HEADER SIGNALING PROTEIN 16-MAR-12 2LQW
TITLE SOLUTION STRUCTURE OF PHOSPHORYLATED CRKL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRK-LIKE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CRKL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET42A
KEYWDS SH2, SH3, V-CRK SARCOMA VIRUS CT10, ONCOGENE HOMOLOG, (AVIAN)-LIKE,
KEYWDS 2 PCRKL, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.JANKOWSKI,T.SALEH,C.KALODIMOS
REVDAT 3 14-JUN-23 2LQW 1 REMARK LINK
REVDAT 2 06-JUN-12 2LQW 1 JRNL
REVDAT 1 16-MAY-12 2LQW 0
JRNL AUTH W.JANKOWSKI,T.SALEH,M.T.PAI,G.SRIRAM,R.B.BIRGE,C.G.KALODIMOS
JRNL TITL DOMAIN ORGANIZATION DIFFERENCES EXPLAIN BCR-ABL'S PREFERENCE
JRNL TITL 2 FOR CRKL OVER CRKII.
JRNL REF NAT.CHEM.BIOL. V. 8 590 2012
JRNL REFN ISSN 1552-4450
JRNL PMID 22581121
JRNL DOI 10.1038/NCHEMBIO.954
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER A. T. ET.AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LQW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000102720.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3-0.8 MM [U-100% 15N]
REMARK 210 POTASSIUM PHOSPHATE, 0.3-0.8 MM
REMARK 210 [U-100% 13C; U-100% 15N]
REMARK 210 POTASSIUM CHLORIDE, 0.3-0.8 MM
REMARK 210 [U-13C; U-15N; U-2H] BETA-
REMARK 210 MERCAPTOETHANOL, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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
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 HD23 LEU A 125 HG21 ILE A 152 1.19
REMARK 500 H SER A 20 HD2 ARG A 39 1.28
REMARK 500 HB3 TYR A 105 HD3 PRO A 106 1.31
REMARK 500 HB2 ARG A 32 HG SER A 53 1.35
REMARK 500 HH21 ARG A 57 O ILE A 153 1.57
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 2 PRO A 237 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 13 ARG A 57 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 15 ARG A 57 N - CA - CB ANGL. DEV. = -12.2 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 1 SER A 2 -85.92 61.72
REMARK 500 1 SER A 3 -51.14 66.49
REMARK 500 1 SER A 9 -53.18 -176.39
REMARK 500 1 SER A 12 23.97 -73.87
REMARK 500 1 PRO A 18 95.96 -69.01
REMARK 500 1 VAL A 19 -71.53 -128.88
REMARK 500 1 SER A 20 170.01 78.52
REMARK 500 1 CYS A 44 121.74 -170.62
REMARK 500 1 PRO A 45 104.59 -40.41
REMARK 500 1 PRO A 67 56.37 -61.69
REMARK 500 1 ASP A 75 -50.21 76.74
REMARK 500 1 TYR A 92 108.90 72.80
REMARK 500 1 ASP A 94 -140.22 172.55
REMARK 500 1 PRO A 103 177.58 -55.80
REMARK 500 1 TYR A 105 -69.30 -159.19
REMARK 500 1 PRO A 106 -87.58 -94.36
REMARK 500 1 PRO A 109 -150.15 -102.16
REMARK 500 1 ALA A 121 166.95 66.90
REMARK 500 1 ASN A 124 -96.06 -97.34
REMARK 500 1 LEU A 125 123.96 62.93
REMARK 500 1 GLU A 126 -74.59 -167.59
REMARK 500 1 ASP A 133 129.30 79.65
REMARK 500 1 ASN A 137 73.32 50.22
REMARK 500 1 ASP A 138 -176.28 -171.14
REMARK 500 1 LYS A 145 -168.51 -122.15
REMARK 500 1 ARG A 183 32.39 -177.95
REMARK 500 1 HIS A 187 -74.82 -103.82
REMARK 500 1 LYS A 189 97.79 67.95
REMARK 500 1 ARG A 193 -93.36 64.78
REMARK 500 1 SER A 197 -94.98 50.37
REMARK 500 1 PTR A 207 -161.53 59.14
REMARK 500 1 PRO A 210 100.61 -55.58
REMARK 500 1 THR A 213 76.00 57.36
REMARK 500 1 PRO A 215 35.65 -83.12
REMARK 500 1 LEU A 216 105.09 64.96
REMARK 500 1 ALA A 225 -43.85 73.24
REMARK 500 1 GLN A 234 98.16 -66.17
REMARK 500 1 PRO A 248 52.88 -69.10
REMARK 500 1 CYS A 249 -146.71 -100.28
REMARK 500 1 ASN A 280 -81.00 64.36
REMARK 500 1 GLU A 301 -75.40 71.51
REMARK 500 2 SER A 9 -41.07 -175.48
REMARK 500 2 VAL A 19 -76.35 -132.88
REMARK 500 2 SER A 20 167.99 74.47
REMARK 500 2 ARG A 32 -51.56 55.58
REMARK 500 2 HIS A 33 134.01 74.19
REMARK 500 2 ASN A 55 89.51 -36.20
REMARK 500 2 SER A 56 62.55 39.80
REMARK 500 2 ARG A 57 50.57 -162.14
REMARK 500 2 ASP A 75 -48.09 75.94
REMARK 500
REMARK 500 THIS ENTRY HAS 872 RAMACHANDRAN OUTLIERS.
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 VAL A 178 GLU A 179 9 144.45
REMARK 500 SER A 56 ARG A 57 11 -149.77
REMARK 500 ASN A 68 ARG A 69 15 -149.01
REMARK 500 ASP A 252 LYS A 253 17 147.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 169 0.09 SIDE CHAIN
REMARK 500 4 ARG A 169 0.08 SIDE CHAIN
REMARK 500 6 ARG A 169 0.09 SIDE CHAIN
REMARK 500 8 ARG A 169 0.07 SIDE CHAIN
REMARK 500 9 ARG A 39 0.08 SIDE CHAIN
REMARK 500 9 ARG A 169 0.11 SIDE CHAIN
REMARK 500 11 ARG A 57 0.10 SIDE CHAIN
REMARK 500 11 ARG A 129 0.08 SIDE CHAIN
REMARK 500 11 ARG A 169 0.08 SIDE CHAIN
REMARK 500 12 ARG A 169 0.08 SIDE CHAIN
REMARK 500 15 ARG A 169 0.10 SIDE CHAIN
REMARK 500 17 ARG A 169 0.10 SIDE CHAIN
REMARK 500 20 ARG A 169 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18333 RELATED DB: BMRB
DBREF 2LQW A 1 303 UNP P46109 CRKL_HUMAN 1 303
SEQRES 1 A 303 MET SER SER ALA ARG PHE ASP SER SER ASP ARG SER ALA
SEQRES 2 A 303 TRP TYR MET GLY PRO VAL SER ARG GLN GLU ALA GLN THR
SEQRES 3 A 303 ARG LEU GLN GLY GLN ARG HIS GLY MET PHE LEU VAL ARG
SEQRES 4 A 303 ASP SER SER THR CYS PRO GLY ASP TYR VAL LEU SER VAL
SEQRES 5 A 303 SER GLU ASN SER ARG VAL SER HIS TYR ILE ILE ASN SER
SEQRES 6 A 303 LEU PRO ASN ARG ARG PHE LYS ILE GLY ASP GLN GLU PHE
SEQRES 7 A 303 ASP HIS LEU PRO ALA LEU LEU GLU PHE TYR LYS ILE HIS
SEQRES 8 A 303 TYR LEU ASP THR THR THR LEU ILE GLU PRO ALA PRO ARG
SEQRES 9 A 303 TYR PRO SER PRO PRO MET GLY SER VAL SER ALA PRO ASN
SEQRES 10 A 303 LEU PRO THR ALA GLU ASP ASN LEU GLU TYR VAL ARG THR
SEQRES 11 A 303 LEU TYR ASP PHE PRO GLY ASN ASP ALA GLU ASP LEU PRO
SEQRES 12 A 303 PHE LYS LYS GLY GLU ILE LEU VAL ILE ILE GLU LYS PRO
SEQRES 13 A 303 GLU GLU GLN TRP TRP SER ALA ARG ASN LYS ASP GLY ARG
SEQRES 14 A 303 VAL GLY MET ILE PRO VAL PRO TYR VAL GLU LYS LEU VAL
SEQRES 15 A 303 ARG SER SER PRO HIS GLY LYS HIS GLY ASN ARG ASN SER
SEQRES 16 A 303 ASN SER TYR GLY ILE PRO GLU PRO ALA HIS ALA PTR ALA
SEQRES 17 A 303 GLN PRO GLN THR THR THR PRO LEU PRO ALA VAL SER GLY
SEQRES 18 A 303 SER PRO GLY ALA ALA ILE THR PRO LEU PRO SER THR GLN
SEQRES 19 A 303 ASN GLY PRO VAL PHE ALA LYS ALA ILE GLN LYS ARG VAL
SEQRES 20 A 303 PRO CYS ALA TYR ASP LYS THR ALA LEU ALA LEU GLU VAL
SEQRES 21 A 303 GLY ASP ILE VAL LYS VAL THR ARG MET ASN ILE ASN GLY
SEQRES 22 A 303 GLN TRP GLU GLY GLU VAL ASN GLY ARG LYS GLY LEU PHE
SEQRES 23 A 303 PRO PHE THR HIS VAL LYS ILE PHE ASP PRO GLN ASN PRO
SEQRES 24 A 303 ASP GLU ASN GLU
MODRES 2LQW PTR A 207 TYR O-PHOSPHOTYROSINE
HET PTR A 207 24
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
HELIX 1 1 ASP A 10 TRP A 14 1 5
HELIX 2 2 VAL A 19 LEU A 28 1 10
HELIX 3 3 HIS A 80 TYR A 92 1 13
HELIX 4 4 LYS A 189 ARG A 193 5 5
HELIX 5 5 CYS A 249 LYS A 253 5 5
SHEET 1 A 6 TYR A 15 PRO A 18 0
SHEET 2 A 6 MET A 35 ASP A 40 1 O VAL A 38 N MET A 16
SHEET 3 A 6 ASP A 47 GLU A 54 -1 O SER A 53 N MET A 35
SHEET 4 A 6 ARG A 57 SER A 65 -1 O TYR A 61 N LEU A 50
SHEET 5 A 6 PHE A 71 ILE A 73 -1 O LYS A 72 N ASN A 64
SHEET 6 A 6 GLN A 76 PHE A 78 -1 O PHE A 78 N PHE A 71
SHEET 1 B 5 VAL A 170 PRO A 174 0
SHEET 2 B 5 TRP A 160 ARG A 164 -1 N TRP A 161 O ILE A 173
SHEET 3 B 5 GLU A 148 GLU A 154 -1 N GLU A 154 O SER A 162
SHEET 4 B 5 TYR A 127 THR A 130 -1 N VAL A 128 O LEU A 150
SHEET 5 B 5 VAL A 178 LYS A 180 -1 O GLU A 179 N ARG A 129
SHEET 1 C 5 ARG A 282 PRO A 287 0
SHEET 2 C 5 GLN A 274 VAL A 279 -1 N TRP A 275 O PHE A 286
SHEET 3 C 5 ILE A 263 MET A 269 -1 N LYS A 265 O GLU A 278
SHEET 4 C 5 VAL A 238 ALA A 242 -1 N ALA A 240 O VAL A 264
SHEET 5 C 5 VAL A 291 ILE A 293 -1 O LYS A 292 N LYS A 241
LINK C ALA A 206 N PTR A 207 1555 1555 1.34
LINK C PTR A 207 N ALA A 208 1555 1555 1.32
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
