
JRNL REFN ESSN 1674-8018
JRNL PMID 25645022
JRNL DOI 10.1007/S13238-015-0132-X
REMARK 2
REMARK 2 RESOLUTION. 3.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 71636
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 3615
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 45.6225 - 9.4746 0.97 2593 123 0.2207 0.2437
REMARK 3 2 9.4746 - 7.5313 1.00 2687 128 0.1665 0.1731
REMARK 3 3 7.5313 - 6.5824 1.00 2647 144 0.1895 0.2361
REMARK 3 4 6.5824 - 5.9820 1.00 2647 153 0.2002 0.2914
REMARK 3 5 5.9820 - 5.5541 1.00 2684 143 0.2048 0.2207
REMARK 3 6 5.5541 - 5.2271 1.00 2624 146 0.1907 0.2593
REMARK 3 7 5.2271 - 4.9657 1.00 2655 140 0.1858 0.2185
REMARK 3 8 4.9657 - 4.7497 1.00 2667 150 0.1884 0.2465
REMARK 3 9 4.7497 - 4.5671 1.00 2608 165 0.1831 0.2199
REMARK 3 10 4.5671 - 4.4096 0.99 2681 120 0.1931 0.2465
REMARK 3 11 4.4096 - 4.2718 0.99 2610 137 0.2127 0.2288
REMARK 3 12 4.2718 - 4.1498 0.99 2639 134 0.2373 0.2819
REMARK 3 13 4.1498 - 4.0406 0.99 2644 143 0.2505 0.2737
REMARK 3 14 4.0406 - 3.9421 0.99 2679 145 0.2575 0.2939
REMARK 3 15 3.9421 - 3.8525 0.99 2618 136 0.2541 0.3591
REMARK 3 16 3.8525 - 3.7706 0.99 2606 145 0.2666 0.3215
REMARK 3 17 3.7706 - 3.6952 0.99 2679 139 0.2630 0.3243
REMARK 3 18 3.6952 - 3.6255 1.00 2685 130 0.2564 0.2998
REMARK 3 19 3.6255 - 3.5608 1.00 2660 131 0.2594 0.2838
REMARK 3 20 3.5608 - 3.5004 1.00 2657 138 0.2560 0.3420
REMARK 3 21 3.5004 - 3.4440 1.00 2632 156 0.3104 0.3751
REMARK 3 22 3.4440 - 3.3910 0.99 2630 146 0.2937 0.3859
REMARK 3 23 3.3910 - 3.3412 0.99 2668 142 0.3272 0.4054
REMARK 3 24 3.3412 - 3.2941 0.99 2617 132 0.3125 0.3918
REMARK 3 25 3.2941 - 3.2496 0.99 2645 146 0.3248 0.4180
REMARK 3 26 3.2496 - 3.2070 0.70 1859 103 0.3183 0.4029
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.590
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 : 0.010 14218
REMARK 3 ANGLE : 1.385 19196
REMARK 3 CHIRALITY : 0.085 2207
REMARK 3 PLANARITY : 0.008 2498
REMARK 3 DIHEDRAL : 19.636 5394
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 4QG6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71636
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
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 : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M PROLINE, HEPES PH 7.5, 24%
REMARK 280 PEG1500, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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 85.68300
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 171.36600
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: 14850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 PRO A 4
REMARK 465 HIS A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 GLY A 9
REMARK 465 THR A 10
REMARK 465 ALA A 11
REMARK 465 PHE A 12
REMARK 465 ILE A 13
REMARK 465 GLN A 14
REMARK 465 THR A 15
REMARK 465 GLN A 16
REMARK 465 GLN A 17
REMARK 465 LEU A 18
REMARK 465 HIS A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 MET A 22
REMARK 465 ALA A 23
REMARK 465 GLU A 118
REMARK 465 ILE A 119
REMARK 465 ARG A 120
REMARK 465 THR A 121
REMARK 465 GLY A 122
REMARK 465 LEU A 123
REMARK 465 ILE A 124
REMARK 465 LYS A 125
REMARK 465 GLY A 126
REMARK 465 SER A 127
REMARK 465 GLY A 128
REMARK 465 THR A 129
REMARK 465 ALA A 130
REMARK 465 GLU A 131
REMARK 465 VAL A 132
REMARK 465 GLU A 133
REMARK 465 LEU A 134
REMARK 465 LYS A 135
REMARK 465 LYS A 136
REMARK 465 GLY A 137
REMARK 465 ALA A 138
REMARK 465 THR A 139
REMARK 465 LEU A 140
REMARK 465 LYS A 141
REMARK 465 ILE A 142
REMARK 465 THR A 143
REMARK 465 LEU A 144
REMARK 465 ASP A 145
REMARK 465 ASN A 146
REMARK 465 ALA A 147
REMARK 465 TYR A 148
REMARK 465 MET A 149
REMARK 465 GLU A 150
REMARK 465 LYS A 151
REMARK 465 CYS A 152
REMARK 465 ASP A 153
REMARK 465 GLU A 154
REMARK 465 ASN A 155
REMARK 465 ILE A 156
REMARK 465 LEU A 157
REMARK 465 TRP A 158
REMARK 465 LEU A 159
REMARK 465 ASP A 160
REMARK 465 TYR A 161
REMARK 465 LYS A 162
REMARK 465 ASN A 163
REMARK 465 ILE A 164
REMARK 465 CYS A 165
REMARK 465 LYS A 166
REMARK 465 VAL A 167
REMARK 465 VAL A 168
REMARK 465 GLU A 169
REMARK 465 VAL A 170
REMARK 465 GLY A 171
REMARK 465 SER A 172
REMARK 465 LYS A 173
REMARK 465 ILE A 174
REMARK 465 TYR A 175
REMARK 465 VAL A 176
REMARK 465 ASP A 177
REMARK 465 ASP A 178
REMARK 465 GLY A 179
REMARK 465 LEU A 180
REMARK 465 ILE A 181
REMARK 465 SER A 182
REMARK 465 LEU A 183
REMARK 465 GLN A 184
REMARK 465 VAL A 185
REMARK 465 LYS A 186
REMARK 465 GLN A 187
REMARK 465 LYS A 188
REMARK 465 GLY A 189
REMARK 465 ALA A 190
REMARK 465 ASP A 191
REMARK 465 PHE A 192
REMARK 465 LEU A 193
REMARK 465 VAL A 194
REMARK 465 THR A 195
REMARK 465 GLU A 196
REMARK 465 VAL A 197
REMARK 465 GLU A 198
REMARK 465 ASN A 199
REMARK 465 GLY A 200
REMARK 465 GLY A 201
REMARK 465 SER A 202
REMARK 465 LEU A 203
REMARK 465 GLY A 204
REMARK 465 SER A 205
REMARK 465 LYS A 206
REMARK 465 LYS A 207
REMARK 465 GLY A 208
REMARK 465 VAL A 209
REMARK 465 ASN A 210
REMARK 465 LEU A 211
REMARK 465 PRO A 212
REMARK 465 GLY A 213
REMARK 465 ALA A 214
REMARK 465 ALA A 215
REMARK 465 VAL A 216
REMARK 465 ASP A 217
REMARK 465 LEU A 218
REMARK 465 PRO A 219
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 PRO B 4
REMARK 465 HIS B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 GLY B 9
REMARK 465 THR B 10
REMARK 465 ALA B 11
REMARK 465 PHE B 12
REMARK 465 ILE B 13
REMARK 465 GLN B 14
REMARK 465 THR B 15
REMARK 465 GLN B 16
REMARK 465 GLN B 17
REMARK 465 LEU B 18
REMARK 465 HIS B 19
REMARK 465 ALA B 20
REMARK 465 ALA B 21
REMARK 465 MET B 22
REMARK 465 ALA B 23
REMARK 465 GLY B 126
REMARK 465 SER B 127
REMARK 465 GLY B 128
REMARK 465 THR B 129
REMARK 465 LEU B 134
REMARK 465 LYS B 135
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
REMARK 465 PRO C 4
REMARK 465 HIS C 5
REMARK 465 SER C 6
REMARK 465 GLU C 7
REMARK 465 ALA C 8
REMARK 465 GLY C 9
REMARK 465 THR C 10
REMARK 465 ALA C 11
REMARK 465 PHE C 12
REMARK 465 ILE C 13
REMARK 465 GLN C 14
REMARK 465 THR C 15
REMARK 465 GLN C 16
REMARK 465 GLN C 17
REMARK 465 LEU C 18
REMARK 465 HIS C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 MET C 22
REMARK 465 ALA C 23
REMARK 465 GLU C 118
REMARK 465 ILE C 119
REMARK 465 ARG C 120
REMARK 465 THR C 121
REMARK 465 GLY C 122
REMARK 465 LEU C 123
REMARK 465 ILE C 124
REMARK 465 LYS C 125
REMARK 465 GLY C 126
REMARK 465 SER C 127
REMARK 465 GLY C 128
REMARK 465 THR C 129
REMARK 465 ALA C 130
REMARK 465 GLU C 131
REMARK 465 VAL C 132
REMARK 465 GLU C 133
REMARK 465 LEU C 134
REMARK 465 LYS C 135
REMARK 465 LYS C 136
REMARK 465 GLY C 137
REMARK 465 ALA C 138
REMARK 465 THR C 139
REMARK 465 LEU C 140
REMARK 465 LYS C 141
REMARK 465 ILE C 142
REMARK 465 THR C 143
REMARK 465 LEU C 144
REMARK 465 ASP C 145
REMARK 465 ASN C 146
REMARK 465 ALA C 147
REMARK 465 TYR C 148
REMARK 465 MET C 149
REMARK 465 GLU C 150
REMARK 465 LYS C 151
REMARK 465 CYS C 152
REMARK 465 ASP C 153
REMARK 465 GLU C 154
REMARK 465 ASN C 155
REMARK 465 ILE C 156
REMARK 465 LEU C 157
REMARK 465 TRP C 158
REMARK 465 LEU C 159
REMARK 465 ASP C 160
REMARK 465 TYR C 161
REMARK 465 LYS C 162
REMARK 465 ASN C 163
REMARK 465 ILE C 164
REMARK 465 CYS C 165
REMARK 465 LYS C 166
REMARK 465 VAL C 167
REMARK 465 VAL C 168
REMARK 465 GLU C 169
REMARK 465 VAL C 170
REMARK 465 GLY C 171
REMARK 465 SER C 172
REMARK 465 LYS C 173
REMARK 465 ILE C 174
REMARK 465 TYR C 175
REMARK 465 VAL C 176
REMARK 465 ASP C 177
REMARK 465 ASP C 178
REMARK 465 GLY C 179
REMARK 465 LEU C 180
REMARK 465 ILE C 181
REMARK 465 SER C 182
REMARK 465 LEU C 183
REMARK 465 GLN C 184
REMARK 465 VAL C 185
REMARK 465 LYS C 186
REMARK 465 GLN C 187
REMARK 465 LYS C 188
REMARK 465 GLY C 189
REMARK 465 ALA C 190
REMARK 465 ASP C 191
REMARK 465 PHE C 192
REMARK 465 LEU C 193
REMARK 465 VAL C 194
REMARK 465 THR C 195
REMARK 465 GLU C 196
REMARK 465 VAL C 197
REMARK 465 GLU C 198
REMARK 465 ASN C 199
REMARK 465 GLY C 200
REMARK 465 GLY C 201
REMARK 465 SER C 202
REMARK 465 LEU C 203
REMARK 465 GLY C 204
REMARK 465 SER C 205
REMARK 465 LYS C 206
REMARK 465 LYS C 207
REMARK 465 GLY C 208
REMARK 465 VAL C 209
REMARK 465 ASN C 210
REMARK 465 LEU C 211
REMARK 465 PRO C 212
REMARK 465 GLY C 213
REMARK 465 ALA C 214
REMARK 465 ALA C 215
REMARK 465 VAL C 216
REMARK 465 ASP C 217
REMARK 465 LEU C 218
REMARK 465 PRO C 219
REMARK 465 GLY D -3
REMARK 465 PRO D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LYS D 3
REMARK 465 PRO D 4
REMARK 465 HIS D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 ALA D 8
REMARK 465 GLY D 9
REMARK 465 THR D 10
REMARK 465 ALA D 11
REMARK 465 PHE D 12
REMARK 465 ILE D 13
REMARK 465 GLN D 14
REMARK 465 THR D 15
REMARK 465 GLN D 16
REMARK 465 GLN D 17
REMARK 465 LEU D 18
REMARK 465 HIS D 19
REMARK 465 ALA D 20
REMARK 465 ALA D 21
REMARK 465 MET D 22
REMARK 465 ALA D 23
REMARK 465 SER D 127
REMARK 465 GLY D 128
REMARK 465 THR D 129
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 NH1 ARG D 73 OD2 ASP D 113 2.03
REMARK 500 NH1 ARG B 73 OD2 ASP B 113 2.03
REMARK 500 NH1 ARG C 73 OD2 ASP C 113 2.10
REMARK 500 O SER C 287 NZ LYS C 322 2.10
REMARK 500 O LYS B 433 OG1 THR B 459 2.11
REMARK 500 O VAL A 417 OG SER A 420 2.12
REMARK 500 O ALA D 147 NZ LYS D 151 2.12
REMARK 500 OE2 GLU B 386 NH2 ARG B 467 2.16
REMARK 500 NH1 ARG D 92 O GLN D 235 2.17
REMARK 500 OE1 GLU B 118 NH1 ARG B 120 2.18
REMARK 500 O ALA C 42 ND2 ASN C 44 2.18
REMARK 500 NH2 ARG C 516 OD2 ASP D 487 2.18
REMARK 500 O ALA A 42 ND2 ASN A 44 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 ARG B 436 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 PRO B 517 C - N - CA ANGL. DEV. = -16.1 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 PRO A 53 -38.45 -36.36
REMARK 500 SER A 97 15.62 -63.77
REMARK 500 ASN A 264 -79.12 -70.37
REMARK 500 ILE A 265 117.44 -15.88
REMARK 500 GLU A 272 -46.67 -132.61
REMARK 500 ASN A 273 -169.97 -73.32
REMARK 500 ILE A 299 -32.99 177.15
REMARK 500 THR A 328 141.90 85.28
REMARK 500 MET A 330 -93.00 -74.89
REMARK 500 LYS A 336 16.77 -140.26
REMARK 500 SER A 362 -109.07 -116.86
REMARK 500 ALA A 387 -9.36 -58.01
REMARK 500 LEU A 392 19.52 -69.18
REMARK 500 GLN A 393 -30.63 -162.24
REMARK 500 LYS A 433 -73.46 -83.78
REMARK 500 ARG A 436 -28.79 -38.34
REMARK 500 ASN A 456 103.47 -54.23
REMARK 500 GLN A 458 -72.55 -70.94
REMARK 500 THR A 459 76.76 -65.02
REMARK 500 ALA A 460 -52.25 176.95
REMARK 500 LEU A 465 41.75 -83.33
REMARK 500 LYS A 498 -71.35 -62.77
REMARK 500 ASN A 523 20.99 -146.50
REMARK 500 LEU B 33 126.85 -37.41
REMARK 500 PRO B 53 -61.06 -14.88
REMARK 500 SER B 57 104.78 -57.44
REMARK 500 VAL B 58 -48.39 -18.54
REMARK 500 ASN B 70 -21.57 -141.03
REMARK 500 ALA B 99 -8.78 -58.53
REMARK 500 ILE B 103 -46.22 -154.84
REMARK 500 ASP B 145 106.68 -59.84
REMARK 500 LYS B 151 60.83 -117.53
REMARK 500 GLU B 154 46.26 -67.44
REMARK 500 ASN B 155 -32.65 -160.43
REMARK 500 TYR B 161 100.48 -31.28
REMARK 500 ASP B 177 78.46 61.01
REMARK 500 GLN B 184 -152.46 -91.52
REMARK 500 ALA B 190 -57.65 -129.33
REMARK 500 GLU B 198 -94.52 -131.40
REMARK 500 SER B 202 102.68 -44.63
REMARK 500 ALA B 215 81.27 -60.85
REMARK 500 LEU B 218 -175.94 -58.99
REMARK 500 PHE B 244 70.58 46.58
REMARK 500 THR B 328 149.20 87.56
REMARK 500 GLN B 329 -22.91 61.84
REMARK 500 MET B 330 -78.42 -32.72
REMARK 500 SER B 362 -127.62 -120.79
REMARK 500 LYS B 367 31.98 -153.44
REMARK 500 TYR B 390 72.19 -63.31
REMARK 500 GLN B 393 -70.05 -68.37
REMARK 500
REMARK 500 THIS ENTRY HAS 121 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 ASP D 217 LEU D 218 -144.37
REMARK 500 LEU D 218 PRO D 219 141.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PRO A 1001
REMARK 610 PRO B 1001
REMARK 610 PRO C 1001
REMARK 610 PRO D 1001
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PRO D 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QGC RELATED DB: PDB
REMARK 900 RELATED ID: 4QG9 RELATED DB: PDB
REMARK 900 RELATED ID: 4QG8 RELATED DB: PDB
REMARK 900 RELATED ID: 4RPP RELATED DB: PDB
DBREF 4QG6 A 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4QG6 B 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4QG6 C 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4QG6 D 1 531 UNP P14618 KPYM_HUMAN 1 531
SEQADV 4QG6 GLY A -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 PRO A -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLY A -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 SER A 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLU A 105 UNP P14618 TYR 105 ENGINEERED MUTATION
SEQADV 4QG6 GLY B -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 PRO B -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLY B -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 SER B 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLU B 105 UNP P14618 TYR 105 ENGINEERED MUTATION
SEQADV 4QG6 GLY C -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 PRO C -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLY C -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 SER C 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLU C 105 UNP P14618 TYR 105 ENGINEERED MUTATION
SEQADV 4QG6 GLY D -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 PRO D -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLY D -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 SER D 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG6 GLU D 105 UNP P14618 TYR 105 ENGINEERED MUTATION
SEQRES 1 A 535 GLY PRO GLY SER MET SER LYS PRO HIS SER GLU ALA GLY
SEQRES 2 A 535 THR ALA PHE ILE GLN THR GLN GLN LEU HIS ALA ALA MET
SEQRES 3 A 535 ALA ASP THR PHE LEU GLU HIS MET CYS ARG LEU ASP ILE
SEQRES 4 A 535 ASP SER PRO PRO ILE THR ALA ARG ASN THR GLY ILE ILE
SEQRES 5 A 535 CYS THR ILE GLY PRO ALA SER ARG SER VAL GLU THR LEU
SEQRES 6 A 535 LYS GLU MET ILE LYS SER GLY MET ASN VAL ALA ARG LEU
SEQRES 7 A 535 ASN PHE SER HIS GLY THR HIS GLU TYR HIS ALA GLU THR
SEQRES 8 A 535 ILE LYS ASN VAL ARG THR ALA THR GLU SER PHE ALA SER
SEQRES 9 A 535 ASP PRO ILE LEU GLU ARG PRO VAL ALA VAL ALA LEU ASP
SEQRES 10 A 535 THR LYS GLY PRO GLU ILE ARG THR GLY LEU ILE LYS GLY
SEQRES 11 A 535 SER GLY THR ALA GLU VAL GLU LEU LYS LYS GLY ALA THR
SEQRES 12 A 535 LEU LYS ILE THR LEU ASP ASN ALA TYR MET GLU LYS CYS
SEQRES 13 A 535 ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS ASN ILE CYS
SEQRES 14 A 535 LYS VAL VAL GLU VAL GLY SER LYS ILE TYR VAL ASP ASP
SEQRES 15 A 535 GLY LEU ILE SER LEU GLN VAL LYS GLN LYS GLY ALA ASP
SEQRES 16 A 535 PHE LEU VAL THR GLU VAL GLU ASN GLY GLY SER LEU GLY
SEQRES 17 A 535 SER LYS LYS GLY VAL ASN LEU PRO GLY ALA ALA VAL ASP
SEQRES 18 A 535 LEU PRO ALA VAL SER GLU LYS ASP ILE GLN ASP LEU LYS
SEQRES 19 A 535 PHE GLY VAL GLU GLN ASP VAL ASP MET VAL PHE ALA SER
SEQRES 20 A 535 PHE ILE ARG LYS ALA SER ASP VAL HIS GLU VAL ARG LYS
SEQRES 21 A 535 VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS ILE ILE SER
SEQRES 22 A 535 LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG PHE ASP GLU
SEQRES 23 A 535 ILE LEU GLU ALA SER ASP GLY ILE MET VAL ALA ARG GLY
SEQRES 24 A 535 ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS VAL PHE LEU
SEQRES 25 A 535 ALA GLN LYS MET MET ILE GLY ARG CYS ASN ARG ALA GLY
SEQRES 26 A 535 LYS PRO VAL ILE CYS ALA THR GLN MET LEU GLU SER MET
SEQRES 27 A 535 ILE LYS LYS PRO ARG PRO THR ARG ALA GLU GLY SER ASP
SEQRES 28 A 535 VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP CYS ILE MET
SEQRES 29 A 535 LEU SER GLY GLU THR ALA LYS GLY ASP TYR PRO LEU GLU
SEQRES 30 A 535 ALA VAL ARG MET GLN HIS LEU ILE ALA ARG GLU ALA GLU
SEQRES 31 A 535 ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU GLU LEU ARG
SEQRES 32 A 535 ARG LEU ALA PRO ILE THR SER ASP PRO THR GLU ALA THR
SEQRES 33 A 535 ALA VAL GLY ALA VAL GLU ALA SER PHE LYS CYS CYS SER
SEQRES 34 A 535 GLY ALA ILE ILE VAL LEU THR LYS SER GLY ARG SER ALA
SEQRES 35 A 535 HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA PRO ILE ILE
SEQRES 36 A 535 ALA VAL THR ARG ASN PRO GLN THR ALA ARG GLN ALA HIS
SEQRES 37 A 535 LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS LYS ASP PRO
SEQRES 38 A 535 VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP LEU ARG VAL
SEQRES 39 A 535 ASN PHE ALA MET ASN VAL GLY LYS ALA ARG GLY PHE PHE
SEQRES 40 A 535 LYS LYS GLY ASP VAL VAL ILE VAL LEU THR GLY TRP ARG
SEQRES 41 A 535 PRO GLY SER GLY PHE THR ASN THR MET ARG VAL VAL PRO
SEQRES 42 A 535 VAL PRO
SEQRES 1 B 535 GLY PRO GLY SER MET SER LYS PRO HIS SER GLU ALA GLY
SEQRES 2 B 535 THR ALA PHE ILE GLN THR GLN GLN LEU HIS ALA ALA MET
SEQRES 3 B 535 ALA ASP THR PHE LEU GLU HIS MET CYS ARG LEU ASP ILE
SEQRES 4 B 535 ASP SER PRO PRO ILE THR ALA ARG ASN THR GLY ILE ILE
SEQRES 5 B 535 CYS THR ILE GLY PRO ALA SER ARG SER VAL GLU THR LEU
SEQRES 6 B 535 LYS GLU MET ILE LYS SER GLY MET ASN VAL ALA ARG LEU
SEQRES 7 B 535 ASN PHE SER HIS GLY THR HIS GLU TYR HIS ALA GLU THR
SEQRES 8 B 535 ILE LYS ASN VAL ARG THR ALA THR GLU SER PHE ALA SER
SEQRES 9 B 535 ASP PRO ILE LEU GLU ARG PRO VAL ALA VAL ALA LEU ASP
SEQRES 10 B 535 THR LYS GLY PRO GLU ILE ARG THR GLY LEU ILE LYS GLY
SEQRES 11 B 535 SER GLY THR ALA GLU VAL GLU LEU LYS LYS GLY ALA THR
SEQRES 12 B 535 LEU LYS ILE THR LEU ASP ASN ALA TYR MET GLU LYS CYS
SEQRES 13 B 535 ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS ASN ILE CYS
SEQRES 14 B 535 LYS VAL VAL GLU VAL GLY SER LYS ILE TYR VAL ASP ASP
SEQRES 15 B 535 GLY LEU ILE SER LEU GLN VAL LYS GLN LYS GLY ALA ASP
SEQRES 16 B 535 PHE LEU VAL THR GLU VAL GLU ASN GLY GLY SER LEU GLY
SEQRES 17 B 535 SER LYS LYS GLY VAL ASN LEU PRO GLY ALA ALA VAL ASP
SEQRES 18 B 535 LEU PRO ALA VAL SER GLU LYS ASP ILE GLN ASP LEU LYS
SEQRES 19 B 535 PHE GLY VAL GLU GLN ASP VAL ASP MET VAL PHE ALA SER
SEQRES 20 B 535 PHE ILE ARG LYS ALA SER ASP VAL HIS GLU VAL ARG LYS
SEQRES 21 B 535 VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS ILE ILE SER
SEQRES 22 B 535 LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG PHE ASP GLU
SEQRES 23 B 535 ILE LEU GLU ALA SER ASP GLY ILE MET VAL ALA ARG GLY
SEQRES 24 B 535 ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS VAL PHE LEU
SEQRES 25 B 535 ALA GLN LYS MET MET ILE GLY ARG CYS ASN ARG ALA GLY
SEQRES 26 B 535 LYS PRO VAL ILE CYS ALA THR GLN MET LEU GLU SER MET
SEQRES 27 B 535 ILE LYS LYS PRO ARG PRO THR ARG ALA GLU GLY SER ASP
SEQRES 28 B 535 VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP CYS ILE MET
SEQRES 29 B 535 LEU SER GLY GLU THR ALA LYS GLY ASP TYR PRO LEU GLU
SEQRES 30 B 535 ALA VAL ARG MET GLN HIS LEU ILE ALA ARG GLU ALA GLU
SEQRES 31 B 535 ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU GLU LEU ARG
SEQRES 32 B 535 ARG LEU ALA PRO ILE THR SER ASP PRO THR GLU ALA THR
SEQRES 33 B 535 ALA VAL GLY ALA VAL GLU ALA SER PHE LYS CYS CYS SER
SEQRES 34 B 535 GLY ALA ILE ILE VAL LEU THR LYS SER GLY ARG SER ALA
SEQRES 35 B 535 HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA PRO ILE ILE
SEQRES 36 B 535 ALA VAL THR ARG ASN PRO GLN THR ALA ARG GLN ALA HIS
SEQRES 37 B 535 LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS LYS ASP PRO
SEQRES 38 B 535 VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP LEU ARG VAL
SEQRES 39 B 535 ASN PHE ALA MET ASN VAL GLY LYS ALA ARG GLY PHE PHE
SEQRES 40 B 535 LYS LYS GLY ASP VAL VAL ILE VAL LEU THR GLY TRP ARG
SEQRES 41 B 535 PRO GLY SER GLY PHE THR ASN THR MET ARG VAL VAL PRO
SEQRES 42 B 535 VAL PRO
SEQRES 1 C 535 GLY PRO GLY SER MET SER LYS PRO HIS SER GLU ALA GLY
SEQRES 2 C 535 THR ALA PHE ILE GLN THR GLN GLN LEU HIS ALA ALA MET
SEQRES 3 C 535 ALA ASP THR PHE LEU GLU HIS MET CYS ARG LEU ASP ILE
SEQRES 4 C 535 ASP SER PRO PRO ILE THR ALA ARG ASN THR GLY ILE ILE
SEQRES 5 C 535 CYS THR ILE GLY PRO ALA SER ARG SER VAL GLU THR LEU
SEQRES 6 C 535 LYS GLU MET ILE LYS SER GLY MET ASN VAL ALA ARG LEU
SEQRES 7 C 535 ASN PHE SER HIS GLY THR HIS GLU TYR HIS ALA GLU THR
SEQRES 8 C 535 ILE LYS ASN VAL ARG THR ALA THR GLU SER PHE ALA SER
SEQRES 9 C 535 ASP PRO ILE LEU GLU ARG PRO VAL ALA VAL ALA LEU ASP
SEQRES 10 C 535 THR LYS GLY PRO GLU ILE ARG THR GLY LEU ILE LYS GLY
SEQRES 11 C 535 SER GLY THR ALA GLU VAL GLU LEU LYS LYS GLY ALA THR
SEQRES 12 C 535 LEU LYS ILE THR LEU ASP ASN ALA TYR MET GLU LYS CYS
SEQRES 13 C 535 ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS ASN ILE CYS
SEQRES 14 C 535 LYS VAL VAL GLU VAL GLY SER LYS ILE TYR VAL ASP ASP
SEQRES 15 C 535 GLY LEU ILE SER LEU GLN VAL LYS GLN LYS GLY ALA ASP
SEQRES 16 C 535 PHE LEU VAL THR GLU VAL GLU ASN GLY GLY SER LEU GLY
SEQRES 17 C 535 SER LYS LYS GLY VAL ASN LEU PRO GLY ALA ALA VAL ASP
SEQRES 18 C 535 LEU PRO ALA VAL SER GLU LYS ASP ILE GLN ASP LEU LYS
SEQRES 19 C 535 PHE GLY VAL GLU GLN ASP VAL ASP MET VAL PHE ALA SER
SEQRES 20 C 535 PHE ILE ARG LYS ALA SER ASP VAL HIS GLU VAL ARG LYS
SEQRES 21 C 535 VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS ILE ILE SER
SEQRES 22 C 535 LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG PHE ASP GLU
SEQRES 23 C 535 ILE LEU GLU ALA SER ASP GLY ILE MET VAL ALA ARG GLY
SEQRES 24 C 535 ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS VAL PHE LEU
SEQRES 25 C 535 ALA GLN LYS MET MET ILE GLY ARG CYS ASN ARG ALA GLY
SEQRES 26 C 535 LYS PRO VAL ILE CYS ALA THR GLN MET LEU GLU SER MET
SEQRES 27 C 535 ILE LYS LYS PRO ARG PRO THR ARG ALA GLU GLY SER ASP
SEQRES 28 C 535 VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP CYS ILE MET
SEQRES 29 C 535 LEU SER GLY GLU THR ALA LYS GLY ASP TYR PRO LEU GLU
SEQRES 30 C 535 ALA VAL ARG MET GLN HIS LEU ILE ALA ARG GLU ALA GLU
SEQRES 31 C 535 ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU GLU LEU ARG
SEQRES 32 C 535 ARG LEU ALA PRO ILE THR SER ASP PRO THR GLU ALA THR
SEQRES 33 C 535 ALA VAL GLY ALA VAL GLU ALA SER PHE LYS CYS CYS SER
SEQRES 34 C 535 GLY ALA ILE ILE VAL LEU THR LYS SER GLY ARG SER ALA
SEQRES 35 C 535 HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA PRO ILE ILE
SEQRES 36 C 535 ALA VAL THR ARG ASN PRO GLN THR ALA ARG GLN ALA HIS
SEQRES 37 C 535 LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS LYS ASP PRO
SEQRES 38 C 535 VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP LEU ARG VAL
SEQRES 39 C 535 ASN PHE ALA MET ASN VAL GLY LYS ALA ARG GLY PHE PHE
SEQRES 40 C 535 LYS LYS GLY ASP VAL VAL ILE VAL LEU THR GLY TRP ARG
SEQRES 41 C 535 PRO GLY SER GLY PHE THR ASN THR MET ARG VAL VAL PRO
SEQRES 42 C 535 VAL PRO
SEQRES 1 D 535 GLY PRO GLY SER MET SER LYS PRO HIS SER GLU ALA GLY
SEQRES 2 D 535 THR ALA PHE ILE GLN THR GLN GLN LEU HIS ALA ALA MET
SEQRES 3 D 535 ALA ASP THR PHE LEU GLU HIS MET CYS ARG LEU ASP ILE
SEQRES 4 D 535 ASP SER PRO PRO ILE THR ALA ARG ASN THR GLY ILE ILE
SEQRES 5 D 535 CYS THR ILE GLY PRO ALA SER ARG SER VAL GLU THR LEU
SEQRES 6 D 535 LYS GLU MET ILE LYS SER GLY MET ASN VAL ALA ARG LEU
SEQRES 7 D 535 ASN PHE SER HIS GLY THR HIS GLU TYR HIS ALA GLU THR
SEQRES 8 D 535 ILE LYS ASN VAL ARG THR ALA THR GLU SER PHE ALA SER
SEQRES 9 D 535 ASP PRO ILE LEU GLU ARG PRO VAL ALA VAL ALA LEU ASP
SEQRES 10 D 535 THR LYS GLY PRO GLU ILE ARG THR GLY LEU ILE LYS GLY
SEQRES 11 D 535 SER GLY THR ALA GLU VAL GLU LEU LYS LYS GLY ALA THR
SEQRES 12 D 535 LEU LYS ILE THR LEU ASP ASN ALA TYR MET GLU LYS CYS
SEQRES 13 D 535 ASP GLU ASN ILE LEU TRP LEU ASP TYR LYS ASN ILE CYS
SEQRES 14 D 535 LYS VAL VAL GLU VAL GLY SER LYS ILE TYR VAL ASP ASP
SEQRES 15 D 535 GLY LEU ILE SER LEU GLN VAL LYS GLN LYS GLY ALA ASP
SEQRES 16 D 535 PHE LEU VAL THR GLU VAL GLU ASN GLY GLY SER LEU GLY
SEQRES 17 D 535 SER LYS LYS GLY VAL ASN LEU PRO GLY ALA ALA VAL ASP
SEQRES 18 D 535 LEU PRO ALA VAL SER GLU LYS ASP ILE GLN ASP LEU LYS
SEQRES 19 D 535 PHE GLY VAL GLU GLN ASP VAL ASP MET VAL PHE ALA SER
SEQRES 20 D 535 PHE ILE ARG LYS ALA SER ASP VAL HIS GLU VAL ARG LYS
SEQRES 21 D 535 VAL LEU GLY GLU LYS GLY LYS ASN ILE LYS ILE ILE SER
SEQRES 22 D 535 LYS ILE GLU ASN HIS GLU GLY VAL ARG ARG PHE ASP GLU
SEQRES 23 D 535 ILE LEU GLU ALA SER ASP GLY ILE MET VAL ALA ARG GLY
SEQRES 24 D 535 ASP LEU GLY ILE GLU ILE PRO ALA GLU LYS VAL PHE LEU
SEQRES 25 D 535 ALA GLN LYS MET MET ILE GLY ARG CYS ASN ARG ALA GLY
SEQRES 26 D 535 LYS PRO VAL ILE CYS ALA THR GLN MET LEU GLU SER MET
SEQRES 27 D 535 ILE LYS LYS PRO ARG PRO THR ARG ALA GLU GLY SER ASP
SEQRES 28 D 535 VAL ALA ASN ALA VAL LEU ASP GLY ALA ASP CYS ILE MET
SEQRES 29 D 535 LEU SER GLY GLU THR ALA LYS GLY ASP TYR PRO LEU GLU
SEQRES 30 D 535 ALA VAL ARG MET GLN HIS LEU ILE ALA ARG GLU ALA GLU
SEQRES 31 D 535 ALA ALA ILE TYR HIS LEU GLN LEU PHE GLU GLU LEU ARG
SEQRES 32 D 535 ARG LEU ALA PRO ILE THR SER ASP PRO THR GLU ALA THR
SEQRES 33 D 535 ALA VAL GLY ALA VAL GLU ALA SER PHE LYS CYS CYS SER
SEQRES 34 D 535 GLY ALA ILE ILE VAL LEU THR LYS SER GLY ARG SER ALA
SEQRES 35 D 535 HIS GLN VAL ALA ARG TYR ARG PRO ARG ALA PRO ILE ILE
SEQRES 36 D 535 ALA VAL THR ARG ASN PRO GLN THR ALA ARG GLN ALA HIS
SEQRES 37 D 535 LEU TYR ARG GLY ILE PHE PRO VAL LEU CYS LYS ASP PRO
SEQRES 38 D 535 VAL GLN GLU ALA TRP ALA GLU ASP VAL ASP LEU ARG VAL
SEQRES 39 D 535 ASN PHE ALA MET ASN VAL GLY LYS ALA ARG GLY PHE PHE
SEQRES 40 D 535 LYS LYS GLY ASP VAL VAL ILE VAL LEU THR GLY TRP ARG
SEQRES 41 D 535 PRO GLY SER GLY PHE THR ASN THR MET ARG VAL VAL PRO
SEQRES 42 D 535 VAL PRO
HET PRO A1001 7
HET PRO B1001 7
HET PRO C1001 7
HET PRO D1001 7
HETNAM PRO PROLINE
FORMUL 5 PRO 4(C5 H9 N O2)
HELIX 1 1 THR A 25 LEU A 33 1 9
HELIX 2 2 SER A 57 ILE A 65 1 9
HELIX 3 3 SER A 77 GLY A 79 5 3
HELIX 4 4 THR A 80 GLU A 96 1 17
HELIX 5 5 SER A 222 GLU A 234 1 13
HELIX 6 6 ALA A 248 GLY A 259 1 12
HELIX 7 7 ASN A 273 ARG A 279 1 7
HELIX 8 8 ARG A 279 ALA A 286 1 8
HELIX 9 9 PRO A 302 GLY A 321 1 20
HELIX 10 10 LEU A 331 LYS A 337 5 7
HELIX 11 11 THR A 341 ALA A 356 1 16
HELIX 12 12 SER A 362 LYS A 367 1 6
HELIX 13 13 TYR A 370 ALA A 385 1 16
HELIX 14 14 GLU A 386 ILE A 389 5 4
HELIX 15 15 TYR A 390 ALA A 402 1 13
HELIX 16 16 ASP A 407 CYS A 423 1 17
HELIX 17 17 GLY A 435 TYR A 444 1 10
HELIX 18 18 PRO A 457 GLN A 462 1 6
HELIX 19 19 ALA A 463 LEU A 465 5 3
HELIX 20 20 ALA A 481 GLY A 501 1 21
HELIX 21 21 THR B 25 LEU B 33 1 9
HELIX 22 22 SER B 57 GLY B 68 1 12
HELIX 23 23 THR B 80 SER B 97 1 18
HELIX 24 24 ASP B 145 MET B 149 5 5
HELIX 25 25 ASN B 163 VAL B 168 5 6
HELIX 26 26 SER B 222 GLN B 235 1 14
HELIX 27 27 LYS B 247 GLY B 259 1 13
HELIX 28 28 GLU B 260 LYS B 263 5 4
HELIX 29 29 ASN B 273 ARG B 279 1 7
HELIX 30 30 ARG B 279 SER B 287 1 9
HELIX 31 31 ARG B 294 ILE B 301 1 8
HELIX 32 32 LYS B 305 ARG B 319 1 15
HELIX 33 33 LEU B 331 LYS B 336 5 6
HELIX 34 34 THR B 341 GLY B 355 1 15
HELIX 35 35 SER B 362 LYS B 367 1 6
HELIX 36 36 PRO B 371 ALA B 385 1 15
HELIX 37 37 GLU B 386 ILE B 389 5 4
HELIX 38 38 LEU B 392 ALA B 402 1 11
HELIX 39 39 ASP B 407 CYS B 423 1 17
HELIX 40 40 ARG B 436 TYR B 444 1 9
HELIX 41 41 ALA B 481 GLY B 501 1 21
HELIX 42 42 THR C 25 LEU C 33 1 9
HELIX 43 43 SER C 57 GLY C 68 1 12
HELIX 44 44 THR C 80 GLU C 96 1 17
HELIX 45 45 SER C 97 ALA C 99 5 3
HELIX 46 46 SER C 222 GLU C 234 1 13
HELIX 47 47 LYS C 247 GLY C 259 1 13
HELIX 48 48 GLU C 260 LYS C 263 5 4
HELIX 49 49 ASN C 273 ARG C 279 1 7
HELIX 50 50 ARG C 279 GLU C 285 1 7
HELIX 51 51 ARG C 294 ILE C 301 1 8
HELIX 52 52 PRO C 302 GLY C 321 1 20
HELIX 53 53 LEU C 331 LYS C 336 5 6
HELIX 54 54 THR C 341 ALA C 356 1 16
HELIX 55 55 SER C 362 LYS C 367 1 6
HELIX 56 56 TYR C 370 ALA C 385 1 16
HELIX 57 57 GLU C 386 ILE C 389 5 4
HELIX 58 58 TYR C 390 ALA C 402 1 13
HELIX 59 59 ASP C 407 CYS C 423 1 17
HELIX 60 60 GLY C 435 TYR C 444 1 10
HELIX 61 61 ASN C 456 ALA C 463 1 8
HELIX 62 62 HIS C 464 TYR C 466 5 3
HELIX 63 63 ALA C 481 ARG C 500 1 20
HELIX 64 64 THR D 25 LEU D 33 1 9
HELIX 65 65 SER D 57 SER D 67 1 11
HELIX 66 66 THR D 80 SER D 97 1 18
HELIX 67 67 ASP D 145 MET D 149 5 5
HELIX 68 68 ASN D 163 VAL D 167 5 5
HELIX 69 69 SER D 222 GLN D 235 1 14
HELIX 70 70 LYS D 247 GLY D 259 1 13
HELIX 71 71 GLU D 260 LYS D 263 5 4
HELIX 72 72 ASN D 273 SER D 287 1 15
HELIX 73 73 ARG D 294 ILE D 301 1 8
HELIX 74 74 PRO D 302 GLY D 321 1 20
HELIX 75 75 LEU D 331 LYS D 336 5 6
HELIX 76 76 THR D 341 LEU D 353 1 13
HELIX 77 77 SER D 362 LYS D 367 1 6
HELIX 78 78 TYR D 370 ALA D 385 1 16
HELIX 79 79 GLU D 386 ILE D 389 5 4
HELIX 80 80 TYR D 390 ALA D 402 1 13
HELIX 81 81 ASP D 407 CYS D 423 1 17
HELIX 82 82 GLY D 435 TYR D 444 1 10
HELIX 83 83 ASN D 456 GLN D 462 1 7
HELIX 84 84 ALA D 481 GLY D 501 1 21
SHEET 1 A 9 GLY A 46 ILE A 51 0
SHEET 2 A 9 VAL A 71 ASN A 75 1 O ARG A 73 N CYS A 49
SHEET 3 A 9 ALA A 109 ASP A 113 1 O ALA A 111 N LEU A 74
SHEET 4 A 9 MET A 239 ALA A 242 1 O MET A 239 N LEU A 112
SHEET 5 A 9 LYS A 266 ILE A 271 1 O ILE A 268 N VAL A 240
SHEET 6 A 9 GLY A 289 ALA A 293 1 O MET A 291 N ILE A 271
SHEET 7 A 9 VAL A 324 ALA A 327 1 O ILE A 325 N ILE A 290
SHEET 8 A 9 CYS A 358 LEU A 361 1 O CYS A 358 N CYS A 326
SHEET 9 A 9 GLY A 46 ILE A 51 1 N ILE A 48 O LEU A 361
SHEET 1 B 5 VAL A 472 LEU A 473 0
SHEET 2 B 5 ILE A 450 THR A 454 1 N ALA A 452 O VAL A 472
SHEET 3 B 5 ILE A 428 LEU A 431 1 N VAL A 430 O ILE A 451
SHEET 4 B 5 VAL A 508 THR A 513 1 O LEU A 512 N ILE A 429
SHEET 5 B 5 VAL A 528 PRO A 529 -1 O VAL A 528 N VAL A 509
SHEET 1 C10 VAL A 472 LEU A 473 0
SHEET 2 C10 ILE A 450 THR A 454 1 N ALA A 452 O VAL A 472
SHEET 3 C10 ILE A 428 LEU A 431 1 N VAL A 430 O ILE A 451
SHEET 4 C10 VAL A 508 THR A 513 1 O LEU A 512 N ILE A 429
SHEET 5 C10 THR A 524 MET A 525 -1 O THR A 524 N THR A 513
SHEET 6 C10 MET B 525 PRO B 529 -1 O MET B 525 N MET A 525
SHEET 7 C10 VAL B 508 LEU B 512 -1 N VAL B 511 O ARG B 526
SHEET 8 C10 ILE B 428 LEU B 431 1 N ILE B 429 O LEU B 512
SHEET 9 C10 ILE B 450 THR B 454 1 O VAL B 453 N VAL B 430
SHEET 10 C10 ILE B 469 LEU B 473 1 O PHE B 470 N ILE B 450
SHEET 1 D 9 GLY B 46 ILE B 51 0
SHEET 2 D 9 MET B 69 ASN B 75 1 O ARG B 73 N CYS B 49
SHEET 3 D 9 ALA B 109 ASP B 113 1 O ALA B 111 N ALA B 72
SHEET 4 D 9 MET B 239 VAL B 240 1 O MET B 239 N LEU B 112
SHEET 5 D 9 LYS B 266 ILE B 271 1 O ILE B 268 N VAL B 240
SHEET 6 D 9 GLY B 289 ALA B 293 1 O MET B 291 N SER B 269
SHEET 7 D 9 VAL B 324 ALA B 327 1 O ILE B 325 N ILE B 290
SHEET 8 D 9 CYS B 358 MET B 360 1 O CYS B 358 N CYS B 326
SHEET 9 D 9 GLY B 46 ILE B 51 1 N ILE B 48 O ILE B 359
SHEET 1 E 4 ILE B 156 TRP B 158 0
SHEET 2 E 4 THR B 139 THR B 143 1 N THR B 143 O LEU B 157
SHEET 3 E 4 PHE B 192 GLU B 196 -1 O LEU B 193 N ILE B 142
SHEET 4 E 4 GLN B 187 LYS B 188 -1 N GLN B 187 O VAL B 194
SHEET 1 F 2 TYR B 175 VAL B 176 0
SHEET 2 F 2 VAL B 209 ASN B 210 -1 O ASN B 210 N TYR B 175
SHEET 1 G 9 GLY C 46 ILE C 51 0
SHEET 2 G 9 VAL C 71 ASN C 75 1 O ARG C 73 N CYS C 49
SHEET 3 G 9 ALA C 109 ASP C 113 1 O ALA C 111 N LEU C 74
SHEET 4 G 9 MET C 239 ALA C 242 1 O MET C 239 N LEU C 112
SHEET 5 G 9 LYS C 266 ILE C 271 1 O LYS C 266 N VAL C 240
SHEET 6 G 9 GLY C 289 ALA C 293 1 O MET C 291 N SER C 269
SHEET 7 G 9 VAL C 324 ALA C 327 1 O ALA C 327 N VAL C 292
SHEET 8 G 9 CYS C 358 LEU C 361 1 O CYS C 358 N CYS C 326
SHEET 9 G 9 GLY C 46 ILE C 51 1 N ILE C 48 O LEU C 361
SHEET 1 H10 VAL C 472 LEU C 473 0
SHEET 2 H10 ILE C 450 THR C 454 1 N ALA C 452 O VAL C 472
SHEET 3 H10 ILE C 428 LEU C 431 1 N VAL C 430 O VAL C 453
SHEET 4 H10 VAL C 508 LEU C 512 1 O LEU C 512 N ILE C 429
SHEET 5 H10 THR C 524 PRO C 529 -1 O VAL C 528 N VAL C 509
SHEET 6 H10 MET D 525 PRO D 529 -1 O MET D 525 N MET C 525
SHEET 7 H10 VAL D 508 LEU D 512 -1 N VAL D 511 O ARG D 526
SHEET 8 H10 ILE D 428 LEU D 431 1 N ILE D 429 O LEU D 512
SHEET 9 H10 ILE D 450 THR D 454 1 O VAL D 453 N VAL D 430
SHEET 10 H10 ILE D 469 LEU D 473 1 O PHE D 470 N ILE D 450
SHEET 1 I 9 GLY D 46 ILE D 51 0
SHEET 2 I 9 VAL D 71 ASN D 75 1 O ARG D 73 N CYS D 49
SHEET 3 I 9 ALA D 109 ASP D 113 1 O ALA D 111 N ALA D 72
SHEET 4 I 9 MET D 239 ALA D 242 1 O MET D 239 N LEU D 112
SHEET 5 I 9 LYS D 266 ILE D 271 1 O ILE D 268 N VAL D 240
SHEET 6 I 9 GLY D 289 ALA D 293 1 O MET D 291 N SER D 269
SHEET 7 I 9 VAL D 324 ALA D 327 1 O ILE D 325 N ILE D 290
SHEET 8 I 9 CYS D 358 MET D 360 1 O CYS D 358 N CYS D 326
SHEET 9 I 9 GLY D 46 ILE D 51 1 N ILE D 48 O ILE D 359
SHEET 1 J 4 ILE D 156 TRP D 158 0
SHEET 2 J 4 THR D 139 THR D 143 1 N THR D 143 O LEU D 157
SHEET 3 J 4 PHE D 192 ASN D 199 -1 O THR D 195 N LEU D 140
SHEET 4 J 4 GLN D 187 LYS D 188 -1 N GLN D 187 O VAL D 194
SHEET 1 K 6 ILE D 156 TRP D 158 0
SHEET 2 K 6 THR D 139 THR D 143 1 N THR D 143 O LEU D 157
SHEET 3 K 6 PHE D 192 ASN D 199 -1 O THR D 195 N LEU D 140
SHEET 4 K 6 ILE D 181 LEU D 183 -1 N SER D 182 O ASN D 199
SHEET 5 K 6 ILE D 174 VAL D 176 -1 N ILE D 174 O LEU D 183
SHEET 6 K 6 VAL D 209 ASN D 210 -1 O ASN D 210 N TYR D 175
CISPEP 1 PRO B 212 GLY B 213 0 -8.63
CISPEP 2 LEU B 218 PRO B 219 0 2.74
CISPEP 3 GLY B 518 SER B 519 0 -4.05
CISPEP 4 GLY D 518 SER D 519 0 -11.30
SITE 1 AC1 5 ASN A 44 ASN A 70 HIS A 464 TYR A 466
SITE 2 AC1 5 ILE A 469
SITE 1 AC2 5 GLY B 46 ASN B 70 HIS B 464 ILE B 469
SITE 2 AC2 5 PHE B 470
SITE 1 AC3 6 ASN C 44 ASN C 70 HIS C 464 TYR C 466
SITE 2 AC3 6 ILE C 469 PHE C 470
SITE 1 AC4 6 ASN D 44 GLY D 46 ASN D 70 HIS D 464
SITE 2 AC4 6 ILE D 469 PHE D 470
CRYST1 124.455 124.455 257.049 90.00 90.00 120.00 P 31 12
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 0.008035 0.004639 0.000000 0.00000
SCALE2 0.000000 0.009278 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003890 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
