HEADER COMPLEX (TRANSFERASE/PEPTIDE) 09-DEC-97 1A07
TITLE C-SRC (SH2 DOMAIN) COMPLEXED WITH ACE-MALONYL TYR-GLU-(N,N-DIPENTYL
TITLE 2 AMINE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-SRC TYROSINE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SH2 DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ACE-MALONYL TYR-GLU-(N,N-DIPENTYL AMINE);
COMPND 9 CHAIN: C, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 6 GENE: SRC;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11B;
SOURCE 12 EXPRESSION_SYSTEM_GENE: SRC;
SOURCE 13 MOL_ID: 2
KEYWDS COMPLEX (TRANSFERASE-PEPTIDE), COMPLEX (TRANSFERASE-PEPTIDE) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SHEWCHUK,S.JORDAN
REVDAT 4 02-AUG-23 1A07 1 REMARK LINK
REVDAT 3 07-MAR-18 1A07 1 REMARK
REVDAT 2 24-FEB-09 1A07 1 VERSN
REVDAT 1 08-APR-98 1A07 0
JRNL AUTH P.S.CHARIFSON,L.M.SHEWCHUK,W.ROCQUE,C.W.HUMMEL,S.R.JORDAN,
JRNL AUTH 2 C.MOHR,G.J.PACOFSKY,M.R.PEEL,M.RODRIGUEZ,D.D.STERNBACH,
JRNL AUTH 3 T.G.CONSLER
JRNL TITL PEPTIDE LIGANDS OF PP60(C-SRC) SH2 DOMAINS: A THERMODYNAMIC
JRNL TITL 2 AND STRUCTURAL STUDY.
JRNL REF BIOCHEMISTRY V. 36 6283 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9174343
JRNL DOI 10.1021/BI970019N
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.0
REMARK 3 NUMBER OF REFLECTIONS : 11141
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.30
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1725
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 3.128
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.09
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : UNRESTRAINED
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.MTY
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.MTY
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PARTIALLY REFINED
REMARK 4
REMARK 4 1A07 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-93
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 8.0
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 : SIEMENS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12012
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 41.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.12000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1SHD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 0.1 M
REMARK 280 MES, PH 6.5, 0.05 M CSCL, 30% JEFFAMINE M-600 AT 4 DEGREES C.,
REMARK 280 PH 8.0, 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 26.25000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.25000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.25000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.25000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.60000
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, 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 MET A 143
REMARK 465 ASP A 144
REMARK 465 MET B 143
REMARK 465 ASP B 144
REMARK 465 SER B 145
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 184 CG CD CE NZ
REMARK 470 ASP A 195 CG OD1 OD2
REMARK 470 ASN A 196 CG OD1 ND2
REMARK 470 ASP A 211 CG OD1 OD2
REMARK 470 SER A 212 OG
REMARK 470 PTR C 101 OH P O1P O2P O3P
REMARK 470 LYS B 155 CG CD CE NZ
REMARK 470 LYS B 184 CG CD CE NZ
REMARK 470 ASP B 195 CG OD1 OD2
REMARK 470 ASN B 196 CG OD1 ND2
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 ASP B 211 CG OD1 OD2
REMARK 470 PTR D 101 OH P O1P O2P O3P
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 HH TYR B 205 H1 HOH B 528 0.86
REMARK 500 H ILE B 217 H1 HOH B 514 0.94
REMARK 500 H HIS B 204 H2 HOH B 502 1.07
REMARK 500 HG1 THR A 183 HZ1 LYS A 206 1.07
REMARK 500 HH TYR B 233 H2 HOH B 514 1.10
REMARK 500 H VAL B 202 H1 HOH B 544 1.15
REMARK 500 H ILE A 217 H1 HOH A 509 1.22
REMARK 500 HG SER A 190 HD1 HIS A 204 1.22
REMARK 500 HH TYR A 233 H2 HOH A 509 1.27
REMARK 500 H LYS A 209 H1 HOH A 548 1.31
REMARK 500 H2 HOH B 513 H1 HOH B 533 1.34
REMARK 500 HH22 ARG B 158 O ACE D 100 1.55
REMARK 500
REMARK 500 REMARK: NULL
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 A 204 NE2 HIS A 204 CD2 -0.072
REMARK 500 HIS A 236 NE2 HIS A 236 CD2 -0.067
REMARK 500 HIS A 242 NE2 HIS A 242 CD2 -0.078
REMARK 500 ARG B 163 CZ ARG B 163 NH1 0.132
REMARK 500 ARG B 163 CZ ARG B 163 NH2 0.088
REMARK 500 HIS B 204 NE2 HIS B 204 CD2 -0.077
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 TRP A 151 CD1 - CG - CD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP A 151 CB - CG - CD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 TRP A 151 CE2 - CD2 - CG ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 158 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 178 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 CYS A 188 CB - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 CYS A 188 N - CA - CB ANGL. DEV. = -14.5 DEGREES
REMARK 500 TYR A 205 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 220 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TRP B 151 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP B 151 CB - CG - CD1 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TRP B 151 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 151 CG - CD2 - CE3 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 159 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 163 CD - NE - CZ ANGL. DEV. = -13.7 DEGREES
REMARK 500 TYR B 205 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 208 NE - CZ - NH2 ANGL. DEV. = -4.1 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 ASP A 238 53.49 36.74
REMARK 500 THR A 245 -61.51 -101.27
REMARK 500 LYS B 155 43.71 -104.66
REMARK 500 ASP B 238 56.80 37.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU B 160 -10.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE C 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE D 100
DBREF 1A07 A 144 249 UNP P12931 SRC_HUMAN 143 248
DBREF 1A07 B 144 249 UNP P12931 SRC_HUMAN 143 248
DBREF 1A07 C 100 103 PDB 1A07 1A07 100 103
DBREF 1A07 D 100 103 PDB 1A07 1A07 100 103
SEQRES 1 A 107 MET ASP SER ILE GLN ALA GLU GLU TRP TYR PHE GLY LYS
SEQRES 2 A 107 ILE THR ARG ARG GLU SER GLU ARG LEU LEU LEU ASN ALA
SEQRES 3 A 107 GLU ASN PRO ARG GLY THR PHE LEU VAL ARG GLU SER GLU
SEQRES 4 A 107 THR THR LYS GLY ALA TYR CYS LEU SER VAL SER ASP PHE
SEQRES 5 A 107 ASP ASN ALA LYS GLY LEU ASN VAL LYS HIS TYR LYS ILE
SEQRES 6 A 107 ARG LYS LEU ASP SER GLY GLY PHE TYR ILE THR SER ARG
SEQRES 7 A 107 THR GLN PHE ASN SER LEU GLN GLN LEU VAL ALA TYR TYR
SEQRES 8 A 107 SER LYS HIS ALA ASP GLY LEU CYS HIS ARG LEU THR THR
SEQRES 9 A 107 VAL CYS PRO
SEQRES 1 C 4 ACE PTR GLU DIP
SEQRES 1 B 107 MET ASP SER ILE GLN ALA GLU GLU TRP TYR PHE GLY LYS
SEQRES 2 B 107 ILE THR ARG ARG GLU SER GLU ARG LEU LEU LEU ASN ALA
SEQRES 3 B 107 GLU ASN PRO ARG GLY THR PHE LEU VAL ARG GLU SER GLU
SEQRES 4 B 107 THR THR LYS GLY ALA TYR CYS LEU SER VAL SER ASP PHE
SEQRES 5 B 107 ASP ASN ALA LYS GLY LEU ASN VAL LYS HIS TYR LYS ILE
SEQRES 6 B 107 ARG LYS LEU ASP SER GLY GLY PHE TYR ILE THR SER ARG
SEQRES 7 B 107 THR GLN PHE ASN SER LEU GLN GLN LEU VAL ALA TYR TYR
SEQRES 8 B 107 SER LYS HIS ALA ASP GLY LEU CYS HIS ARG LEU THR THR
SEQRES 9 B 107 VAL CYS PRO
SEQRES 1 D 4 ACE PTR GLU DIP
MODRES 1A07 PTR C 101 TYR O-PHOSPHOTYROSINE
MODRES 1A07 PTR D 101 TYR O-PHOSPHOTYROSINE
HET ACE C 100 3
HET PTR C 101 12
HET DIP C 103 11
HET ACE D 100 3
HET PTR D 101 12
HET DIP D 103 11
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM DIP DIPENTYLAMINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 ACE 2(C2 H4 O)
FORMUL 2 PTR 2(C9 H12 N O6 P)
FORMUL 2 DIP 2(C10 H23 N)
FORMUL 5 HOH *50(H2 O)
HELIX 1 1 ILE A 146 ALA A 148 5 3
HELIX 2 2 ARG A 158 LEU A 165 1 8
HELIX 3 3 LEU A 226 LYS A 235 1 10
HELIX 4 4 ARG B 158 LEU B 165 1 8
HELIX 5 5 LEU B 226 LYS B 235 1 10
SHEET 1 A 3 PHE A 175 GLU A 179 0
SHEET 2 A 3 TYR A 187 ASP A 195 -1 N SER A 190 O LEU A 176
SHEET 3 A 3 GLY A 199 ILE A 207 -1 N ILE A 207 O TYR A 187
SHEET 1 B 2 PHE A 215 THR A 218 0
SHEET 2 B 2 THR A 221 PHE A 223 -1 N PHE A 223 O PHE A 215
SHEET 1 C 3 PHE B 175 GLU B 179 0
SHEET 2 C 3 TYR B 187 ASP B 195 -1 N SER B 190 O LEU B 176
SHEET 3 C 3 GLY B 199 ILE B 207 -1 N ILE B 207 O TYR B 187
SHEET 1 D 2 PHE B 215 THR B 218 0
SHEET 2 D 2 THR B 221 PHE B 223 -1 N PHE B 223 O PHE B 215
LINK C ACE C 100 N PTR C 101 1555 1555 1.31
LINK C PTR C 101 N GLU C 102 1555 1555 1.32
LINK C GLU C 102 N DIP C 103 1555 1555 1.36
LINK C ACE D 100 N PTR D 101 1555 1555 1.33
LINK C PTR D 101 N GLU D 102 1555 1555 1.31
LINK C GLU D 102 N DIP D 103 1555 1555 1.36
SITE 1 AC1 2 ARG A 158 HOH C 501
SITE 1 AC2 1 HOH B 502
CRYST1 52.500 67.200 74.500 90.00 90.00 90.00 P 21 21 21 8
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 0.019048 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013423 0.00000
MTRIX1 1 -0.773100 0.287200 -0.565500 99.89480 1
MTRIX2 1 0.288900 0.953200 0.089100 -0.59030 1
MTRIX3 1 0.564700 -0.094500 -0.819900 29.96440 1
(ATOM LINES ARE NOT SHOWN.)
END