HEADER TRANSFERASE 16-JAN-15 4XP0
TITLE CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN INHIBITOR
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: NORWAY 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,F.ALLEMAND,G.LABESSE,J.F.GUICHOU
REVDAT 3 06-SEP-17 4XP0 1 REMARK SITE ATOM
REVDAT 2 19-AUG-15 4XP0 1 JRNL
REVDAT 1 12-AUG-15 4XP0 0
JRNL AUTH M.GELIN,V.DELFOSSE,F.ALLEMAND,F.HOH,Y.SALLAZ-DAMAZ,
JRNL AUTH 2 M.PIROCCHI,W.BOURGUET,J.L.FERRER,G.LABESSE,J.F.GUICHOU
JRNL TITL COMBINING `DRY' CO-CRYSTALLIZATION AND IN SITU DIFFRACTION
JRNL TITL 2 TO FACILITATE LIGAND SCREENING BY X-RAY CRYSTALLOGRAPHY.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 1777 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 26249358
JRNL DOI 10.1107/S1399004715010342
REMARK 2
REMARK 2 RESOLUTION. 1.46 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.310
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.3
REMARK 3 NUMBER OF REFLECTIONS : 64302
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 5500
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 28.6365 - 4.5309 0.93 3944 197 0.1938 0.2182
REMARK 3 2 4.5309 - 3.5985 0.92 3860 225 0.1459 0.1547
REMARK 3 3 3.5985 - 3.1443 0.90 3829 176 0.1665 0.2157
REMARK 3 4 3.1443 - 2.8571 0.89 3728 195 0.1681 0.1832
REMARK 3 5 2.8571 - 2.6525 0.89 3746 213 0.1764 0.2051
REMARK 3 6 2.6525 - 2.4962 0.88 3679 232 0.1716 0.1881
REMARK 3 7 2.4962 - 2.3712 0.87 3626 213 0.1764 0.2296
REMARK 3 8 2.3712 - 2.2681 0.86 3630 193 0.1812 0.2185
REMARK 3 9 2.2681 - 2.1808 0.85 3553 216 0.1816 0.1796
REMARK 3 10 2.1808 - 2.1055 0.86 3576 216 0.1697 0.1911
REMARK 3 11 2.1055 - 2.0397 0.85 3547 175 0.1725 0.1964
REMARK 3 12 2.0397 - 1.9814 0.84 3613 146 0.1827 0.1998
REMARK 3 13 1.9814 - 1.9293 0.84 3525 199 0.1867 0.2382
REMARK 3 14 1.9293 - 1.8822 0.83 3519 153 0.1982 0.2398
REMARK 3 15 1.8822 - 1.8394 0.83 3521 162 0.1992 0.2159
REMARK 3 16 1.8394 - 1.8003 0.83 3533 175 0.1992 0.2297
REMARK 3 17 1.8003 - 1.7643 0.83 3498 156 0.2103 0.2157
REMARK 3 18 1.7643 - 1.7310 0.82 3452 187 0.2186 0.2456
REMARK 3 19 1.7310 - 1.7001 0.82 3433 189 0.2308 0.2400
REMARK 3 20 1.7001 - 1.6713 0.81 3448 153 0.2449 0.2838
REMARK 3 21 1.6713 - 1.6443 0.81 3382 193 0.2614 0.2955
REMARK 3 22 1.6443 - 1.6190 0.80 3387 185 0.2818 0.3377
REMARK 3 23 1.6190 - 1.5952 0.79 3340 183 0.2976 0.3243
REMARK 3 24 1.5952 - 1.5728 0.80 3339 221 0.3125 0.3452
REMARK 3 25 1.5728 - 1.5515 0.79 3355 168 0.3241 0.3563
REMARK 3 26 1.5515 - 1.5314 0.79 3294 171 0.3409 0.3743
REMARK 3 27 1.5314 - 1.5122 0.78 3349 156 0.3613 0.3561
REMARK 3 28 1.5122 - 1.4940 0.76 3179 159 0.3846 0.4450
REMARK 3 29 1.4940 - 1.4766 0.64 2702 156 0.3958 0.4194
REMARK 3 30 1.4766 - 1.4600 0.58 2441 137 0.3937 0.3950
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 : 0.35
REMARK 3 B_SOL : 64.31
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43090
REMARK 3 B22 (A**2) : 0.80240
REMARK 3 B33 (A**2) : -0.37150
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.26970
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 : 0.014 2989
REMARK 3 ANGLE : 1.100 4051
REMARK 3 CHIRALITY : 0.076 454
REMARK 3 PLANARITY : 0.006 508
REMARK 3 DIHEDRAL : 13.453 1174
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3706 5.6043 48.3292
REMARK 3 T TENSOR
REMARK 3 T11: 0.0659 T22: 0.0964
REMARK 3 T33: 0.1017 T12: -0.0035
REMARK 3 T13: 0.0108 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 0.5986 L22: 0.3794
REMARK 3 L33: 0.8474 L12: 0.2456
REMARK 3 L13: 0.2897 L23: 0.2926
REMARK 3 S TENSOR
REMARK 3 S11: -0.0507 S12: 0.0735 S13: 0.0827
REMARK 3 S21: -0.0643 S22: 0.0478 S23: -0.0111
REMARK 3 S31: -0.0770 S32: 0.0477 S33: -0.0007
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 4XP0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206003.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-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 : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.872600
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.19
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64331
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 28.631
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : 0.03100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : 0.48000
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: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
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, VAPOR DIFFUSION,
REMARK 280 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 35.39500
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 LYS A 328
REMARK 465 PHE A 329
REMARK 465 ASP A 330
REMARK 465 MET A 331
REMARK 465 GLU A 332
REMARK 465 LEU A 333
REMARK 465 ASP A 334
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 TYR A 34 CZ OH
REMARK 470 GLU A 184 OE1 OE2
REMARK 470 ASP A 335 CB CG OD1 OD2
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 147 41.37 -147.80
REMARK 500 ASP A 165 87.23 63.35
REMARK 500 ASN A 199 18.72 -160.46
REMARK 500 LEU A 292 46.35 -98.62
REMARK 500 ASP A 316 97.13 -160.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 852 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A 853 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH A 854 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 855 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH A 856 DISTANCE = 7.54 ANGSTROMS
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 DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 42A A 404
DBREF 4XP0 A 8 358 UNP P63086 MK01_RAT 8 358
SEQRES 1 A 351 GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY
SEQRES 2 A 351 PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA
SEQRES 3 A 351 TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS
SEQRES 4 A 351 VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS
SEQRES 5 A 351 GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE
SEQRES 6 A 351 LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN
SEQRES 7 A 351 ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP
SEQRES 8 A 351 VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR
SEQRES 9 A 351 LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE
SEQRES 10 A 351 CME TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR
SEQRES 11 A 351 ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 12 A 351 SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE
SEQRES 13 A 351 CME ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS
SEQRES 14 A 351 ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG
SEQRES 15 A 351 TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY
SEQRES 16 A 351 TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE
SEQRES 17 A 351 LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY
SEQRES 18 A 351 LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE
SEQRES 19 A 351 LEU GLY SER PRO SER GLN GLU ASP LEU ASN CME ILE ILE
SEQRES 20 A 351 ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS
SEQRES 21 A 351 LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA
SEQRES 22 A 351 ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR
SEQRES 23 A 351 PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU
SEQRES 24 A 351 ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP
SEQRES 25 A 351 GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU
SEQRES 26 A 351 LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE
SEQRES 27 A 351 PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER
MODRES 4XP0 CME A 125 CYS MODIFIED RESIDUE
MODRES 4XP0 CME A 159 CYS MODIFIED RESIDUE
MODRES 4XP0 CME A 164 CYS MODIFIED RESIDUE
MODRES 4XP0 CME A 252 CYS MODIFIED RESIDUE
HET CME A 125 10
HET CME A 159 10
HET CME A 164 10
HET CME A 252 10
HET SO4 A 401 5
HET DMS A 402 4
HET DMS A 403 4
HET 42A A 404 11
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM 42A 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBONITRILE
FORMUL 1 CME 4(C5 H11 N O3 S2)
FORMUL 2 SO4 O4 S 2-
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 42A C8 H5 N3
FORMUL 6 HOH *356(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 MET A 197 5 5
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 CME A 252 1 7
HELIX 11 AB2 ASN A 255 LEU A 265 1 11
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 ALA A 350 1 14
HELIX 18 AB9 ARG A 351 GLN A 353 5 3
SHEET 1 AA1 2 MET A 11 VAL A 12 0
SHEET 2 AA1 2 GLN A 15 VAL A 16 -1 O GLN A 15 N VAL A 12
SHEET 1 AA2 5 TYR A 23 GLU A 31 0
SHEET 2 AA2 5 MET A 36 ASP A 42 -1 O TYR A 41 N THR A 24
SHEET 3 AA2 5 VAL A 47 ILE A 54 -1 O ILE A 51 N CYS A 38
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 ASP A 86 O VAL A 102
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 ILE A 124 N CME A 125 1555 1555 1.33
LINK C CME A 125 N TYR A 126 1555 1555 1.33
LINK C THR A 158 N CME A 159 1555 1555 1.32
LINK C CME A 159 N ASP A 160 1555 1555 1.33
LINK C ILE A 163 N CME A 164 1555 1555 1.32
LINK C CME A 164 N ASP A 165 1555 1555 1.33
LINK C ASN A 251 N CME A 252 1555 1555 1.33
LINK C CME A 252 N ILE A 253 1555 1555 1.33
CISPEP 1 GLY A 20 PRO A 21 0 -0.48
CISPEP 2 GLN A 353 PRO A 354 0 1.04
SITE 1 AC1 5 ARG A 189 ARG A 192 TYR A 231 HOH A 633
SITE 2 AC1 5 HOH A 671
SITE 1 AC2 3 HIS A 123 ILE A 254 ARG A 259
SITE 1 AC3 5 GLU A 312 GLN A 313 TYR A 314 TYR A 315
SITE 2 AC3 5 HOH A 513
SITE 1 AC4 6 ALA A 50 GLN A 103 ASP A 104 MET A 106
SITE 2 AC4 6 HOH A 709 HOH A 617
CRYST1 48.910 70.790 60.410 90.00 108.99 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 0.020446 0.000000 0.007036 0.00000
SCALE2 0.000000 0.014126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017506 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
