HEADER TRANSFERASE 16-JAN-15 4XOZ
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 4XOZ 1 REMARK SITE ATOM
REVDAT 2 19-AUG-15 4XOZ 1 JRNL
REVDAT 1 12-AUG-15 4XOZ 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. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.260
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 27176
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2515
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 28.9521 - 5.1017 0.85 2566 122 0.1350 0.1538
REMARK 3 2 5.1017 - 4.0530 0.87 2625 158 0.1141 0.1587
REMARK 3 3 4.0530 - 3.5417 0.89 2708 126 0.1158 0.1763
REMARK 3 4 3.5417 - 3.2183 0.89 2666 133 0.1402 0.1832
REMARK 3 5 3.2183 - 2.9879 0.89 2725 139 0.1434 0.1706
REMARK 3 6 2.9879 - 2.8119 0.90 2702 142 0.1555 0.2005
REMARK 3 7 2.8119 - 2.6712 0.90 2726 151 0.1522 0.2224
REMARK 3 8 2.6712 - 2.5550 0.91 2709 173 0.1569 0.1934
REMARK 3 9 2.5550 - 2.4567 0.90 2725 162 0.1565 0.2081
REMARK 3 10 2.4567 - 2.3719 0.90 2743 148 0.1664 0.2362
REMARK 3 11 2.3719 - 2.2978 0.91 2726 161 0.1646 0.2189
REMARK 3 12 2.2978 - 2.2321 0.92 2731 149 0.1677 0.1940
REMARK 3 13 2.2321 - 2.1734 0.91 2728 178 0.1637 0.2064
REMARK 3 14 2.1734 - 2.1204 0.91 2723 176 0.1721 0.1970
REMARK 3 15 2.1204 - 2.0722 0.88 2680 136 0.1803 0.2164
REMARK 3 16 2.0722 - 2.0281 0.79 2403 94 0.1937 0.2428
REMARK 3 17 2.0281 - 1.9875 0.66 2023 87 0.2265 0.2810
REMARK 3 18 1.9875 - 1.9500 0.58 1754 80 0.2414 0.2682
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.44
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 : 0.012 2927
REMARK 3 ANGLE : 1.424 3967
REMARK 3 CHIRALITY : 0.062 438
REMARK 3 PLANARITY : 0.007 504
REMARK 3 DIHEDRAL : 14.354 1114
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 9:118)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5128 12.7231 34.5441
REMARK 3 T TENSOR
REMARK 3 T11: 0.3268 T22: 0.3337
REMARK 3 T33: 0.2574 T12: 0.0110
REMARK 3 T13: -0.0354 T23: 0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 0.5619 L22: 0.0615
REMARK 3 L33: 3.1190 L12: 0.0274
REMARK 3 L13: -0.9726 L23: -0.0767
REMARK 3 S TENSOR
REMARK 3 S11: 0.0265 S12: 0.2616 S13: 0.2481
REMARK 3 S21: -0.1210 S22: 0.0708 S23: 0.0783
REMARK 3 S31: -0.4224 S32: -0.4985 S33: -0.0920
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 119:312)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6291 7.9980 58.3074
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.0976
REMARK 3 T33: 0.1510 T12: 0.0162
REMARK 3 T13: 0.0192 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.1773 L22: 0.7683
REMARK 3 L33: 1.3591 L12: 0.9797
REMARK 3 L13: 1.0372 L23: 0.2412
REMARK 3 S TENSOR
REMARK 3 S11: -0.0134 S12: 0.0572 S13: 0.1375
REMARK 3 S21: -0.0017 S22: 0.0134 S23: -0.0365
REMARK 3 S31: -0.0826 S32: 0.0917 S33: -0.0032
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 313:354)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4147 0.2926 35.1931
REMARK 3 T TENSOR
REMARK 3 T11: 0.2589 T22: 0.2757
REMARK 3 T33: 0.2503 T12: -0.0135
REMARK 3 T13: 0.0123 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.7780 L22: 1.5051
REMARK 3 L33: 3.2735 L12: -0.1020
REMARK 3 L13: -0.0238 L23: -1.8052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0049 S12: 0.2078 S13: -0.0269
REMARK 3 S21: -0.2692 S22: -0.2581 S23: -0.1036
REMARK 3 S31: 0.3056 S32: 0.4419 S33: 0.1347
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN S
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2080 6.1452 51.6357
REMARK 3 T TENSOR
REMARK 3 T11: 0.2351 T22: 0.2102
REMARK 3 T33: 0.2395 T12: -0.0072
REMARK 3 T13: 0.0038 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.9122 L22: 0.5225
REMARK 3 L33: 0.8725 L12: 0.0893
REMARK 3 L13: -0.1217 L23: 0.0580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0303 S12: -0.0410 S13: 0.0135
REMARK 3 S21: -0.0450 S22: 0.0308 S23: -0.0205
REMARK 3 S31: 0.0595 S32: 0.0080 S33: -0.0027
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5385 11.9959 38.5255
REMARK 3 T TENSOR
REMARK 3 T11: 0.6844 T22: 0.3098
REMARK 3 T33: 0.2629 T12: -0.0488
REMARK 3 T13: 0.1057 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.0165 L22: 3.5175
REMARK 3 L33: 1.5307 L12: 0.4765
REMARK 3 L13: 0.9809 L23: -0.9299
REMARK 3 S TENSOR
REMARK 3 S11: 0.4275 S12: 0.0766 S13: 0.2365
REMARK 3 S21: 0.0707 S22: 0.2537 S23: 0.0026
REMARK 3 S31: -0.1958 S32: 0.0726 S33: -0.6088
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 4XOZ 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_1000206000.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-10
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 : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27177
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 29.025
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.02300
REMARK 200 R SYM (I) : 0.02300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.20900
REMARK 200 R SYM FOR SHELL (I) : 0.20900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 3QYW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG MME 2000, 0.1M MES PH 6.5,
REMARK 280 0.1M AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, 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 35.77500
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: 180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16720 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 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 ARG A 77 CZ NH1 NH2
REMARK 470 LYS A 115 CE NZ
REMARK 470 ARG A 223 CZ NH1 NH2
REMARK 470 LYS A 229 CE NZ
REMARK 470 GLU A 324 CD OE1 OE2
REMARK 470 ASP A 335 CG OD1 OD2
REMARK 470 GLU A 347 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 ARG A 146 -1.02 72.29
REMARK 500 ASP A 147 40.83 -142.32
REMARK 500 ASP A 165 75.89 64.03
REMARK 500 ASN A 199 15.04 -160.75
REMARK 500 LEU A 292 56.76 -94.00
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 620 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
DBREF 4XOZ 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 CYS 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 CYS 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 CYS 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 4XOZ CME A 159 CYS MODIFIED RESIDUE
HET CME A 159 10
HET 620 A 401 22
HET SO4 A 402 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM 620 N~1~-[3-(BENZYLOXY)BENZYL]-1H-TETRAZOLE-1,5-DIAMINE
HETNAM SO4 SULFATE ION
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 620 C15 H16 N6 O
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *141(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 ASN A 251 1 6
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 GLY A 30 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 ILE A 51 N CYS A 38
SHEET 4 AA2 5 VAL A 99 ASP A 104 -1 O GLN A 103 N ALA A 50
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 3.35
CISPEP 2 GLN A 353 PRO A 354 0 -1.17
SITE 1 AC1 9 LYS A 52 ILE A 54 GLU A 69 ILE A 101
SITE 2 AC1 9 GLN A 103 ASP A 104 MET A 106 HOH A 625
SITE 3 AC1 9 HOH A 568
SITE 1 AC2 3 ARG A 189 ARG A 192 TYR A 231
CRYST1 49.170 71.550 60.890 90.00 108.60 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 0.020338 0.000000 0.006844 0.00000
SCALE2 0.000000 0.013976 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017328 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
