HEADER PROTEIN BINDING 02-OCT-06 2J6O
TITLE ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3 DOMAIN.
TITLE 2 CMS:CD2 HETEROTRIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD2-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN, RESIDUES 1-62;
COMPND 5 SYNONYM: CAS LIGAND WITH MULTIPLE SH3 DOMAINS, ADAPTER PROTEIN CMS,
COMPND 6 CMS;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: T-CELL SURFACE ANTIGEN CD2;
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: CMS BINDING SEQUENCE, RESIDUES 324-333;
COMPND 12 SYNONYM: T-CELL SURFACE ANTIGEN T11/LEU-5, LFA-2, LFA-3 RECEPTOR,
COMPND 13 ERYTHROCYTE RECEPTOR, ROSETTE RECEPTOR, CD2;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS PHOSPHORYLATION, ADAPTOR PROTEIN, EGFR DOWNREGULATION, CMS, SH3
KEYWDS 2 DOMAIN, SH3-BINDING, COILED COIL, SH3 DOMAIN RECOGNITION, SIGNALING
KEYWDS 3 PROTEIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MONCALIAN,N.CARDENES,Y.L.DERIBE,M.SPINOLA-AMILIBIA,I.DIKIC,J.BRAVO
REVDAT 4 05-JUL-17 2J6O 1 REMARK
REVDAT 3 24-FEB-09 2J6O 1 VERSN
REVDAT 2 13-DEC-06 2J6O 1 JRNL
REVDAT 1 11-OCT-06 2J6O 0
JRNL AUTH G.MONCALIAN,N.CARDENES,Y.L.DERIBE,M.SPINOLA-AMILIBIA,
JRNL AUTH 2 I.DIKIC,J.BRAVO
JRNL TITL ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3
JRNL TITL 2 DOMAIN.
JRNL REF J.BIOL.CHEM. V. 281 38845 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 17020880
JRNL DOI 10.1074/JBC.M606411200
REMARK 2
REMARK 2 RESOLUTION. 2.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 3932
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.520
REMARK 3 FREE R VALUE TEST SET COUNT : 177
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) : 9.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 47.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.4050
REMARK 3 BIN FREE R VALUE SET COUNT : 3
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 534
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : 0.42000
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): 0.361
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.259
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.792
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.907
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.891
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 562 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 762 ; 1.306 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 68 ; 5.750 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 32 ;29.944 ;24.062
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 104 ;16.883 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;17.052 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 82 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 432 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 220 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 353 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 33 ; 0.172 ; 0.200
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): 31 ; 0.256 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.196 ; 0.200
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): 335 ; 1.482 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 534 ; 2.310 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 254 ; 2.058 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 225 ; 3.007 ; 6.000
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 : BABINET MODEL PLUS MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. THE BIOLOGICAL UNIT OF THIS STRUCTURE IS A
REMARK 3 HETEROTRIMER CONSISTING OF TWO CMS SH3A DOMAINS AND ONE CD2
REMARK 3 PEPTIDE IN TWO ORIENTATIONS, WITH 0.5 OCCUPANCY EACH. THE SECOND
REMARK 3 CMS SH3A MOLECULES, AS WELL AS THE SECOND ORIENTATION OF THE
REMARK 3 PEPTIDE, ARE RELATED TO THAT IN THE ASYMMETRIC UNIT BY A
REMARK 3 CRYSTALLOGRAPHIC SYMMETRY OPERATION.
REMARK 4
REMARK 4 2J6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1290029425.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 110.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3933
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 34.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 16.66
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.6
REMARK 200 DATA REDUNDANCY IN SHELL : 14.22
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.74
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: CMSA-CBL-B STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3000, 0.1M ACETATE PH 5.5, PH
REMARK 280 5.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 33.19550
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 34.36800
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 33.19550
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 34.36800
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 33.19550
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 34.36800
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 33.19550
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 34.36800
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 33.19550
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 34.36800
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 33.19550
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 34.36800
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 33.19550
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 34.36800
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 33.19550
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 33.19550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 34.36800
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2002 LIES ON A SPECIAL POSITION.
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 ARG A 59
REMARK 465 GLU A 60
REMARK 465 THR A 61
REMARK 465 GLU A 62
REMARK 465 LYS C 324
REMARK 465 GLY C 325
REMARK 465 PRO C 326
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG C 330 CZ ARG C 330 NH1 0.089
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 C 330 NE - CZ - NH1 ANGL. DEV. = 3.0 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 VAL A 22 124.98 -38.12
REMARK 500 GLU A 34 108.81 -52.31
REMARK 500 PRO C 329 -167.43 -74.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CDB RELATED DB: PDB
REMARK 900 RELATED ID: 1GYA RELATED DB: PDB
REMARK 900 N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION
REMARK 900 DOMAIN OF HUMAN CD2
REMARK 900 RELATED ID: 1HNF RELATED DB: PDB
REMARK 900 CD2 (HUMAN)
REMARK 900 RELATED ID: 1L2Z RELATED DB: PDB
REMARK 900 CD2BP2-GYF DOMAIN IN COMPLEX WITH PROLINE- RICH CD2 TAILSEGMENT
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 2BZ8 RELATED DB: PDB
REMARK 900 N-TERMINAL SH3 DOMAIN OF CIN85 BOUND TO CBL-B PEPTIDE
REMARK 900 RELATED ID: 2J6F RELATED DB: PDB
REMARK 900 N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG) BOUND TO CBL-B
REMARK 900 PEPTIDE
REMARK 900 RELATED ID: 2J6K RELATED DB: PDB
REMARK 900 N-TERMINAL SH3 DOMAIN OF CMS (CD2AP HUMAN HOMOLOG)
REMARK 900 RELATED ID: 2J7I RELATED DB: PDB
REMARK 900 ATYPICAL POLYPROLINE RECOGNITION BY THE CMS N-TERMINAL SH3
REMARK 900 DOMAIN.CMS:CD2 HETERODIMER
DBREF 2J6O A 1 62 UNP Q9Y5K6 CD2AP_HUMAN 1 62
DBREF 2J6O C 324 333 UNP P06729 CD2_HUMAN 324 333
SEQRES 1 A 62 MET VAL ASP TYR ILE VAL GLU TYR ASP TYR ASP ALA VAL
SEQRES 2 A 62 HIS ASP ASP GLU LEU THR ILE ARG VAL GLY GLU ILE ILE
SEQRES 3 A 62 ARG ASN VAL LYS LYS LEU GLN GLU GLU GLY TRP LEU GLU
SEQRES 4 A 62 GLY GLU LEU ASN GLY ARG ARG GLY MET PHE PRO ASP ASN
SEQRES 5 A 62 PHE VAL LYS GLU ILE LYS ARG GLU THR GLU
SEQRES 1 C 10 LYS GLY PRO PRO LEU PRO ARG PRO ARG VAL
FORMUL 3 HOH *46(H2 O)
HELIX 1 1 ASP A 51 PHE A 53 5 3
SHEET 1 AA 5 ARG A 45 PRO A 50 0
SHEET 2 AA 5 TRP A 37 LEU A 42 -1 O LEU A 38 N PHE A 49
SHEET 3 AA 5 ILE A 25 LYS A 31 -1 O ARG A 27 N GLU A 41
SHEET 4 AA 5 TYR A 4 VAL A 6 -1 O TYR A 4 N ILE A 26
SHEET 5 AA 5 VAL A 54 GLU A 56 -1 O LYS A 55 N ILE A 5
CRYST1 66.391 66.391 68.736 90.00 90.00 90.00 I 4 2 2 16
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 0.015062 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014548 0.00000
(ATOM LINES ARE NOT SHOWN.)
END