HEADER TRANSFERASE/INHIBITOR 15-MAR-17 5V62
TITLE PHOSPHO-ERK2 BOUND TO BIVALENT INHIBITOR SBP3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 10-360;
COMPND 5 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,
COMPND 6 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,
COMPND 7 MAPK 2;
COMPND 8 EC: 2.7.11.24;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: DUAL PHOSPHORYLATED ERK2;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: RIBOSOMAL PROTEIN S6 KINASE ALPHA-1;
COMPND 13 CHAIN: I;
COMPND 14 FRAGMENT: UNP RESIDUES 713-729;
COMPND 15 SYNONYM: S6K-ALPHA-1,90 KDA RIBOSOMAL PROTEIN S6 KINASE 1,P90S6K,MAP
COMPND 16 KINASE-ACTIVATED PROTEIN KINASE 1A,MAPKAPK-1A,RIBOSOMAL S6 KINASE 1,
COMPND 17 RSK-1;
COMPND 18 EC: 2.7.11.1;
COMPND 19 ENGINEERED: YES;
COMPND 20 OTHER_DETAILS: BIVALENT ERK INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MAPK1, ERK2, PRKM1, PRKM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS KINASE, MAPK, PHOSPHORYLATION, CANCER, TRANSFERASE, TRANSFERASE-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.LECHTENBERG,S.J.RIEDL
REVDAT 4 04-DEC-19 5V62 1 REMARK
REVDAT 3 18-APR-18 5V62 1 JRNL REMARK
REVDAT 2 13-SEP-17 5V62 1 REMARK
REVDAT 1 26-JUL-17 5V62 0
JRNL AUTH B.C.LECHTENBERG,P.D.MACE,E.H.SESSIONS,R.WILLIAMSON,
JRNL AUTH 2 R.STALDER,Y.WALLEZ,G.P.ROTH,S.J.RIEDL,E.B.PASQUALE
JRNL TITL STRUCTURE-GUIDED STRATEGY FOR THE DEVELOPMENT OF POTENT
JRNL TITL 2 BIVALENT ERK INHIBITORS.
JRNL REF ACS MED CHEM LETT V. 8 726 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 28740606
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00127
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 38622
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.75000
REMARK 3 B22 (A**2) : 0.80000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.338
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 5V62 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000226937.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40711
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 19.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 1.11200
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-BICINE PH 8.5, 0.02 M EACH
REMARK 280 OF 1,6-HEXANEDIOL, 1-BUTANOL, 1,2-PROPANEDIOL, 2-PROPANOL, 1,4-
REMARK 280 BUTANEDIOL, 1,3-PROPANEDIOL, 20% V/V PEG550MME, 10% W/V PEG20,
REMARK 280 000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 21.16350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.46900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.94400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.46900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.16350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.94400
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
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 AZK I 709
REMARK 465 GLY I 710
REMARK 465 THR I 711
REMARK 465 ALA I 712
REMARK 465 VAL I 727
REMARK 465 ARG I 728
REMARK 465 LYS I 729
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 ND2 ASN A 158 O HOH A 501 2.04
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 ASP A 149 41.11 -152.40
REMARK 500 ASP A 167 83.65 62.38
REMARK 500 ASP A 167 83.65 68.95
REMARK 500 ALA A 189 166.64 63.65
REMARK 500 ASN A 201 59.36 -144.17
REMARK 500 LEU A 294 45.53 -92.40
REMARK 500 MET A 333 4.54 -68.75
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 755 DISTANCE = 7.38 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 LIGAND AKS LINKS FRZ AND AZIDO-LYSINE (AZK) OF PEPTIDE INHIBITOR TO
REMARK 600 FORM BIVALENT ERK INHIBITOR SBP3
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 AKS A 407
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues FRZ A 406 and AKS A
REMARK 800 407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V60 RELATED DB: PDB
REMARK 900 RELATED ID: 5V61 RELATED DB: PDB
DBREF 5V62 A 10 360 UNP P28482 MK01_HUMAN 10 360
DBREF 5V62 I 713 729 UNP Q15418 KS6A1_HUMAN 713 729
SEQADV 5V62 AZK I 709 UNP Q15418 INSERTION
SEQADV 5V62 GLY I 710 UNP Q15418 INSERTION
SEQADV 5V62 THR I 711 UNP Q15418 INSERTION
SEQADV 5V62 ALA I 712 UNP Q15418 INSERTION
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 VAL 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 CYS 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 TPO GLU PTR 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
SEQRES 1 I 21 AZK GLY THR ALA GLN LEU LYS PRO ILE GLU SER SER ILE
SEQRES 2 I 21 LEU ALA GLN ARG ARG VAL ARG LYS
MODRES 5V62 TPO A 185 THR MODIFIED RESIDUE
MODRES 5V62 PTR A 187 TYR MODIFIED RESIDUE
HET TPO A 185 11
HET PTR A 187 16
HET GOL A 401 6
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET FRZ A 406 25
HET AKS A 407 5
HETNAM TPO PHOSPHOTHREONINE
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM GOL GLYCEROL
HETNAM FRZ 5-(2-PHENYLPYRAZOLO[1,5-A]PYRIDIN-3-YL)-1H-PYRAZOLO[3,
HETNAM 2 FRZ 4-C]PYRIDAZIN-3-AMINE
HETNAM AKS N-(HEX-5-YN-1-YL)HEXANAMIDE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN PTR PHOSPHONOTYROSINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN FRZ FR180204
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 3 GOL 5(C3 H8 O3)
FORMUL 8 FRZ C18 H13 N7
FORMUL 9 AKS C12 H21 N O
FORMUL 10 HOH *255(H2 O)
HELIX 1 AA1 HIS A 61 PHE A 78 1 18
HELIX 2 AA2 THR A 94 MET A 98 5 5
HELIX 3 AA3 LEU A 112 GLN A 119 1 8
HELIX 4 AA4 SER A 122 ALA A 143 1 22
HELIX 5 AA5 LYS A 151 SER A 153 5 3
HELIX 6 AA6 THR A 190 ARG A 194 5 5
HELIX 7 AA7 ALA A 195 ASN A 201 1 7
HELIX 8 AA8 LYS A 207 ASN A 224 1 18
HELIX 9 AA9 HIS A 232 GLY A 245 1 14
HELIX 10 AB1 SER A 248 ASN A 253 1 6
HELIX 11 AB2 ASN A 257 LEU A 267 1 11
HELIX 12 AB3 PRO A 274 PHE A 279 1 6
HELIX 13 AB4 ASP A 283 LEU A 294 1 12
HELIX 14 AB5 GLU A 303 ALA A 309 1 7
HELIX 15 AB6 HIS A 310 GLU A 314 5 5
HELIX 16 AB7 ASP A 318 GLU A 322 5 5
HELIX 17 AB8 LYS A 330 LEU A 335 5 6
HELIX 18 AB9 PRO A 339 ALA A 352 1 14
HELIX 19 AC1 ARG A 353 GLN A 355 5 3
HELIX 20 AC2 PRO I 716 SER I 719 5 4
HELIX 21 AC3 SER I 720 ARG I 726 1 7
SHEET 1 AA1 2 GLU A 12 VAL A 14 0
SHEET 2 AA1 2 GLN A 17 PHE A 19 -1 O PHE A 19 N GLU A 12
SHEET 1 AA2 5 TYR A 25 GLY A 34 0
SHEET 2 AA2 5 GLY A 37 ASP A 44 -1 O VAL A 39 N GLY A 32
SHEET 3 AA2 5 VAL A 49 ILE A 56 -1 O LYS A 55 N MET A 38
SHEET 4 AA2 5 VAL A 101 ASP A 106 -1 O GLN A 105 N ALA A 52
SHEET 5 AA2 5 ASP A 88 ILE A 90 -1 N ILE A 90 O TYR A 102
SHEET 1 AA3 3 THR A 110 ASP A 111 0
SHEET 2 AA3 3 LEU A 155 LEU A 157 -1 O LEU A 157 N THR A 110
SHEET 3 AA3 3 LEU A 163 ILE A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 AA4 2 VAL A 145 LEU A 146 0
SHEET 2 AA4 2 ARG A 172 VAL A 173 -1 O ARG A 172 N LEU A 146
LINK C LEU A 184 N TPO A 185 1555 1555 1.32
LINK C TPO A 185 N GLU A 186 1555 1555 1.32
LINK C GLU A 186 N PTR A 187 1555 1555 1.32
LINK C PTR A 187 N VAL A 188 1555 1555 1.33
LINK N29 FRZ A 406 C5 AKS A 407 1555 1555 1.45
CISPEP 1 GLY A 22 PRO A 23 0 -2.58
SITE 1 AC1 3 ASN A 238 HIS A 239 HOH A 529
SITE 1 AC2 2 TYR A 233 HOH A 557
SITE 1 AC3 1 MET A 199
SITE 1 AC4 8 ASP A 20 ARG A 91 ALA A 92 GLN A 97
SITE 2 AC4 8 MET A 98 LYS A 99 ASP A 100 HOH A 548
SITE 1 AC5 4 ASP A 179 PHE A 183 PHE A 331 HOH A 606
SITE 1 AC6 16 TYR A 36 ALA A 52 LYS A 54 ILE A 103
SITE 2 AC6 16 GLN A 105 ASP A 106 MET A 108 GLU A 109
SITE 3 AC6 16 THR A 110 LYS A 114 ASN A 154 LEU A 156
SITE 4 AC6 16 CYS A 166 ASP A 167 HOH A 541 HOH A 568
CRYST1 42.327 77.888 152.938 90.00 90.00 90.00 P 21 21 21 4
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 0.023626 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012839 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006539 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
