HEADER TRANSFERASE 26-JAN-15 4S30
TITLE ERK2 INTRINSICALLY ACTIVE MUTANT (I84A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED
COMPND 5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED
COMPND 6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
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 SIGNAL TRANSDUCTION, PHOSPHORYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.LIVNAH,Y.KARAMANSHA
REVDAT 2 20-SEP-23 4S30 1 SEQADV
REVDAT 1 27-JAN-16 4S30 0
JRNL AUTH O.LIVNAH,Y.KARAMANSHA
JRNL TITL MULTIPLE MECHANISMS RENDER ERK PROTEINS MEK-INDEPENDENT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 24449
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1306
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1801
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 102
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.17000
REMARK 3 B22 (A**2) : -0.25000
REMARK 3 B33 (A**2) : 0.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.09000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.688
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2838 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2742 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3842 ; 1.803 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6312 ; 0.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 338 ; 7.070 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;38.777 ;24.118
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 504 ;19.077 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;22.567 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 424 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3159 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 652 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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
REMARK 4
REMARK 4 4S30 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000088115.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.93
REMARK 200 MONOCHROMATOR : OPTICAL HUTCH
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: AMORE
REMARK 200 STARTING MODEL: 1ERK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 61 MM AMMONIUM SULFATE, 100MM BIS TRIS
REMARK 280 PH 7.0, 12-15% (V/V) PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 34.77100
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 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 9
REMARK 465 GLU A 10
REMARK 465 MET A 11
REMARK 465 VAL A 12
REMARK 465 ARG A 13
REMARK 465 GLY A 14
REMARK 465 TYR A 34
REMARK 465 LEU A 333
REMARK 465 ASP A 334
REMARK 465 ASP A 335
REMARK 465 TYR A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
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 ALA A 33 N GLY A 35 1.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
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 ALA A 5 113.06 178.94
REMARK 500 PHE A 17 77.93 -155.18
REMARK 500 ILE A 29 34.43 -155.73
REMARK 500 GLU A 31 79.54 47.52
REMARK 500 LYS A 46 17.25 56.95
REMARK 500 GLU A 58 -76.52 -76.64
REMARK 500 ARG A 146 -0.94 71.10
REMARK 500 ASP A 165 77.97 69.38
REMARK 500 ASN A 199 15.46 -159.86
REMARK 500 ASN A 255 106.12 -31.02
REMARK 500 LEU A 292 49.89 -98.18
REMARK 500 ASP A 316 98.63 -162.07
REMARK 500 PHE A 329 79.39 55.67
REMARK 500 ASP A 330 -152.92 -61.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 29 GLY A 30 -142.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ERK RELATED DB: PDB
REMARK 900 RELATED ID: 4S2Z RELATED DB: PDB
REMARK 900 RELATED ID: 4S31 RELATED DB: PDB
REMARK 900 RELATED ID: 4S32 RELATED DB: PDB
REMARK 900 RELATED ID: 4S33 RELATED DB: PDB
REMARK 900 RELATED ID: 4S34 RELATED DB: PDB
DBREF 4S30 A 1 358 UNP P63086 MK01_RAT 1 358
SEQADV 4S30 ALA A 84 UNP P63086 ILE 84 ENGINEERED MUTATION
SEQRES 1 A 358 MET ALA ALA ALA ALA ALA ALA GLY PRO GLU MET VAL ARG
SEQRES 2 A 358 GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR THR ASN LEU
SEQRES 3 A 358 SER TYR ILE GLY GLU GLY ALA TYR GLY MET VAL CYS SER
SEQRES 4 A 358 ALA TYR ASP ASN LEU ASN LYS VAL ARG VAL ALA ILE LYS
SEQRES 5 A 358 LYS ILE SER PRO PHE GLU HIS GLN THR TYR CYS GLN ARG
SEQRES 6 A 358 THR LEU ARG GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS
SEQRES 7 A 358 GLU ASN ILE ILE GLY ALA ASN ASP ILE ILE ARG ALA PRO
SEQRES 8 A 358 THR ILE GLU GLN MET LYS ASP VAL TYR ILE VAL GLN ASP
SEQRES 9 A 358 LEU MET GLU THR ASP LEU TYR LYS LEU LEU LYS THR GLN
SEQRES 10 A 358 HIS LEU SER ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN
SEQRES 11 A 358 ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA ASN VAL
SEQRES 12 A 358 LEU HIS ARG ASP LEU LYS PRO SER ASN LEU LEU LEU ASN
SEQRES 13 A 358 THR THR CYS ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA
SEQRES 14 A 358 ARG VAL ALA ASP PRO ASP HIS ASP HIS THR GLY PHE LEU
SEQRES 15 A 358 THR GLU TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU
SEQRES 16 A 358 ILE MET LEU ASN SER LYS GLY TYR THR LYS SER ILE ASP
SEQRES 17 A 358 ILE TRP SER VAL GLY CYS ILE LEU ALA GLU MET LEU SER
SEQRES 18 A 358 ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN
SEQRES 19 A 358 LEU ASN HIS ILE LEU GLY ILE LEU GLY SER PRO SER GLN
SEQRES 20 A 358 GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN
SEQRES 21 A 358 TYR LEU LEU SER LEU PRO HIS LYS ASN LYS VAL PRO TRP
SEQRES 22 A 358 ASN ARG LEU PHE PRO ASN ALA ASP SER LYS ALA LEU ASP
SEQRES 23 A 358 LEU LEU ASP LYS MET LEU THR PHE ASN PRO HIS LYS ARG
SEQRES 24 A 358 ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU
SEQRES 25 A 358 GLN TYR TYR ASP PRO SER ASP GLU PRO ILE ALA GLU ALA
SEQRES 26 A 358 PRO PHE LYS PHE ASP MET GLU LEU ASP ASP LEU PRO LYS
SEQRES 27 A 358 GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU THR ALA ARG
SEQRES 28 A 358 PHE GLN PRO GLY TYR ARG SER
FORMUL 2 HOH *82(H2 O)
HELIX 1 1 HIS A 59 PHE A 76 1 18
HELIX 2 2 LEU A 110 GLN A 117 1 8
HELIX 3 3 SER A 120 ALA A 141 1 22
HELIX 4 4 LYS A 149 SER A 151 5 3
HELIX 5 5 ASP A 173 ASP A 177 5 5
HELIX 6 6 THR A 188 ARG A 192 5 5
HELIX 7 7 ALA A 193 MET A 197 5 5
HELIX 8 8 LYS A 205 ASN A 222 1 18
HELIX 9 9 HIS A 230 GLY A 243 1 14
HELIX 10 10 SER A 246 CYS A 252 1 7
HELIX 11 11 ASN A 255 LEU A 265 1 11
HELIX 12 12 PRO A 272 PHE A 277 1 6
HELIX 13 13 ASP A 281 LEU A 292 1 12
HELIX 14 14 GLU A 301 ALA A 307 1 7
HELIX 15 15 HIS A 308 GLU A 312 5 5
HELIX 16 16 ASP A 316 GLU A 320 5 5
HELIX 17 17 PRO A 337 ALA A 350 1 14
HELIX 18 18 ARG A 351 GLN A 353 5 3
SHEET 1 A 5 TYR A 23 TYR A 28 0
SHEET 2 A 5 VAL A 37 ASP A 42 -1 O TYR A 41 N THR A 24
SHEET 3 A 5 ARG A 48 ILE A 54 -1 O ILE A 51 N CYS A 38
SHEET 4 A 5 VAL A 99 ASP A 104 -1 O GLN A 103 N ALA A 50
SHEET 5 A 5 ASP A 86 ILE A 88 -1 N ILE A 88 O TYR A 100
SHEET 1 B 3 THR A 108 ASP A 109 0
SHEET 2 B 3 LEU A 153 LEU A 155 -1 O LEU A 155 N THR A 108
SHEET 3 B 3 LEU A 161 ILE A 163 -1 O LYS A 162 N LEU A 154
SHEET 1 C 2 VAL A 143 LEU A 144 0
SHEET 2 C 2 ARG A 170 VAL A 171 -1 O ARG A 170 N LEU A 144
CRYST1 49.017 69.542 59.798 90.00 109.06 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 0.020401 0.000000 0.007049 0.00000
SCALE2 0.000000 0.014380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017693 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
