HEADER CALCIUM-BINDING PROTEIN 28-AUG-08 3EBM
TITLE CRYSTAL STRUCTURE OF HUMAN TRANSLATIONALLY CONTROLLED TUMOUR
TITLE 2 ASSOCIATED PROTEIN (HTCTP) MUTANT E12V
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATIONALLY-CONTROLLED TUMOR PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TRANSLATIONALLY CONTROLLED TUMOUR ASSOCIATED PROTEIN, HTCTP,
COMPND 5 TCTP, P23, HISTAMINE-RELEASING FACTOR, HRF, FORTILIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: MAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TPT1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-22B+
KEYWDS TCTP, E12V, CALCIUM, CYTOPLASM, PHOSPHOPROTEIN, CALCIUM-BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.YANG,X.DONG,C.ZHONG,J.DING
REVDAT 4 01-NOV-23 3EBM 1 REMARK
REVDAT 3 10-NOV-21 3EBM 1 SEQADV
REVDAT 2 10-NOV-09 3EBM 1 JRNL
REVDAT 1 30-JUN-09 3EBM 0
JRNL AUTH X.DONG,B.YANG,Y.LI,C.ZHONG,J.DING
JRNL TITL MOLECULAR BASIS OF THE ACCELERATION OF THE GDP-GTP EXCHANGE
JRNL TITL 2 OF HUMAN RAS HOMOLOG ENRICHED IN BRAIN BY HUMAN
JRNL TITL 3 TRANSLATIONALLY CONTROLLED TUMOR PROTEIN.
JRNL REF J.BIOL.CHEM. V. 284 23754 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19570981
JRNL DOI 10.1074/JBC.M109.012823
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 26115
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) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1366
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1832
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.3980
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.4590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4788
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 37
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.24000
REMARK 3 B22 (A**2) : 7.40000
REMARK 3 B33 (A**2) : -5.15000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.322
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.267
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.599
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4888 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6542 ; 0.897 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 575 ; 4.505 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;34.026 ;24.625
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 962 ;15.131 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.239 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 691 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3631 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1984 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3388 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 140 ; 0.124 ; 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): 44 ; 0.228 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.175 ; 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): 3006 ; 3.118 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4668 ; 4.263 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2133 ; 4.078 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1874 ; 6.503 ; 4.500
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): 5139 ; 3.453 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 37 ; 1.227 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4792 ; 1.004 ; 3.000
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: NULL
REMARK 4
REMARK 4 3EBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049120.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27483
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 97.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.46700
REMARK 200 R SYM FOR SHELL (I) : 0.46700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1YZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, PH 8.2, 22% PEG 6000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277.0K
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 39.09600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.96000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.77150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.96000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.09600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.77150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 350
REMARK 350 BIOMOLECULE: 3
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: 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 350
REMARK 350 BIOMOLECULE: 4
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: D
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 ARG A 38
REMARK 465 THR A 39
REMARK 465 GLU A 40
REMARK 465 GLY A 41
REMARK 465 ASN A 42
REMARK 465 ILE A 43
REMARK 465 ASP A 44
REMARK 465 ASP A 45
REMARK 465 SER A 46
REMARK 465 LEU A 47
REMARK 465 ILE A 48
REMARK 465 GLY A 49
REMARK 465 GLY A 50
REMARK 465 ASN A 51
REMARK 465 ALA A 52
REMARK 465 SER A 53
REMARK 465 ALA A 54
REMARK 465 GLU A 55
REMARK 465 GLY A 56
REMARK 465 PRO A 57
REMARK 465 GLU A 58
REMARK 465 GLY A 59
REMARK 465 GLU A 60
REMARK 465 GLY A 61
REMARK 465 THR A 62
REMARK 465 GLU A 63
REMARK 465 SER A 64
REMARK 465 THR A 65
REMARK 465 VAL A 66
REMARK 465 HIS A 177
REMARK 465 HIS A 178
REMARK 465 HIS A 179
REMARK 465 HIS A 180
REMARK 465 THR B 39
REMARK 465 GLU B 40
REMARK 465 GLY B 41
REMARK 465 ASN B 42
REMARK 465 ILE B 43
REMARK 465 ASP B 44
REMARK 465 ASP B 45
REMARK 465 SER B 46
REMARK 465 LEU B 47
REMARK 465 ILE B 48
REMARK 465 GLY B 49
REMARK 465 GLY B 50
REMARK 465 ASN B 51
REMARK 465 ALA B 52
REMARK 465 SER B 53
REMARK 465 ALA B 54
REMARK 465 GLU B 55
REMARK 465 GLY B 56
REMARK 465 PRO B 57
REMARK 465 GLU B 58
REMARK 465 GLY B 59
REMARK 465 GLU B 60
REMARK 465 GLY B 61
REMARK 465 THR B 62
REMARK 465 GLU B 63
REMARK 465 SER B 64
REMARK 465 THR B 65
REMARK 465 VAL B 66
REMARK 465 ILE B 67
REMARK 465 THR B 68
REMARK 465 HIS B 178
REMARK 465 HIS B 179
REMARK 465 HIS B 180
REMARK 465 SER C 37
REMARK 465 ARG C 38
REMARK 465 THR C 39
REMARK 465 GLU C 40
REMARK 465 GLY C 41
REMARK 465 ASN C 42
REMARK 465 ILE C 43
REMARK 465 ASP C 44
REMARK 465 ASP C 45
REMARK 465 SER C 46
REMARK 465 LEU C 47
REMARK 465 ILE C 48
REMARK 465 GLY C 49
REMARK 465 GLY C 50
REMARK 465 ASN C 51
REMARK 465 ALA C 52
REMARK 465 SER C 53
REMARK 465 ALA C 54
REMARK 465 GLU C 55
REMARK 465 GLY C 56
REMARK 465 PRO C 57
REMARK 465 GLU C 58
REMARK 465 GLY C 59
REMARK 465 GLU C 60
REMARK 465 GLY C 61
REMARK 465 THR C 62
REMARK 465 GLU C 63
REMARK 465 SER C 64
REMARK 465 THR C 65
REMARK 465 VAL C 66
REMARK 465 ILE C 67
REMARK 465 HIS C 177
REMARK 465 HIS C 178
REMARK 465 HIS C 179
REMARK 465 HIS C 180
REMARK 465 ARG D 38
REMARK 465 THR D 39
REMARK 465 GLU D 40
REMARK 465 GLY D 41
REMARK 465 ASN D 42
REMARK 465 ILE D 43
REMARK 465 ASP D 44
REMARK 465 ASP D 45
REMARK 465 SER D 46
REMARK 465 LEU D 47
REMARK 465 ILE D 48
REMARK 465 GLY D 49
REMARK 465 GLY D 50
REMARK 465 ASN D 51
REMARK 465 ALA D 52
REMARK 465 SER D 53
REMARK 465 ALA D 54
REMARK 465 GLU D 55
REMARK 465 GLY D 56
REMARK 465 PRO D 57
REMARK 465 GLU D 58
REMARK 465 GLY D 59
REMARK 465 GLU D 60
REMARK 465 GLY D 61
REMARK 465 THR D 62
REMARK 465 GLU D 63
REMARK 465 SER D 64
REMARK 465 THR D 65
REMARK 465 VAL D 66
REMARK 465 ILE D 67
REMARK 465 HIS D 175
REMARK 465 HIS D 176
REMARK 465 HIS D 177
REMARK 465 HIS D 178
REMARK 465 HIS D 179
REMARK 465 HIS D 180
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 HIS B 177 CG HIS B 177 CD2 0.058
REMARK 500 LYS D 130 CE LYS D 130 NZ 0.284
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 B 152 -165.85 -68.45
REMARK 500 GLN D 106 -51.86 -129.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YZ1 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF WILD TYPE PROTEIN
DBREF 3EBM A 1 172 UNP P13693 TCTP_HUMAN 1 172
DBREF 3EBM B 1 172 UNP P13693 TCTP_HUMAN 1 172
DBREF 3EBM C 1 172 UNP P13693 TCTP_HUMAN 1 172
DBREF 3EBM D 1 172 UNP P13693 TCTP_HUMAN 1 172
SEQADV 3EBM VAL A 12 UNP P13693 GLU 12 ENGINEERED MUTATION
SEQADV 3EBM LEU A 173 UNP P13693 EXPRESSION TAG
SEQADV 3EBM GLU A 174 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS A 175 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS A 176 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS A 177 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS A 178 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS A 179 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS A 180 UNP P13693 EXPRESSION TAG
SEQADV 3EBM VAL B 12 UNP P13693 GLU 12 ENGINEERED MUTATION
SEQADV 3EBM LEU B 173 UNP P13693 EXPRESSION TAG
SEQADV 3EBM GLU B 174 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS B 175 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS B 176 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS B 177 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS B 178 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS B 179 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS B 180 UNP P13693 EXPRESSION TAG
SEQADV 3EBM VAL C 12 UNP P13693 GLU 12 ENGINEERED MUTATION
SEQADV 3EBM LEU C 173 UNP P13693 EXPRESSION TAG
SEQADV 3EBM GLU C 174 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS C 175 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS C 176 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS C 177 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS C 178 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS C 179 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS C 180 UNP P13693 EXPRESSION TAG
SEQADV 3EBM VAL D 12 UNP P13693 GLU 12 ENGINEERED MUTATION
SEQADV 3EBM LEU D 173 UNP P13693 EXPRESSION TAG
SEQADV 3EBM GLU D 174 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS D 175 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS D 176 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS D 177 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS D 178 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS D 179 UNP P13693 EXPRESSION TAG
SEQADV 3EBM HIS D 180 UNP P13693 EXPRESSION TAG
SEQRES 1 A 180 MET ILE ILE TYR ARG ASP LEU ILE SER HIS ASP VAL MET
SEQRES 2 A 180 PHE SER ASP ILE TYR LYS ILE ARG GLU ILE ALA ASP GLY
SEQRES 3 A 180 LEU CYS LEU GLU VAL GLU GLY LYS MET VAL SER ARG THR
SEQRES 4 A 180 GLU GLY ASN ILE ASP ASP SER LEU ILE GLY GLY ASN ALA
SEQRES 5 A 180 SER ALA GLU GLY PRO GLU GLY GLU GLY THR GLU SER THR
SEQRES 6 A 180 VAL ILE THR GLY VAL ASP ILE VAL MET ASN HIS HIS LEU
SEQRES 7 A 180 GLN GLU THR SER PHE THR LYS GLU ALA TYR LYS LYS TYR
SEQRES 8 A 180 ILE LYS ASP TYR MET LYS SER ILE LYS GLY LYS LEU GLU
SEQRES 9 A 180 GLU GLN ARG PRO GLU ARG VAL LYS PRO PHE MET THR GLY
SEQRES 10 A 180 ALA ALA GLU GLN ILE LYS HIS ILE LEU ALA ASN PHE LYS
SEQRES 11 A 180 ASN TYR GLN PHE PHE ILE GLY GLU ASN MET ASN PRO ASP
SEQRES 12 A 180 GLY MET VAL ALA LEU LEU ASP TYR ARG GLU ASP GLY VAL
SEQRES 13 A 180 THR PRO TYR MET ILE PHE PHE LYS ASP GLY LEU GLU MET
SEQRES 14 A 180 GLU LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 180 MET ILE ILE TYR ARG ASP LEU ILE SER HIS ASP VAL MET
SEQRES 2 B 180 PHE SER ASP ILE TYR LYS ILE ARG GLU ILE ALA ASP GLY
SEQRES 3 B 180 LEU CYS LEU GLU VAL GLU GLY LYS MET VAL SER ARG THR
SEQRES 4 B 180 GLU GLY ASN ILE ASP ASP SER LEU ILE GLY GLY ASN ALA
SEQRES 5 B 180 SER ALA GLU GLY PRO GLU GLY GLU GLY THR GLU SER THR
SEQRES 6 B 180 VAL ILE THR GLY VAL ASP ILE VAL MET ASN HIS HIS LEU
SEQRES 7 B 180 GLN GLU THR SER PHE THR LYS GLU ALA TYR LYS LYS TYR
SEQRES 8 B 180 ILE LYS ASP TYR MET LYS SER ILE LYS GLY LYS LEU GLU
SEQRES 9 B 180 GLU GLN ARG PRO GLU ARG VAL LYS PRO PHE MET THR GLY
SEQRES 10 B 180 ALA ALA GLU GLN ILE LYS HIS ILE LEU ALA ASN PHE LYS
SEQRES 11 B 180 ASN TYR GLN PHE PHE ILE GLY GLU ASN MET ASN PRO ASP
SEQRES 12 B 180 GLY MET VAL ALA LEU LEU ASP TYR ARG GLU ASP GLY VAL
SEQRES 13 B 180 THR PRO TYR MET ILE PHE PHE LYS ASP GLY LEU GLU MET
SEQRES 14 B 180 GLU LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 180 MET ILE ILE TYR ARG ASP LEU ILE SER HIS ASP VAL MET
SEQRES 2 C 180 PHE SER ASP ILE TYR LYS ILE ARG GLU ILE ALA ASP GLY
SEQRES 3 C 180 LEU CYS LEU GLU VAL GLU GLY LYS MET VAL SER ARG THR
SEQRES 4 C 180 GLU GLY ASN ILE ASP ASP SER LEU ILE GLY GLY ASN ALA
SEQRES 5 C 180 SER ALA GLU GLY PRO GLU GLY GLU GLY THR GLU SER THR
SEQRES 6 C 180 VAL ILE THR GLY VAL ASP ILE VAL MET ASN HIS HIS LEU
SEQRES 7 C 180 GLN GLU THR SER PHE THR LYS GLU ALA TYR LYS LYS TYR
SEQRES 8 C 180 ILE LYS ASP TYR MET LYS SER ILE LYS GLY LYS LEU GLU
SEQRES 9 C 180 GLU GLN ARG PRO GLU ARG VAL LYS PRO PHE MET THR GLY
SEQRES 10 C 180 ALA ALA GLU GLN ILE LYS HIS ILE LEU ALA ASN PHE LYS
SEQRES 11 C 180 ASN TYR GLN PHE PHE ILE GLY GLU ASN MET ASN PRO ASP
SEQRES 12 C 180 GLY MET VAL ALA LEU LEU ASP TYR ARG GLU ASP GLY VAL
SEQRES 13 C 180 THR PRO TYR MET ILE PHE PHE LYS ASP GLY LEU GLU MET
SEQRES 14 C 180 GLU LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 180 MET ILE ILE TYR ARG ASP LEU ILE SER HIS ASP VAL MET
SEQRES 2 D 180 PHE SER ASP ILE TYR LYS ILE ARG GLU ILE ALA ASP GLY
SEQRES 3 D 180 LEU CYS LEU GLU VAL GLU GLY LYS MET VAL SER ARG THR
SEQRES 4 D 180 GLU GLY ASN ILE ASP ASP SER LEU ILE GLY GLY ASN ALA
SEQRES 5 D 180 SER ALA GLU GLY PRO GLU GLY GLU GLY THR GLU SER THR
SEQRES 6 D 180 VAL ILE THR GLY VAL ASP ILE VAL MET ASN HIS HIS LEU
SEQRES 7 D 180 GLN GLU THR SER PHE THR LYS GLU ALA TYR LYS LYS TYR
SEQRES 8 D 180 ILE LYS ASP TYR MET LYS SER ILE LYS GLY LYS LEU GLU
SEQRES 9 D 180 GLU GLN ARG PRO GLU ARG VAL LYS PRO PHE MET THR GLY
SEQRES 10 D 180 ALA ALA GLU GLN ILE LYS HIS ILE LEU ALA ASN PHE LYS
SEQRES 11 D 180 ASN TYR GLN PHE PHE ILE GLY GLU ASN MET ASN PRO ASP
SEQRES 12 D 180 GLY MET VAL ALA LEU LEU ASP TYR ARG GLU ASP GLY VAL
SEQRES 13 D 180 THR PRO TYR MET ILE PHE PHE LYS ASP GLY LEU GLU MET
SEQRES 14 D 180 GLU LYS CYS LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *37(H2 O)
HELIX 1 1 ASP A 71 HIS A 77 1 7
HELIX 2 2 THR A 84 ARG A 107 1 24
HELIX 3 3 ARG A 110 ASN A 128 1 19
HELIX 4 4 PHE A 129 TYR A 132 5 4
HELIX 5 5 VAL B 70 HIS B 76 1 7
HELIX 6 6 THR B 84 ARG B 107 1 24
HELIX 7 7 ARG B 110 ASN B 128 1 19
HELIX 8 8 PHE B 129 TYR B 132 5 4
HELIX 9 9 ALA C 24 GLY C 26 5 3
HELIX 10 10 VAL C 70 HIS C 77 1 8
HELIX 11 11 THR C 84 ARG C 107 1 24
HELIX 12 12 ARG C 110 ASN C 128 1 19
HELIX 13 13 PHE C 129 TYR C 132 5 4
HELIX 14 14 ASP D 71 HIS D 76 1 6
HELIX 15 15 THR D 84 ARG D 107 1 24
HELIX 16 16 ARG D 110 LEU D 126 1 17
HELIX 17 17 ASN D 128 TYR D 132 5 5
SHEET 1 A 3 VAL A 12 SER A 15 0
SHEET 2 A 3 ILE A 2 ASP A 6 -1 N TYR A 4 O PHE A 14
SHEET 3 A 3 LEU A 167 LYS A 171 -1 O GLU A 168 N ARG A 5
SHEET 1 B 6 LYS A 19 ILE A 23 0
SHEET 2 B 6 CYS A 28 GLU A 32 -1 O GLU A 30 N ARG A 21
SHEET 3 B 6 PRO A 158 PHE A 163 -1 O MET A 160 N VAL A 31
SHEET 4 B 6 ALA A 147 TYR A 151 -1 N ASP A 150 O TYR A 159
SHEET 5 B 6 GLN A 133 ILE A 136 -1 N PHE A 135 O ALA A 147
SHEET 6 B 6 GLN A 79 THR A 81 -1 N GLN A 79 O ILE A 136
SHEET 1 C 2 MET A 35 VAL A 36 0
SHEET 2 C 2 GLY A 69 VAL A 70 -1 O GLY A 69 N VAL A 36
SHEET 1 D 6 VAL B 12 SER B 15 0
SHEET 2 D 6 ILE B 2 ASP B 6 -1 N TYR B 4 O PHE B 14
SHEET 3 D 6 LEU B 167 HIS B 175 -1 O GLU B 168 N ARG B 5
SHEET 4 D 6 LEU C 167 HIS C 175 -1 O LYS C 171 N LEU B 173
SHEET 5 D 6 ILE C 2 ASP C 6 -1 N ILE C 3 O GLU C 170
SHEET 6 D 6 VAL C 12 SER C 15 -1 O PHE C 14 N TYR C 4
SHEET 1 E 6 ILE B 20 ILE B 23 0
SHEET 2 E 6 CYS B 28 GLU B 32 -1 O GLU B 30 N ARG B 21
SHEET 3 E 6 PRO B 158 PHE B 163 -1 O MET B 160 N VAL B 31
SHEET 4 E 6 ALA B 147 TYR B 151 -1 N ASP B 150 O TYR B 159
SHEET 5 E 6 GLN B 133 ILE B 136 -1 N GLN B 133 O LEU B 149
SHEET 6 E 6 GLN B 79 THR B 81 -1 N GLN B 79 O ILE B 136
SHEET 1 F 6 LYS C 19 ILE C 23 0
SHEET 2 F 6 CYS C 28 GLU C 32 -1 O GLU C 30 N ARG C 21
SHEET 3 F 6 PRO C 158 PHE C 163 -1 O MET C 160 N VAL C 31
SHEET 4 F 6 ALA C 147 TYR C 151 -1 N ASP C 150 O TYR C 159
SHEET 5 F 6 GLN C 133 ILE C 136 -1 N PHE C 135 O ALA C 147
SHEET 6 F 6 GLN C 79 THR C 81 -1 N GLN C 79 O ILE C 136
SHEET 1 G 3 VAL D 12 SER D 15 0
SHEET 2 G 3 ILE D 2 ASP D 6 -1 N TYR D 4 O MET D 13
SHEET 3 G 3 LEU D 167 LYS D 171 -1 O GLU D 168 N ARG D 5
SHEET 1 H 6 LYS D 19 ILE D 23 0
SHEET 2 H 6 CYS D 28 GLU D 32 -1 O GLU D 30 N ARG D 21
SHEET 3 H 6 PRO D 158 PHE D 163 -1 O MET D 160 N VAL D 31
SHEET 4 H 6 ALA D 147 TYR D 151 -1 N ASP D 150 O TYR D 159
SHEET 5 H 6 GLN D 133 ILE D 136 -1 N PHE D 135 O ALA D 147
SHEET 6 H 6 GLN D 79 THR D 81 -1 N THR D 81 O PHE D 134
SHEET 1 I 2 MET D 35 VAL D 36 0
SHEET 2 I 2 GLY D 69 VAL D 70 -1 O GLY D 69 N VAL D 36
SSBOND 1 CYS B 172 CYS C 172 1555 1555 2.04
CRYST1 78.192 81.543 139.920 90.00 90.00 90.00 P 21 21 21 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 0.012789 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007147 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
