HEADER TRANSFERASE 22-MAY-14 4QG9
TITLE CRYSTAL STRUCTURE OF PKM2-R399E 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 4QG9 1 JRNL REMARK SEQADV LINK
REVDAT 2 25-MAR-15 4QG9 1 TITLE
REVDAT 1 25-FEB-15 4QG9 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. 2.38 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) : 2.38
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 87765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4385
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 43.6539 - 7.3870 0.98 2912 157 0.2071 0.2354
REMARK 3 2 7.3870 - 5.8678 1.00 2890 154 0.2381 0.3059
REMARK 3 3 5.8678 - 5.1274 1.00 2867 127 0.2113 0.2401
REMARK 3 4 5.1274 - 4.6591 1.00 2875 142 0.1814 0.2068
REMARK 3 5 4.6591 - 4.3255 1.00 2847 144 0.1739 0.1876
REMARK 3 6 4.3255 - 4.0707 1.00 2836 145 0.1842 0.2414
REMARK 3 7 4.0707 - 3.8670 1.00 2839 147 0.1958 0.2047
REMARK 3 8 3.8670 - 3.6987 1.00 2798 163 0.1947 0.2290
REMARK 3 9 3.6987 - 3.5564 1.00 2788 167 0.1960 0.2234
REMARK 3 10 3.5564 - 3.4337 1.00 2854 147 0.1986 0.2644
REMARK 3 11 3.4337 - 3.3264 1.00 2846 126 0.2103 0.2626
REMARK 3 12 3.3264 - 3.2313 1.00 2780 151 0.2236 0.2713
REMARK 3 13 3.2313 - 3.1463 1.00 2848 146 0.2257 0.2663
REMARK 3 14 3.1463 - 3.0696 1.00 2809 140 0.2325 0.3032
REMARK 3 15 3.0696 - 2.9998 1.00 2811 153 0.2270 0.2604
REMARK 3 16 2.9998 - 2.9360 1.00 2827 155 0.2228 0.2837
REMARK 3 17 2.9360 - 2.8773 1.00 2830 143 0.2320 0.2897
REMARK 3 18 2.8773 - 2.8230 1.00 2814 146 0.2234 0.3134
REMARK 3 19 2.8230 - 2.7726 1.00 2809 148 0.2170 0.2836
REMARK 3 20 2.7726 - 2.7256 1.00 2747 176 0.2243 0.2787
REMARK 3 21 2.7256 - 2.6816 1.00 2850 131 0.2155 0.3176
REMARK 3 22 2.6816 - 2.6404 1.00 2775 146 0.2239 0.2832
REMARK 3 23 2.6404 - 2.6015 1.00 2828 168 0.2351 0.2886
REMARK 3 24 2.6015 - 2.5649 1.00 2818 151 0.2287 0.3116
REMARK 3 25 2.5649 - 2.5302 1.00 2785 128 0.2271 0.3663
REMARK 3 26 2.5302 - 2.4974 1.00 2854 158 0.2361 0.2660
REMARK 3 27 2.4974 - 2.4662 1.00 2755 142 0.2346 0.3032
REMARK 3 28 2.4662 - 2.4365 1.00 2818 144 0.2405 0.3095
REMARK 3 29 2.4365 - 2.4081 1.00 2822 170 0.2522 0.3647
REMARK 3 30 2.4081 - 2.3811 0.52 1448 70 0.2613 0.3333
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.710
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 : 0.002 14237
REMARK 3 ANGLE : 0.572 19221
REMARK 3 CHIRALITY : 0.040 2208
REMARK 3 PLANARITY : 0.002 2505
REMARK 3 DIHEDRAL : 13.216 5392
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 4QG9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000086016.
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 : 7.0
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 : 87765
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.381
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 (%) : 98.3
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 (%): 48.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CAAC2, 20% PEG3350, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.59000
REMARK 290 SMTRY3 2 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: 14460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 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 SER A 127
REMARK 465 GLY A 128
REMARK 465 THR A 129
REMARK 465 ILE A 404
REMARK 465 THR A 405
REMARK 465 SER A 406
REMARK 465 SER A 519
REMARK 465 GLY A 520
REMARK 465 PHE A 521
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 ILE B 404
REMARK 465 THR B 405
REMARK 465 SER B 519
REMARK 465 GLY B 520
REMARK 465 PHE B 521
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 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 ILE C 404
REMARK 465 THR C 405
REMARK 465 SER C 406
REMARK 465 GLY C 520
REMARK 465 PHE C 521
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 ASP D 24
REMARK 465 GLU D 118
REMARK 465 ILE D 119
REMARK 465 ARG D 120
REMARK 465 THR D 121
REMARK 465 GLY D 122
REMARK 465 LEU D 123
REMARK 465 ILE D 124
REMARK 465 LYS D 125
REMARK 465 GLY D 126
REMARK 465 SER D 127
REMARK 465 GLY D 128
REMARK 465 THR D 129
REMARK 465 ALA D 130
REMARK 465 GLU D 131
REMARK 465 VAL D 132
REMARK 465 GLU D 133
REMARK 465 LEU D 134
REMARK 465 LYS D 135
REMARK 465 LYS D 136
REMARK 465 GLY D 137
REMARK 465 ALA D 138
REMARK 465 THR D 139
REMARK 465 LEU D 140
REMARK 465 LYS D 141
REMARK 465 ILE D 142
REMARK 465 THR D 143
REMARK 465 LEU D 144
REMARK 465 ASP D 145
REMARK 465 ASN D 146
REMARK 465 ALA D 147
REMARK 465 TYR D 148
REMARK 465 MET D 149
REMARK 465 GLU D 150
REMARK 465 LYS D 151
REMARK 465 CYS D 152
REMARK 465 ASP D 153
REMARK 465 GLU D 154
REMARK 465 ASN D 155
REMARK 465 ILE D 156
REMARK 465 LEU D 157
REMARK 465 TRP D 158
REMARK 465 LEU D 159
REMARK 465 ASP D 160
REMARK 465 TYR D 161
REMARK 465 LYS D 162
REMARK 465 ASN D 163
REMARK 465 ILE D 164
REMARK 465 CYS D 165
REMARK 465 LYS D 166
REMARK 465 VAL D 167
REMARK 465 VAL D 168
REMARK 465 GLU D 169
REMARK 465 VAL D 170
REMARK 465 GLY D 171
REMARK 465 SER D 172
REMARK 465 LYS D 173
REMARK 465 ILE D 174
REMARK 465 TYR D 175
REMARK 465 VAL D 176
REMARK 465 ASP D 177
REMARK 465 ASP D 178
REMARK 465 GLY D 179
REMARK 465 LEU D 180
REMARK 465 ILE D 181
REMARK 465 SER D 182
REMARK 465 LEU D 183
REMARK 465 GLN D 184
REMARK 465 VAL D 185
REMARK 465 LYS D 186
REMARK 465 GLN D 187
REMARK 465 LYS D 188
REMARK 465 GLY D 189
REMARK 465 ALA D 190
REMARK 465 ASP D 191
REMARK 465 PHE D 192
REMARK 465 LEU D 193
REMARK 465 VAL D 194
REMARK 465 THR D 195
REMARK 465 GLU D 196
REMARK 465 VAL D 197
REMARK 465 GLU D 198
REMARK 465 ASN D 199
REMARK 465 GLY D 200
REMARK 465 GLY D 201
REMARK 465 SER D 202
REMARK 465 LEU D 203
REMARK 465 GLY D 204
REMARK 465 SER D 205
REMARK 465 LYS D 206
REMARK 465 LYS D 207
REMARK 465 GLY D 208
REMARK 465 VAL D 209
REMARK 465 ASN D 210
REMARK 465 LEU D 211
REMARK 465 PRO D 212
REMARK 465 GLY D 213
REMARK 465 ALA D 214
REMARK 465 ALA D 215
REMARK 465 PRO D 403
REMARK 465 ILE D 404
REMARK 465 THR D 405
REMARK 465 SER D 406
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 ASP A 36 35.35 -94.19
REMARK 500 THR A 121 -141.67 -79.99
REMARK 500 VAL A 132 -169.54 -112.59
REMARK 500 ASP A 153 -158.10 -159.04
REMARK 500 ASP A 177 77.27 58.97
REMARK 500 ASP A 191 35.41 -156.77
REMARK 500 THR A 328 144.07 68.33
REMARK 500 MET A 330 -72.53 -95.66
REMARK 500 SER A 362 -108.08 -109.32
REMARK 500 ILE B 40 42.97 -108.18
REMARK 500 THR B 129 85.22 -155.95
REMARK 500 ALA B 130 96.52 72.50
REMARK 500 ASP B 153 -158.28 -154.02
REMARK 500 ASP B 177 60.73 62.38
REMARK 500 THR B 328 145.58 66.25
REMARK 500 MET B 330 -71.02 -115.65
REMARK 500 SER B 362 -103.38 -107.96
REMARK 500 ARG B 445 71.45 52.51
REMARK 500 SER C 55 20.69 -140.16
REMARK 500 ARG C 279 33.68 -98.77
REMARK 500 THR C 328 145.84 67.38
REMARK 500 MET C 330 -68.00 -96.70
REMARK 500 SER C 362 -106.10 -112.45
REMARK 500 ARG D 279 35.15 -95.70
REMARK 500 THR D 328 145.60 66.57
REMARK 500 MET D 330 -83.48 -99.64
REMARK 500 SER D 362 -101.22 -117.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 272 OE1
REMARK 620 2 ASP A 296 OD1 66.5
REMARK 620 3 HOH A1181 O 110.1 136.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 118 OE2
REMARK 620 2 GLU B 272 OE1 82.3
REMARK 620 3 HOH B1108 O 80.4 75.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RPP RELATED DB: PDB
REMARK 900 RELATED ID: 4QGC RELATED DB: PDB
REMARK 900 RELATED ID: 4QG8 RELATED DB: PDB
REMARK 900 RELATED ID: 4QG6 RELATED DB: PDB
DBREF 4QG9 A 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4QG9 B 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4QG9 C 1 531 UNP P14618 KPYM_HUMAN 1 531
DBREF 4QG9 D 1 531 UNP P14618 KPYM_HUMAN 1 531
SEQADV 4QG9 GLY A -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 PRO A -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLY A -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 SER A 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLU A 399 UNP P14618 ARG 399 ENGINEERED MUTATION
SEQADV 4QG9 GLY B -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 PRO B -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLY B -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 SER B 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLU B 399 UNP P14618 ARG 399 ENGINEERED MUTATION
SEQADV 4QG9 GLY C -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 PRO C -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLY C -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 SER C 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLU C 399 UNP P14618 ARG 399 ENGINEERED MUTATION
SEQADV 4QG9 GLY D -3 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 PRO D -2 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLY D -1 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 SER D 0 UNP P14618 EXPRESSION TAG
SEQADV 4QG9 GLU D 399 UNP P14618 ARG 399 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 TYR 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 GLU
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 TYR 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 GLU
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 TYR 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 GLU
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 TYR 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 GLU
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 MG A1001 1
HET ACT A1002 4
HET MG B1001 1
HET ACT B1002 4
HET MG C1001 1
HET ACT C1002 4
HET ACT D 601 4
HETNAM MG MAGNESIUM ION
HETNAM ACT ACETATE ION
FORMUL 5 MG 3(MG 2+)
FORMUL 6 ACT 4(C2 H3 O2 1-)
FORMUL 12 HOH *448(H2 O)
HELIX 1 1 THR A 25 ARG A 32 1 8
HELIX 2 2 SER A 57 GLY A 68 1 12
HELIX 3 3 THR A 80 GLU A 96 1 17
HELIX 4 4 SER A 97 ALA A 99 5 3
HELIX 5 5 ASP A 145 MET A 149 5 5
HELIX 6 6 ASN A 163 VAL A 168 1 6
HELIX 7 7 SER A 222 GLN A 235 1 14
HELIX 8 8 LYS A 247 GLY A 259 1 13
HELIX 9 9 ASN A 273 ARG A 279 1 7
HELIX 10 10 ARG A 279 SER A 287 1 9
HELIX 11 11 ARG A 294 ILE A 301 1 8
HELIX 12 12 PRO A 302 GLY A 321 1 20
HELIX 13 13 LEU A 331 LYS A 336 5 6
HELIX 14 14 THR A 341 GLY A 355 1 15
HELIX 15 15 SER A 362 LYS A 367 1 6
HELIX 16 16 TYR A 370 GLU A 386 1 17
HELIX 17 17 ALA A 387 ILE A 389 5 3
HELIX 18 18 TYR A 390 LEU A 401 1 12
HELIX 19 19 PRO A 408 CYS A 423 1 16
HELIX 20 20 GLY A 435 ARG A 443 1 9
HELIX 21 21 ASN A 456 ALA A 463 1 8
HELIX 22 22 HIS A 464 TYR A 466 5 3
HELIX 23 23 ALA A 481 ARG A 500 1 20
HELIX 24 24 THR B 25 ARG B 32 1 8
HELIX 25 25 SER B 57 GLY B 68 1 12
HELIX 26 26 THR B 80 GLU B 96 1 17
HELIX 27 27 SER B 97 ALA B 99 5 3
HELIX 28 28 ASP B 145 MET B 149 5 5
HELIX 29 29 ASN B 163 VAL B 168 1 6
HELIX 30 30 SER B 222 GLN B 235 1 14
HELIX 31 31 LYS B 247 GLY B 259 1 13
HELIX 32 32 ASN B 273 ARG B 279 1 7
HELIX 33 33 ARG B 279 SER B 287 1 9
HELIX 34 34 ARG B 294 ILE B 301 1 8
HELIX 35 35 PRO B 302 GLY B 321 1 20
HELIX 36 36 LEU B 331 LYS B 336 5 6
HELIX 37 37 THR B 341 GLY B 355 1 15
HELIX 38 38 SER B 362 LYS B 367 1 6
HELIX 39 39 TYR B 370 GLU B 386 1 17
HELIX 40 40 ALA B 387 ILE B 389 5 3
HELIX 41 41 TYR B 390 LEU B 401 1 12
HELIX 42 42 ASP B 407 CYS B 423 1 17
HELIX 43 43 GLY B 435 ARG B 443 1 9
HELIX 44 44 ASN B 456 ALA B 463 1 8
HELIX 45 45 HIS B 464 TYR B 466 5 3
HELIX 46 46 ALA B 481 ARG B 500 1 20
HELIX 47 47 THR C 25 ARG C 32 1 8
HELIX 48 48 SER C 57 GLY C 68 1 12
HELIX 49 49 THR C 80 SER C 97 1 18
HELIX 50 50 SER C 222 GLN C 235 1 14
HELIX 51 51 LYS C 247 GLY C 259 1 13
HELIX 52 52 GLU C 260 LYS C 263 5 4
HELIX 53 53 ASN C 273 ARG C 279 1 7
HELIX 54 54 ARG C 279 SER C 287 1 9
HELIX 55 55 ARG C 294 ILE C 301 1 8
HELIX 56 56 PRO C 302 GLY C 321 1 20
HELIX 57 57 LEU C 331 LYS C 336 5 6
HELIX 58 58 THR C 341 GLY C 355 1 15
HELIX 59 59 SER C 362 LYS C 367 1 6
HELIX 60 60 TYR C 370 GLU C 386 1 17
HELIX 61 61 ALA C 387 ILE C 389 5 3
HELIX 62 62 TYR C 390 LEU C 401 1 12
HELIX 63 63 PRO C 408 CYS C 423 1 16
HELIX 64 64 GLY C 435 ARG C 443 1 9
HELIX 65 65 ASN C 456 ALA C 463 1 8
HELIX 66 66 HIS C 464 TYR C 466 5 3
HELIX 67 67 ALA C 481 ARG C 500 1 20
HELIX 68 68 PHE D 26 ARG D 32 1 7
HELIX 69 69 SER D 57 SER D 67 1 11
HELIX 70 70 THR D 80 SER D 97 1 18
HELIX 71 71 SER D 222 GLN D 235 1 14
HELIX 72 72 LYS D 247 GLY D 259 1 13
HELIX 73 73 ASN D 273 ARG D 279 1 7
HELIX 74 74 ARG D 279 SER D 287 1 9
HELIX 75 75 ARG D 294 ILE D 301 1 8
HELIX 76 76 PRO D 302 GLY D 321 1 20
HELIX 77 77 LEU D 331 LYS D 336 5 6
HELIX 78 78 THR D 341 GLY D 355 1 15
HELIX 79 79 SER D 362 LYS D 367 1 6
HELIX 80 80 TYR D 370 ALA D 385 1 16
HELIX 81 81 GLU D 386 ILE D 389 5 4
HELIX 82 82 TYR D 390 LEU D 401 1 12
HELIX 83 83 PRO D 408 CYS D 423 1 16
HELIX 84 84 GLY D 435 TYR D 444 1 10
HELIX 85 85 ASN D 456 ALA D 463 1 8
HELIX 86 86 HIS D 464 TYR D 466 5 3
HELIX 87 87 ALA D 481 GLY D 501 1 21
SHEET 1 A 9 GLY A 46 THR A 50 0
SHEET 2 A 9 VAL A 71 ASN A 75 1 O VAL A 71 N CYS A 49
SHEET 3 A 9 ALA A 109 ASP A 113 1 O ALA A 111 N ALA A 72
SHEET 4 A 9 MET A 239 ALA A 242 1 O PHE A 241 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 SER A 269
SHEET 7 A 9 VAL A 324 ALA A 327 1 O ILE A 325 N VAL A 292
SHEET 8 A 9 CYS A 358 LEU A 361 1 O MET A 360 N CYS A 326
SHEET 9 A 9 GLY A 46 THR A 50 1 N ILE A 48 O LEU A 361
SHEET 1 B 7 ILE A 119 ARG A 120 0
SHEET 2 B 7 GLY A 208 ASN A 210 -1 O VAL A 209 N ILE A 119
SHEET 3 B 7 LYS A 173 VAL A 176 -1 N TYR A 175 O ASN A 210
SHEET 4 B 7 ILE A 181 GLN A 187 -1 O ILE A 181 N VAL A 176
SHEET 5 B 7 LEU A 193 ASN A 199 -1 O VAL A 194 N LYS A 186
SHEET 6 B 7 THR A 139 THR A 143 -1 N ILE A 142 O LEU A 193
SHEET 7 B 7 ILE A 156 TRP A 158 1 O LEU A 157 N THR A 143
SHEET 1 C10 ILE A 469 LEU A 473 0
SHEET 2 C10 ILE A 450 THR A 454 1 N ILE A 450 O PHE A 470
SHEET 3 C10 ILE A 428 LEU A 431 1 N VAL A 430 O VAL A 453
SHEET 4 C10 VAL A 508 THR A 513 1 O ILE A 510 N ILE A 429
SHEET 5 C10 THR A 524 PRO A 529 -1 O VAL A 528 N VAL A 509
SHEET 6 C10 THR C 524 PRO C 529 -1 O MET C 525 N MET A 525
SHEET 7 C10 VAL C 508 THR C 513 -1 N VAL C 509 O VAL C 528
SHEET 8 C10 ILE C 428 LEU C 431 1 N ILE C 429 O ILE C 510
SHEET 9 C10 ILE C 450 THR C 454 1 O VAL C 453 N VAL C 430
SHEET 10 C10 ILE C 469 LEU C 473 1 O PHE C 470 N ILE C 450
SHEET 1 D 9 GLY B 46 THR B 50 0
SHEET 2 D 9 VAL B 71 ASN B 75 1 O VAL B 71 N CYS B 49
SHEET 3 D 9 ALA B 109 ASP B 113 1 O ALA B 111 N LEU B 74
SHEET 4 D 9 MET B 239 ALA B 242 1 O PHE B 241 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 ILE B 271
SHEET 7 D 9 VAL B 324 ALA B 327 1 O ILE B 325 N VAL B 292
SHEET 8 D 9 CYS B 358 LEU B 361 1 O MET B 360 N CYS B 326
SHEET 9 D 9 GLY B 46 THR B 50 1 N ILE B 48 O LEU B 361
SHEET 1 E 7 ILE B 119 ARG B 120 0
SHEET 2 E 7 GLY B 208 ASN B 210 -1 O VAL B 209 N ILE B 119
SHEET 3 E 7 LYS B 173 VAL B 176 -1 N TYR B 175 O ASN B 210
SHEET 4 E 7 ILE B 181 LYS B 188 -1 O ILE B 181 N VAL B 176
SHEET 5 E 7 PHE B 192 ASN B 199 -1 O VAL B 194 N LYS B 186
SHEET 6 E 7 THR B 139 THR B 143 -1 N ILE B 142 O LEU B 193
SHEET 7 E 7 ILE B 156 TRP B 158 1 O LEU B 157 N LYS B 141
SHEET 1 F 2 VAL B 132 LEU B 134 0
SHEET 2 F 2 GLY B 201 LEU B 203 -1 O LEU B 203 N VAL B 132
SHEET 1 G10 ILE B 469 LEU B 473 0
SHEET 2 G10 ILE B 450 THR B 454 1 N ILE B 450 O PHE B 470
SHEET 3 G10 ALA B 427 LEU B 431 1 N VAL B 430 O ILE B 451
SHEET 4 G10 VAL B 508 THR B 513 1 O ILE B 510 N ILE B 429
SHEET 5 G10 THR B 524 PRO B 529 -1 O VAL B 528 N VAL B 509
SHEET 6 G10 THR D 524 PRO D 529 -1 O MET D 525 N MET B 525
SHEET 7 G10 VAL D 508 THR D 513 -1 N THR D 513 O THR D 524
SHEET 8 G10 ILE D 428 LEU D 431 1 N ILE D 429 O ILE D 510
SHEET 9 G10 ILE D 450 THR D 454 1 O ILE D 451 N VAL D 430
SHEET 10 G10 ILE D 469 LEU D 473 1 O PHE D 470 N ILE D 450
SHEET 1 H 9 GLY C 46 THR C 50 0
SHEET 2 H 9 VAL C 71 ASN C 75 1 O VAL C 71 N CYS C 49
SHEET 3 H 9 ALA C 109 ASP C 113 1 O ALA C 111 N ALA C 72
SHEET 4 H 9 MET C 239 ALA C 242 1 O PHE C 241 N LEU C 112
SHEET 5 H 9 LYS C 266 ILE C 271 1 O ILE C 268 N VAL C 240
SHEET 6 H 9 GLY C 289 ALA C 293 1 O MET C 291 N SER C 269
SHEET 7 H 9 VAL C 324 ALA C 327 1 O ILE C 325 N VAL C 292
SHEET 8 H 9 CYS C 358 LEU C 361 1 O MET C 360 N CYS C 326
SHEET 9 H 9 GLY C 46 THR C 50 1 N ILE C 48 O LEU C 361
SHEET 1 I 9 GLY D 46 THR D 50 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 109 N ALA D 72
SHEET 4 I 9 MET D 239 ALA D 242 1 O PHE D 241 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 ILE D 271
SHEET 7 I 9 VAL D 324 ALA D 327 1 O ILE D 325 N VAL D 292
SHEET 8 I 9 CYS D 358 LEU D 361 1 O MET D 360 N CYS D 326
SHEET 9 I 9 GLY D 46 THR D 50 1 N ILE D 48 O LEU D 361
LINK OE1 GLU A 272 MG MG A1001 1555 1555 2.81
LINK OD1 ASP A 296 MG MG A1001 1555 1555 2.72
LINK MG MG A1001 O HOH A1181 1555 1555 2.36
LINK OE2 GLU B 118 MG MG B1001 1555 1555 2.31
LINK OE1 GLU B 272 MG MG B1001 1555 1555 2.45
LINK MG MG B1001 O HOH B1108 1555 1555 2.39
CISPEP 1 THR B 129 ALA B 130 0 1.75
SITE 1 AC1 3 GLU A 272 ASP A 296 HOH A1181
SITE 1 AC2 5 THR A 432 LYS A 433 SER A 434 ARG A 436
SITE 2 AC2 5 SER A 437
SITE 1 AC3 5 GLU B 118 ASP B 178 GLU B 272 ASP B 296
SITE 2 AC3 5 HOH B1108
SITE 1 AC4 5 THR B 432 LYS B 433 SER B 434 ARG B 436
SITE 2 AC4 5 SER B 437
SITE 1 AC5 2 GLU C 272 ASP C 296
SITE 1 AC6 5 THR C 432 LYS C 433 SER C 434 SER C 437
SITE 2 AC6 5 HOH C1219
SITE 1 AC7 6 THR D 432 LYS D 433 SER D 434 ARG D 436
SITE 2 AC7 6 SER D 437 GLY D 520
CRYST1 95.632 71.180 170.289 90.00 104.25 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010457 0.000000 0.002655 0.00000
SCALE2 0.000000 0.014049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
