HEADER TRANSFORMING PROTEIN 02-MAY-97 1BKM
TITLE COCRYSTAL STRUCTURE OF D-AMINO ACID SUBSTITUTED PHOSPHOPEPTIDE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PP60 V-SRC TYROSINE KINASE TRANSFORMING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN;
COMPND 5 SYNONYM: SRC SH2;
COMPND 6 EC: 2.7.1.112;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ROUS SARCOMA VIRUS;
SOURCE 3 ORGANISM_TAXID: 11886;
SOURCE 4 STRAIN: SCHMIDT-RUPPIN STRAIN A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM83
KEYWDS V-SRC SH2 DOMAIN, PHOSPHOTYROSINE RECOGNITION DOMAIN, PP60 SRC SH2
KEYWDS 2 DOMAIN, TRIPEPTIDE, D-AMINO ACID, TRANSFORMING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.HOLLAND,J.R.RUBIN
REVDAT 4 02-AUG-23 1BKM 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1BKM 1 VERSN
REVDAT 2 14-DEC-04 1BKM 1 JRNL
REVDAT 1 07-JUL-97 1BKM 0
JRNL AUTH D.R.HOLLAND,E.A.LUNNEY,M.S.PLUMMER,W.T.MUELLER,P.MCCONNELL,
JRNL AUTH 2 A.PAVLOVSKY,K.S.PARA,A.SHAHRIPOUR,C.HUMBLET,T.K.SAWYER,
JRNL AUTH 3 J.R.RUBIN
JRNL TITL STRUCTURE-BASED DESIGN OF A NOVEL SERIES OF NONPEPTIDE
JRNL TITL 2 LIGANDS THAT BIND TO THE PP60SRC SH2 DOMAIN
JRNL REF J.AM.CHEM.SOC. V. 119 12471 1997
JRNL REFN ISSN 0002-7863
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.WAKSMAN,S.E.SHOELSON,N.PANT,D.COWBURN,J.KURIYAN
REMARK 1 TITL BINDING OF A HIGH AFFINITY PHOSPHOTYROSYL PEPTIDE TO THE SRC
REMARK 1 TITL 2 SH2 DOMAIN: CRYSTAL STRUCTURES OF THE COMPLEXED AND
REMARK 1 TITL 3 PEPTIDE-FREE FORMS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 72 779 1993
REMARK 1 REFN ISSN 0092-8674
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 5528
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : R-FREE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 546
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 50.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 387
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37
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 : 812
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
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) : 3.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 29.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.700
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 : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BKM 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_1000171864.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-94
REMARK 200 TEMPERATURE (KELVIN) : 293
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 : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : CU FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6768
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.31700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
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: PROTEIN MODEL FROM 1SPS
REMARK 200
REMARK 200 REMARK: WAKSMAN AND KURIYAN SRC SH2 STRUCTURE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 6K, 0.1M TRIS, PH 8, SITTING
REMARK 280 DROP EXPERIMENT, PROTEIN 50 MG/ML, INHIBITOR 4 MG/ML, 4:4:2
REMARK 280 RATIO (WELL:PROT:INHIB), PH 8.0, VAPOR DIFFUSION - SITTING DROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP
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 15.10000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.26000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.26000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 15.10000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.45000
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: 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 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 GLY A 0
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 SER A 105
REMARK 465 LYS A 106
REMARK 465 GLU A 107
REMARK 465 PHE A 108
REMARK 465 ILE A 109
REMARK 465 VAL A 110
REMARK 465 THR A 111
REMARK 465 ASP A 112
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 GLU A 3 CB CG CD OE1 OE2
REMARK 470 GLU A 4 CG CD OE1 OE2
REMARK 470 TYR A 6 OH
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 CZ ARG A 13 H1 HOH A 140 0.80
REMARK 500 HG1 THR A 11 H GLU A 14 1.03
REMARK 500 OG1 THR A 11 H GLU A 14 1.16
REMARK 500 NH2 ARG A 13 H1 HOH A 140 1.18
REMARK 500 HE ARG A 13 H2 HOH A 140 1.27
REMARK 500 HH21 ARG A 13 O HOH A 140 1.34
REMARK 500 NE ARG A 13 H1 HOH A 140 1.39
REMARK 500 O ARG A 12 HG SER A 15 1.41
REMARK 500 HH21 ARG A 13 OE1 GLU A 14 1.46
REMARK 500 NH2 ARG A 13 OE1 GLU A 14 1.49
REMARK 500 HE ARG A 13 O HOH A 140 1.55
REMARK 500 NH2 ARG A 13 O HOH A 140 1.63
REMARK 500 CZ ARG A 13 O HOH A 140 1.69
REMARK 500 NE ARG A 13 O HOH A 140 1.75
REMARK 500 OG1 THR A 11 N GLU A 14 2.04
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 THR A 11 CB - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 THR A 11 CA - CB - OG1 ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR A 11 CA - CB - CG2 ANGL. DEV. = -19.8 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 13 NE - CZ - NH1 ANGL. DEV. = -15.6 DEGREES
REMARK 500 ARG A 13 NE - CZ - NH2 ANGL. DEV. = 13.5 DEGREES
REMARK 500 GLU A 14 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 GLU A 14 CG - CD - OE1 ANGL. DEV. = 13.3 DEGREES
REMARK 500 GLU A 14 CG - CD - OE2 ANGL. DEV. = -14.8 DEGREES
REMARK 500 LEU A 30 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 TYR A 87 CB - CG - CD1 ANGL. DEV. = -3.6 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 LYS A 9 39.12 -90.49
REMARK 500 THR A 99 -103.88 -120.80
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 TYR A 41 0.08 SIDE CHAIN
REMARK 500 TYR A 70 0.07 SIDE CHAIN
REMARK 500 ARG A 97 0.09 SIDE CHAIN
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 1C5 A 113
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 G-S ARE NOT NATURAL SEQUENCE - BYPRODUCT OF CLONING
REMARK 999 E-F-I-V-T-D NOT NATURAL SEQUENCE - BYPRODUCT OF CLONING
DBREF 1BKM A 2 106 UNP P00524 SRC_RSVSA 145 249
SEQADV 1BKM ALA A 17 UNP P00524 ARG 160 CONFLICT
SEQRES 1 A 113 GLY SER ALA GLU GLU TRP TYR PHE GLY LYS ILE THR ARG
SEQRES 2 A 113 ARG GLU SER GLU ALA LEU LEU LEU ASN PRO GLU ASN PRO
SEQRES 3 A 113 ARG GLY THR PHE LEU VAL ARG GLU SER GLU THR THR LYS
SEQRES 4 A 113 GLY ALA TYR CYS LEU SER VAL SER ASP PHE ASP ASN ALA
SEQRES 5 A 113 LYS GLY LEU ASN VAL LYS HIS TYR LYS ILE ARG LYS LEU
SEQRES 6 A 113 ASP SER GLY GLY PHE TYR ILE THR SER ARG THR GLN PHE
SEQRES 7 A 113 SER SER LEU GLN GLN LEU VAL ALA TYR TYR SER LYS HIS
SEQRES 8 A 113 ALA ASP GLY LEU CYS HIS ARG LEU THR ASN VAL CYS PRO
SEQRES 9 A 113 THR SER LYS GLU PHE ILE VAL THR ASP
HET 1C5 A 113 47
HETNAM 1C5 [[O-PHOSPHONO-N-ACETYL-TYROSINYL]-GLUTAMYL-
HETNAM 2 1C5 3[CYCLOHEXYLMETHYL]ALANINYL]-AMINE
FORMUL 2 1C5 C26 H39 N4 O10 P
FORMUL 3 HOH *61(H2 O)
HELIX 1 1 ARG A 12 LEU A 19 1 8
HELIX 2 2 LEU A 80 LYS A 89 1 10
SHEET 1 A 3 PHE A 29 GLU A 33 0
SHEET 2 A 3 TYR A 41 ASP A 49 -1 N SER A 44 O LEU A 30
SHEET 3 A 3 GLY A 53 ILE A 61 -1 N ILE A 61 O TYR A 41
CISPEP 1 GLU A 4 TRP A 5 0 4.90
SITE 1 AC1 16 ARG A 12 ARG A 32 SER A 34 GLU A 35
SITE 2 AC1 16 THR A 36 CYS A 42 HIS A 58 TYR A 59
SITE 3 AC1 16 LYS A 60 THR A 72 LYS A 89 GLY A 93
SITE 4 AC1 16 HOH A 117 HOH A 118 HOH A 119 HOH A 127
CRYST1 30.200 46.900 74.520 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 0.033113 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021322 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013419 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
