HEADER APOPTOSIS 21-JAN-15 4XRJ
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 KINASE INHIBITOR, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GELIN,F.ALLEMAND,G.LABESSE,J.F.GUICHOU
REVDAT 2 19-AUG-15 4XRJ 1 JRNL
REVDAT 1 12-AUG-15 4XRJ 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. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 39592
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2088
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2846
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 138
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2839
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : 0.31000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.42000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.565
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3104 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3025 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4244 ; 1.456 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7001 ; 0.898 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 393 ; 5.603 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;40.569 ;24.342
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 570 ;16.921 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;25.525 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 469 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3499 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 721 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1435 ; 3.355 ; 2.373
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1434 ; 3.330 ; 2.370
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1805 ; 4.075 ; 3.571
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 6129 ; 3.618 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 53 ;26.337 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6140 ;11.449 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4XRJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206009.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 298
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 : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39592
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 44.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.6000
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: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100MM PH 6.5, (NH4)2SO4 200MM,
REMARK 280 BETA-MERCAPTOETHANOL 20MM AND 26% (W/V) PEG MME2000, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 35.74000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16890 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR A 34 OH TYR A 62 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 GLN A 247 O HOH A 516 1656 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 -130.57 52.03
REMARK 500 ARG A 146 -5.74 80.19
REMARK 500 ASP A 147 40.42 -141.95
REMARK 500 ASP A 165 78.35 62.78
REMARK 500 ASP A 165 76.72 65.09
REMARK 500 ASP A 173 73.46 -151.29
REMARK 500 ASN A 199 13.73 -157.20
REMARK 500 TYR A 231 -74.83 -47.01
REMARK 500 LEU A 292 58.27 -95.12
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 650 DISTANCE = 6.06 ANGSTROMS
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 4XRJ A 9 354 UNP P63086 MK01_RAT 9 354
SEQRES 1 A 346 PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO
SEQRES 2 A 346 ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA TYR
SEQRES 3 A 346 GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS VAL
SEQRES 4 A 346 ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS GLN
SEQRES 5 A 346 THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE LEU
SEQRES 6 A 346 LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP
SEQRES 7 A 346 ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP VAL
SEQRES 8 A 346 TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR LYS
SEQRES 9 A 346 LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE CYS
SEQRES 10 A 346 TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE
SEQRES 11 A 346 HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO SER
SEQRES 12 A 346 ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE CYS
SEQRES 13 A 346 ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP
SEQRES 14 A 346 HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG TRP
SEQRES 15 A 346 TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY TYR
SEQRES 16 A 346 THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE LEU
SEQRES 17 A 346 ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY LYS
SEQRES 18 A 346 HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU
SEQRES 19 A 346 GLY SER PRO SER GLN GLU ASP LEU ASN CME ILE ILE ASN
SEQRES 20 A 346 LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS LYS
SEQRES 21 A 346 ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP
SEQRES 22 A 346 SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR PHE
SEQRES 23 A 346 ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA
SEQRES 24 A 346 HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP GLU
SEQRES 25 A 346 PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU LEU
SEQRES 26 A 346 ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE
SEQRES 27 A 346 GLU GLU THR ALA ARG PHE GLN PRO
MODRES 4XRJ CME A 159 CYS MODIFIED RESIDUE
MODRES 4XRJ CME A 252 CYS MODIFIED RESIDUE
HET CME A 159 10
HET CME A 252 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 2(C5 H11 N O3 S2)
FORMUL 2 620 C15 H16 N6 O
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *161(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 ALA A 193 5 6
HELIX 7 AA7 PRO A 194 ASN A 199 1 6
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 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 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 32 0
SHEET 2 AA2 5 GLY A 35 ASP A 42 -1 O VAL A 37 N GLY A 30
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 THR A 158 N CME A 159 1555 1555 1.33
LINK C CME A 159 N ASP A 160 1555 1555 1.33
LINK C ASN A 251 N CME A 252 1555 1555 1.34
LINK C CME A 252 N ILE A 253 1555 1555 1.33
CISPEP 1 GLY A 20 PRO A 21 0 0.49
SITE 1 AC1 10 ALA A 50 LYS A 52 ILE A 54 GLU A 69
SITE 2 AC1 10 ILE A 101 GLN A 103 ASP A 104 MET A 106
SITE 3 AC1 10 HOH A 556 HOH A 624
SITE 1 AC2 2 ARG A 189 ARG A 192
CRYST1 49.155 71.480 60.760 90.00 108.70 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 0.020344 0.000000 0.006886 0.00000
SCALE2 0.000000 0.013990 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017375 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
