HEADER TRANSFERASE/PROTEIN BINDING 26-MAR-12 4EC9
TITLE CRYSTAL STRUCTURE OF FULL-LENGTH CDK9 IN COMPLEX WITH CYCLIN T
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 9;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: C-2K, CELL DIVISION CYCLE 2-LIKE PROTEIN KINASE 4, CELL
COMPND 5 DIVISION PROTEIN KINASE 9, SERINE/THREONINE-PROTEIN KINASE PITALRE,
COMPND 6 TAT-ASSOCIATED KINASE COMPLEX CATALYTIC SUBUNIT;
COMPND 7 EC: 2.7.11.22, 2.7.11.23;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CYCLIN-T1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 2-259;
COMPND 13 SYNONYM: CYCT1, CYCLIN-T;
COMPND 14 ENGINEERED: YES;
COMPND 15 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: CDC2L4, CDK9, TAK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL1392;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CCNT1;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PVL1392
KEYWDS CYCLIN DEPENDENT KINASE, CYCLIN, KINASE, PHOSPHORYLATION, NUCLEAR,
KEYWDS 2 TRANSFERASE-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BAUMLI,A.J.HOLE,J.A.ENDICOTT
REVDAT 2 02-JAN-13 4EC9 1 JRNL
REVDAT 1 12-SEP-12 4EC9 0
JRNL AUTH S.BAUMLI,A.J.HOLE,L.Z.WANG,M.E.NOBLE,J.A.ENDICOTT
JRNL TITL THE CDK9 TAIL DETERMINES THE REACTION PATHWAY OF POSITIVE
JRNL TITL 2 TRANSCRIPTION ELONGATION FACTOR B.
JRNL REF STRUCTURE V. 20 1788 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22959624
JRNL DOI 10.1016/J.STR.2012.08.011
REMARK 2
REMARK 2 RESOLUTION. 3.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 17257
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 877
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 46.6047 - 5.8263 0.97 2791 153 0.1950 0.2293
REMARK 3 2 5.8263 - 4.6259 0.99 2818 161 0.1932 0.2146
REMARK 3 3 4.6259 - 4.0415 0.98 2864 144 0.1698 0.2152
REMARK 3 4 4.0415 - 3.6722 0.97 2771 141 0.2119 0.2326
REMARK 3 5 3.6722 - 3.4090 0.93 2648 159 0.2528 0.2800
REMARK 3 6 3.4090 - 3.2081 0.86 2488 119 0.2953 0.3509
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.89
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 106.09
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 144.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.71160
REMARK 3 B22 (A**2) : -4.71160
REMARK 3 B33 (A**2) : 9.42320
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
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 : 0.008 4635
REMARK 3 ANGLE : 1.456 6283
REMARK 3 CHIRALITY : 0.071 707
REMARK 3 PLANARITY : 0.008 794
REMARK 3 DIHEDRAL : 13.178 1736
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 4EC9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071436.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93300
REMARK 200 MONOCHROMATOR : SINGLE SILICON MONOCHROMATOR AND
REMARK 200 TOROIDAL FOCUSING MIRROR
REMARK 200 OPTICS : SINGLE SILICON (111)
REMARK 200 MONOCHROMATOR AND TOROIDAL
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17982
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.208
REMARK 200 RESOLUTION RANGE LOW (A) : 46.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
REMARK 200 R SYM FOR SHELL (I) : 0.51400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX.REFINE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1% PEG 1K, 200MM NK PHSOPHATE, PH 6.2,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 87.11450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 50.29558
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 32.66333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 87.11450
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 50.29558
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 32.66333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 87.11450
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 50.29558
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.66333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.59116
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 65.32667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 100.59116
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 65.32667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 100.59116
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 65.32667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 TYR A 5
REMARK 465 ASP A 6
REMARK 465 GLN A 27
REMARK 465 GLY A 28
REMARK 465 THR A 29
REMARK 465 PHE A 30
REMARK 465 ALA A 89
REMARK 465 SER A 90
REMARK 465 PRO A 91
REMARK 465 TYR A 92
REMARK 465 ASN A 93
REMARK 465 ARG A 94
REMARK 465 CYS A 95
REMARK 465 LYS A 96
REMARK 465 GLN A 271
REMARK 465 LYS A 272
REMARK 465 LEU A 328
REMARK 465 SER A 329
REMARK 465 THR A 330
REMARK 465 HIS A 331
REMARK 465 LEU A 332
REMARK 465 THR A 333
REMARK 465 SER A 334
REMARK 465 MET A 335
REMARK 465 PHE A 336
REMARK 465 GLU A 337
REMARK 465 TYR A 338
REMARK 465 LEU A 339
REMARK 465 ALA A 340
REMARK 465 PRO A 341
REMARK 465 PRO A 342
REMARK 465 ARG A 343
REMARK 465 ARG A 344
REMARK 465 LYS A 345
REMARK 465 GLY A 346
REMARK 465 SER A 347
REMARK 465 GLN A 348
REMARK 465 ILE A 349
REMARK 465 THR A 350
REMARK 465 GLN A 351
REMARK 465 GLN A 352
REMARK 465 SER A 353
REMARK 465 THR A 354
REMARK 465 ASN A 355
REMARK 465 GLN A 356
REMARK 465 SER A 357
REMARK 465 ARG A 358
REMARK 465 ASN A 359
REMARK 465 PRO A 360
REMARK 465 ALA A 361
REMARK 465 THR A 362
REMARK 465 THR A 363
REMARK 465 ASN A 364
REMARK 465 GLN A 365
REMARK 465 THR A 366
REMARK 465 GLU A 367
REMARK 465 PHE A 368
REMARK 465 GLU A 369
REMARK 465 ARG A 370
REMARK 465 VAL A 371
REMARK 465 PHE A 372
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 GLU B 2
REMARK 465 GLY B 3
REMARK 465 GLU B 4
REMARK 465 ARG B 5
REMARK 465 LYS B 6
REMARK 465 ASN B 7
REMARK 465 ASN B 8
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 CYS A 10 57.66 -155.71
REMARK 500 LYS A 24 98.61 -61.22
REMARK 500 GLU A 53 -59.20 -26.60
REMARK 500 ASN A 54 -64.91 -125.18
REMARK 500 GLU A 55 77.15 45.13
REMARK 500 LEU A 118 12.78 -69.70
REMARK 500 ASP A 149 40.98 -141.10
REMARK 500 ASP A 167 78.14 63.86
REMARK 500 LYS A 178 -158.19 -93.58
REMARK 500 ARG A 184 68.18 -117.75
REMARK 500 VAL A 190 133.17 84.51
REMARK 500 ASP A 205 64.88 -112.87
REMARK 500 SER A 226 141.12 -170.79
REMARK 500 THR A 249 133.03 -170.73
REMARK 500 ASN A 255 -2.24 85.35
REMARK 500 ASN A 258 -29.20 -38.53
REMARK 500 TYR A 262 -71.27 -52.47
REMARK 500 LYS A 264 1.55 -62.45
REMARK 500 GLU A 266 71.10 42.74
REMARK 500 LEU A 296 49.52 -85.30
REMARK 500 ASP A 318 -57.75 -28.70
REMARK 500 ASP A 323 171.14 -53.62
REMARK 500 LYS A 325 -77.37 -29.26
REMARK 500 THR B 121 5.32 -62.93
REMARK 500 PHE B 146 15.65 57.91
REMARK 500 LEU B 163 17.65 -69.13
REMARK 500 ASN B 250 -8.28 75.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EC8 RELATED DB: PDB
DBREF 4EC9 A 2 372 UNP P50750 CDK9_HUMAN 2 372
DBREF 4EC9 B 2 259 UNP O60563 CCNT1_HUMAN 2 259
SEQADV 4EC9 GLY A 0 UNP P50750 EXPRESSION TAG
SEQADV 4EC9 PRO A 1 UNP P50750 EXPRESSION TAG
SEQADV 4EC9 GLY B 0 UNP O60563 EXPRESSION TAG
SEQADV 4EC9 PRO B 1 UNP O60563 EXPRESSION TAG
SEQADV 4EC9 ARG B 77 UNP O60563 GLN 77 ENGINEERED MUTATION
SEQADV 4EC9 GLY B 96 UNP O60563 GLU 96 ENGINEERED MUTATION
SEQADV 4EC9 LEU B 241 UNP O60563 PHE 241 ENGINEERED MUTATION
SEQRES 1 A 373 GLY PRO ALA LYS GLN TYR ASP SER VAL GLU CYS PRO PHE
SEQRES 2 A 373 CYS ASP GLU VAL SER LYS TYR GLU LYS LEU ALA LYS ILE
SEQRES 3 A 373 GLY GLN GLY THR PHE GLY GLU VAL PHE LYS ALA ARG HIS
SEQRES 4 A 373 ARG LYS THR GLY GLN LYS VAL ALA LEU LYS LYS VAL LEU
SEQRES 5 A 373 MET GLU ASN GLU LYS GLU GLY PHE PRO ILE THR ALA LEU
SEQRES 6 A 373 ARG GLU ILE LYS ILE LEU GLN LEU LEU LYS HIS GLU ASN
SEQRES 7 A 373 VAL VAL ASN LEU ILE GLU ILE CYS ARG THR LYS ALA SER
SEQRES 8 A 373 PRO TYR ASN ARG CYS LYS GLY SER ILE TYR LEU VAL PHE
SEQRES 9 A 373 ASP PHE CYS GLU HIS ASP LEU ALA GLY LEU LEU SER ASN
SEQRES 10 A 373 VAL LEU VAL LYS PHE THR LEU SER GLU ILE LYS ARG VAL
SEQRES 11 A 373 MET GLN MET LEU LEU ASN GLY LEU TYR TYR ILE HIS ARG
SEQRES 12 A 373 ASN LYS ILE LEU HIS ARG ASP MET LYS ALA ALA ASN VAL
SEQRES 13 A 373 LEU ILE THR ARG ASP GLY VAL LEU LYS LEU ALA ASP PHE
SEQRES 14 A 373 GLY LEU ALA ARG ALA PHE SER LEU ALA LYS ASN SER GLN
SEQRES 15 A 373 PRO ASN ARG TYR TPO ASN ARG VAL VAL THR LEU TRP TYR
SEQRES 16 A 373 ARG PRO PRO GLU LEU LEU LEU GLY GLU ARG ASP TYR GLY
SEQRES 17 A 373 PRO PRO ILE ASP LEU TRP GLY ALA GLY CYS ILE MET ALA
SEQRES 18 A 373 GLU MET TRP THR ARG SER PRO ILE MET GLN GLY ASN THR
SEQRES 19 A 373 GLU GLN HIS GLN LEU ALA LEU ILE SER GLN LEU CYS GLY
SEQRES 20 A 373 SER ILE THR PRO GLU VAL TRP PRO ASN VAL ASP ASN TYR
SEQRES 21 A 373 GLU LEU TYR GLU LYS LEU GLU LEU VAL LYS GLY GLN LYS
SEQRES 22 A 373 ARG LYS VAL LYS ASP ARG LEU LYS ALA TYR VAL ARG ASP
SEQRES 23 A 373 PRO TYR ALA LEU ASP LEU ILE ASP LYS LEU LEU VAL LEU
SEQRES 24 A 373 ASP PRO ALA GLN ARG ILE ASP SER ASP ASP ALA LEU ASN
SEQRES 25 A 373 HIS ASP PHE PHE TRP SER ASP PRO MET PRO SER ASP LEU
SEQRES 26 A 373 LYS GLY MET LEU SER THR HIS LEU THR SER MET PHE GLU
SEQRES 27 A 373 TYR LEU ALA PRO PRO ARG ARG LYS GLY SER GLN ILE THR
SEQRES 28 A 373 GLN GLN SER THR ASN GLN SER ARG ASN PRO ALA THR THR
SEQRES 29 A 373 ASN GLN THR GLU PHE GLU ARG VAL PHE
SEQRES 1 B 260 GLY PRO GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP
SEQRES 2 B 260 TYR PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG
SEQRES 3 B 260 ARG PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG
SEQRES 4 B 260 GLN GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG
SEQRES 5 B 260 LEU ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL
SEQRES 6 B 260 TYR MET HIS ARG PHE TYR MET ILE GLN SER PHE THR ARG
SEQRES 7 B 260 PHE PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU
SEQRES 8 B 260 ALA ALA LYS VAL GLU GLY GLN PRO LYS LYS LEU GLU HIS
SEQRES 9 B 260 VAL ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU
SEQRES 10 B 260 SER LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN
SEQRES 11 B 260 VAL GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN
SEQRES 12 B 260 THR LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR
SEQRES 13 B 260 HIS VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS
SEQRES 14 B 260 ASP LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER
SEQRES 15 B 260 LEU HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO
SEQRES 16 B 260 VAL VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP
SEQRES 17 B 260 SER ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS
SEQRES 18 B 260 TRP TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU
SEQRES 19 B 260 LEU ASP GLU LEU THR HIS GLU LEU LEU GLN ILE LEU GLU
SEQRES 20 B 260 LYS THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG
MODRES 4EC9 TPO A 186 THR PHOSPHOTHREONINE
HET TPO A 186 11
HETNAM TPO PHOSPHOTHREONINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
HELIX 1 1 PRO A 60 LEU A 73 1 14
HELIX 2 2 LEU A 110 ASN A 116 1 7
HELIX 3 3 THR A 122 ASN A 143 1 22
HELIX 4 4 LYS A 151 ALA A 153 5 3
HELIX 5 5 THR A 191 ARG A 195 5 5
HELIX 6 6 PRO A 196 LEU A 201 1 6
HELIX 7 7 PRO A 208 ARG A 225 1 18
HELIX 8 8 THR A 233 GLY A 246 1 14
HELIX 9 9 ASN A 255 TYR A 259 5 5
HELIX 10 10 LYS A 274 LYS A 280 1 7
HELIX 11 11 ASP A 285 LEU A 296 1 12
HELIX 12 12 ASP A 305 HIS A 312 1 8
HELIX 13 13 ASP A 313 TRP A 316 5 4
HELIX 14 14 THR B 15 ASN B 21 1 7
HELIX 15 15 SER B 24 GLY B 28 5 5
HELIX 16 16 ASP B 30 LEU B 52 1 23
HELIX 17 17 SER B 55 TYR B 70 1 16
HELIX 18 18 PRO B 79 GLU B 95 1 17
HELIX 19 19 LYS B 100 HIS B 113 1 14
HELIX 20 20 SER B 123 LEU B 144 1 22
HELIX 21 21 HIS B 152 LEU B 163 1 12
HELIX 22 22 SER B 167 THR B 185 1 19
HELIX 23 23 THR B 186 GLN B 190 5 5
HELIX 24 24 THR B 192 SER B 208 1 17
HELIX 25 25 HIS B 220 VAL B 225 5 6
HELIX 26 26 THR B 230 THR B 248 1 19
HELIX 27 27 ARG B 251 TRP B 256 5 6
SHEET 1 A 6 ASP A 14 GLU A 15 0
SHEET 2 A 6 LEU A 81 ARG A 86 1 O ARG A 86 N ASP A 14
SHEET 3 A 6 ILE A 99 ASP A 104 -1 O VAL A 102 N ILE A 82
SHEET 4 A 6 LYS A 44 LYS A 49 -1 N LYS A 48 O LEU A 101
SHEET 5 A 6 VAL A 33 HIS A 38 -1 N PHE A 34 O LEU A 47
SHEET 6 A 6 TYR A 19 LYS A 24 -1 N LEU A 22 O LYS A 35
SHEET 1 B 3 HIS A 108 ASP A 109 0
SHEET 2 B 3 VAL A 155 ILE A 157 -1 O ILE A 157 N HIS A 108
SHEET 3 B 3 LEU A 163 LEU A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 C 2 ILE A 145 LEU A 146 0
SHEET 2 C 2 ARG A 172 ALA A 173 -1 O ARG A 172 N LEU A 146
LINK C TYR A 185 N TPO A 186 1555 1555 1.33
LINK C TPO A 186 N ASN A 187 1555 1555 1.33
CRYST1 174.229 174.229 97.990 90.00 90.00 120.00 H 3 9
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 0.005740 0.003314 0.000000 0.00000
SCALE2 0.000000 0.006627 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
