HEADER TRANSFERASE 23-JAN-18 6FJZ
TITLE CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN ADENOSINE DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,
COMPND 5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,
COMPND 6 MAPK 2;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: MAPK1, ERK2, MAPK, PRKM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GELIN,G.LABESSE
REVDAT 1 06-FEB-19 6FJZ 0
JRNL AUTH M.GELIN,S.POCHET,G.LABESSE
JRNL TITL NONE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.120
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 31839
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2993
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 35.4864 - 5.1377 0.94 2688 138 0.1659 0.1664
REMARK 3 2 5.1377 - 4.0798 0.96 2685 169 0.1277 0.1442
REMARK 3 3 4.0798 - 3.5647 0.97 2754 144 0.1367 0.1667
REMARK 3 4 3.5647 - 3.2390 0.96 2725 126 0.1497 0.1989
REMARK 3 5 3.2390 - 3.0070 0.95 2732 132 0.1705 0.2314
REMARK 3 6 3.0070 - 2.8298 0.94 2683 134 0.1705 0.2118
REMARK 3 7 2.8298 - 2.6881 0.94 2622 168 0.1707 0.2320
REMARK 3 8 2.6881 - 2.5711 0.94 2668 156 0.1700 0.1759
REMARK 3 9 2.5711 - 2.4722 0.94 2695 152 0.1746 0.2236
REMARK 3 10 2.4722 - 2.3869 0.94 2677 146 0.1693 0.2234
REMARK 3 11 2.3869 - 2.3123 0.94 2636 160 0.1827 0.2666
REMARK 3 12 2.3123 - 2.2462 0.93 2681 146 0.1843 0.2360
REMARK 3 13 2.2462 - 2.1870 0.94 2673 133 0.1960 0.2297
REMARK 3 14 2.1870 - 2.1337 0.94 2621 189 0.1984 0.2416
REMARK 3 15 2.1337 - 2.0852 0.94 2662 156 0.1992 0.2627
REMARK 3 16 2.0852 - 2.0408 0.93 2616 123 0.2234 0.2376
REMARK 3 17 2.0408 - 2.0000 0.94 2733 118 0.2203 0.2490
REMARK 3 18 2.0000 - 1.9623 0.95 2663 115 0.2480 0.2990
REMARK 3 19 1.9623 - 1.9272 0.95 2706 162 0.2487 0.2921
REMARK 3 20 1.9272 - 1.8946 0.92 2671 105 0.2709 0.2821
REMARK 3 21 1.8946 - 1.8640 0.86 2429 121 0.2929 0.3127
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.20
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1399 15.3448 30.6350
REMARK 3 T TENSOR
REMARK 3 T11: 0.5250 T22: 0.3011
REMARK 3 T33: 0.3023 T12: -0.1099
REMARK 3 T13: -0.1500 T23: 0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 0.8923 L22: 0.6434
REMARK 3 L33: 2.6882 L12: 0.0316
REMARK 3 L13: 0.0687 L23: -0.4286
REMARK 3 S TENSOR
REMARK 3 S11: -0.3051 S12: 0.2072 S13: 0.3665
REMARK 3 S21: -0.3277 S22: 0.1295 S23: 0.1979
REMARK 3 S31: -0.7551 S32: -0.0776 S33: 0.0760
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 99 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1901 10.1447 49.0474
REMARK 3 T TENSOR
REMARK 3 T11: 0.1244 T22: 0.1440
REMARK 3 T33: 0.1934 T12: 0.0067
REMARK 3 T13: 0.0018 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 1.7116 L22: 1.9165
REMARK 3 L33: 1.7333 L12: 0.2747
REMARK 3 L13: 0.7530 L23: 0.3444
REMARK 3 S TENSOR
REMARK 3 S11: -0.1541 S12: -0.0038 S13: 0.2523
REMARK 3 S21: -0.0521 S22: 0.0410 S23: 0.3157
REMARK 3 S31: -0.2056 S32: -0.2134 S33: 0.0854
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3242 11.0814 57.5710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1384
REMARK 3 T33: 0.1437 T12: 0.0204
REMARK 3 T13: 0.0172 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 2.5476 L22: 2.0989
REMARK 3 L33: 1.3725 L12: 1.6147
REMARK 3 L13: 1.1535 L23: 0.6361
REMARK 3 S TENSOR
REMARK 3 S11: -0.0904 S12: 0.0456 S13: 0.0596
REMARK 3 S21: 0.0533 S22: 0.0679 S23: -0.0321
REMARK 3 S31: -0.0520 S32: 0.1215 S33: 0.0128
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1224 8.1111 26.5532
REMARK 3 T TENSOR
REMARK 3 T11: 0.5919 T22: 0.5422
REMARK 3 T33: 0.2650 T12: -0.1970
REMARK 3 T13: 0.0091 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.2184 L22: 1.9270
REMARK 3 L33: 2.5880 L12: -0.5253
REMARK 3 L13: 0.7938 L23: -1.5942
REMARK 3 S TENSOR
REMARK 3 S11: -0.1568 S12: 0.6389 S13: 0.0352
REMARK 3 S21: -0.6508 S22: 0.0058 S23: -0.1347
REMARK 3 S31: -0.0459 S32: 1.0196 S33: 0.0728
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 6FJZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008477.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93340
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.19
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.864
REMARK 200 RESOLUTION RANGE LOW (A) : 35.489
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : 0.03300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24300
REMARK 200 R SYM FOR SHELL (I) : 0.24300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 3QYZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, 0.1M MES PH 6.5, 0.1M
REMARK 280 AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, 0.002M MAGNESIUM
REMARK 280 SULFATE, VAPOR 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 35.48000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 355
REMARK 465 TYR A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 MET A 331 CG SD CE
REMARK 470 ASP A 335 CB CG OD1 OD2
REMARK 470 PRO A 354 C O
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 ARG A 13 50.21 35.57
REMARK 500 TYR A 34 33.84 -141.72
REMARK 500 ARG A 146 -0.68 75.90
REMARK 500 ASP A 147 41.02 -145.10
REMARK 500 ASP A 165 -86.27 82.46
REMARK 500 ASP A 173 67.68 -150.83
REMARK 500 ASN A 199 18.46 -162.55
REMARK 500 LEU A 292 50.02 -97.07
REMARK 500 ASP A 316 89.56 -159.27
REMARK 500 ASP A 335 72.86 -114.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DKW A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QYZ RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FI3 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FI6 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FJ0 RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
REMARK 900 RELATED ID: 6FJB RELATED DB: PDB
REMARK 900 CONTAINS THE SAME PROTEIN IN COMPLEX WITH ANOTHER ADENOSINE
REMARK 900 DERIVATIVE
DBREF 6FJZ A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 6FJZ HIS A -5 UNP P63086 EXPRESSION TAG
SEQADV 6FJZ HIS A -4 UNP P63086 EXPRESSION TAG
SEQADV 6FJZ HIS A -3 UNP P63086 EXPRESSION TAG
SEQADV 6FJZ HIS A -2 UNP P63086 EXPRESSION TAG
SEQADV 6FJZ HIS A -1 UNP P63086 EXPRESSION TAG
SEQADV 6FJZ HIS A 0 UNP P63086 EXPRESSION TAG
SEQRES 1 A 364 HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA ALA
SEQRES 2 A 364 GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY
SEQRES 3 A 364 PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA
SEQRES 4 A 364 TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS
SEQRES 5 A 364 VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS
SEQRES 6 A 364 GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE
SEQRES 7 A 364 LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN
SEQRES 8 A 364 ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP
SEQRES 9 A 364 VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR
SEQRES 10 A 364 LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE
SEQRES 11 A 364 CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR
SEQRES 12 A 364 ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 13 A 364 SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE
SEQRES 14 A 364 CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS
SEQRES 15 A 364 ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG
SEQRES 16 A 364 TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY
SEQRES 17 A 364 TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE
SEQRES 18 A 364 LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY
SEQRES 19 A 364 LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE
SEQRES 20 A 364 LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE
SEQRES 21 A 364 ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS
SEQRES 22 A 364 LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA
SEQRES 23 A 364 ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR
SEQRES 24 A 364 PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU
SEQRES 25 A 364 ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP
SEQRES 26 A 364 GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU
SEQRES 27 A 364 LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE
SEQRES 28 A 364 PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER
MODRES 6FJZ CME A 159 CYS MODIFIED RESIDUE
HET CME A 159 10
HET SO4 A 401 5
HET DKW A 402 23
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
HETNAM DKW (2~{S},3~{S},4~{R},5~{R})-5-(6-AMINOPURIN-9-YL)-3,4-
HETNAM 2 DKW BIS(OXIDANYL)-~{N}-PROP-2-YNYL-OXOLANE-2-CARBOXAMIDE
HETSYN DKW 6-CARBOXYMETHYLURACIL
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 SO4 O4 S 2-
FORMUL 3 DKW C13 H14 N6 O4
FORMUL 4 HOH *330(H2 O)
HELIX 1 AA1 HIS A 59 PHE A 76 1 18
HELIX 2 AA2 LEU A 110 GLN A 117 1 8
HELIX 3 AA3 SER A 120 ALA A 141 1 22
HELIX 4 AA4 LYS A 149 SER A 151 5 3
HELIX 5 AA5 ASP A 173 ASP A 177 5 5
HELIX 6 AA6 THR A 188 ARG A 192 5 5
HELIX 7 AA7 ALA A 193 ASN A 199 1 7
HELIX 8 AA8 LYS A 205 ASN A 222 1 18
HELIX 9 AA9 HIS A 230 GLY A 243 1 14
HELIX 10 AB1 SER A 246 CYS A 252 1 7
HELIX 11 AB2 ASN A 255 SER A 264 1 10
HELIX 12 AB3 PRO A 272 PHE A 277 1 6
HELIX 13 AB4 ASP A 281 LEU A 292 1 12
HELIX 14 AB5 GLU A 301 ALA A 307 1 7
HELIX 15 AB6 HIS A 308 GLU A 312 5 5
HELIX 16 AB7 ASP A 316 GLU A 320 5 5
HELIX 17 AB8 PRO A 337 THR A 349 1 13
HELIX 18 AB9 ALA A 350 GLN A 353 5 4
SHEET 1 AA1 2 GLU A 10 VAL A 12 0
SHEET 2 AA1 2 GLN A 15 PHE A 17 -1 O GLN A 15 N VAL A 12
SHEET 1 AA2 5 TYR A 23 GLY A 32 0
SHEET 2 AA2 5 GLY A 35 ASP A 42 -1 O TYR A 41 N THR A 24
SHEET 3 AA2 5 VAL A 47 ILE A 54 -1 O LYS A 53 N MET A 36
SHEET 4 AA2 5 VAL A 99 ASP A 104 -1 O VAL A 99 N ILE A 54
SHEET 5 AA2 5 ASP A 86 ILE A 88 -1 N ILE A 88 O TYR A 100
SHEET 1 AA3 3 THR A 108 ASP A 109 0
SHEET 2 AA3 3 LEU A 153 LEU A 155 -1 O LEU A 155 N THR A 108
SHEET 3 AA3 3 LEU A 161 ILE A 163 -1 O LYS A 162 N LEU A 154
SHEET 1 AA4 2 VAL A 143 LEU A 144 0
SHEET 2 AA4 2 ARG A 170 VAL A 171 -1 O ARG A 170 N LEU A 144
LINK C THR A 158 N CME A 159 1555 1555 1.33
LINK C CME A 159 N ASP A 160 1555 1555 1.33
CISPEP 1 GLY A 20 PRO A 21 0 -0.43
CISPEP 2 GLN A 353 PRO A 354 0 -7.69
SITE 1 AC1 6 TYR A 185 ARG A 189 ARG A 192 TYR A 231
SITE 2 AC1 6 HOH A 542 HOH A 558
SITE 1 AC2 13 ILE A 29 GLY A 32 VAL A 37 ALA A 50
SITE 2 AC2 13 GLN A 103 ASP A 104 MET A 106 ASP A 109
SITE 3 AC2 13 LYS A 112 HOH A 545 HOH A 556 HOH A 636
SITE 4 AC2 13 HOH A 678
CRYST1 48.870 70.960 59.280 90.00 108.97 90.00 P 1 21 1 2
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 0.020462 0.000000 0.007034 0.00000
SCALE2 0.000000 0.014092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017838 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
