Header list of 1rgr.pdb file
Complete list - t 27 2 Bytes
HEADER STRUCTURAL PROTEIN/DE NOVO PROTEIN 12-NOV-03 1RGR
TITLE CYCLIC PEPTIDES TARGETING PDZ DOMAINS OF PSD-95: STRUCTURAL BASIS FOR
TITLE 2 ENHANCED AFFINITY AND ENZYMATIC STABILITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRESYNAPTIC DENSITY PROTEIN 95;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ1 DOMAIN OF PSD-95;
COMPND 5 SYNONYM: PSD-95, DISCS, LARGE HOMOLOG 4, POSTSYNAPTIC DENSITY-95;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: POSTSYNAPTIC PROTEIN CRIPT PEPTIDE;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: C-TERMINUS;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES;
COMPND 13 OTHER_DETAILS: BETA-ALANINE LINKS RESIDUES 3 TO 5 TO FORM A CYCLIC
COMPND 14 PEPTIDE.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: DLG4, PSD95;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS PDZ1 DOMAIN, STRUCTURAL PROTEIN-DE NOVO PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR A.PISERCHIO,G.D.SALINAS,T.LI,J.MARSHALL,M.R.SPALLER,D.F.MIERKE
REVDAT 4 27-OCT-21 1RGR 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1RGR 1 VERSN
REVDAT 2 24-FEB-09 1RGR 1 VERSN
REVDAT 1 18-MAY-04 1RGR 0
JRNL AUTH A.PISERCHIO,G.D.SALINAS,T.LI,J.MARSHALL,M.R.SPALLER,
JRNL AUTH 2 D.F.MIERKE
JRNL TITL TARGETING SPECIFIC PDZ DOMAINS OF PSD-95; STRUCTURAL BASIS
JRNL TITL 2 FOR ENHANCED AFFINITY AND ENZYMATIC STABILITY OF A CYCLIC
JRNL TITL 3 PEPTIDE.
JRNL REF CHEM.BIOL. V. 11 469 2004
JRNL REFN ISSN 1074-5521
JRNL PMID 15123241
JRNL DOI 10.1016/J.CHEMBIOL.2004.03.013
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RGR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020731.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1MM PZ1 U-15N,13C, 3MM PEPTIDE,
REMARK 210 10 MM PHOSPATE BUFFER 150 MM
REMARK 210 NACL, PH 6.8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 CARTESIAN MD IN WATER
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-22
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 155
REMARK 465 HIS A 156
REMARK 465 HIS A 157
REMARK 465 HIS A 158
REMARK 465 HIS A 159
REMARK 465 HIS A 160
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
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 1 HIS A 87 CG HIS A 87 CD2 0.055
REMARK 500 2 HIS A 130 CG HIS A 130 CD2 0.055
REMARK 500 3 HIS A 87 CG HIS A 87 CD2 0.058
REMARK 500 4 HIS A 87 CG HIS A 87 CD2 0.055
REMARK 500 5 HIS A 87 CG HIS A 87 CD2 0.054
REMARK 500 6 HIS A 87 CG HIS A 87 CD2 0.055
REMARK 500 8 HIS A 87 CG HIS A 87 CD2 0.058
REMARK 500 9 HIS A 87 CG HIS A 87 CD2 0.057
REMARK 500 10 HIS A 87 CG HIS A 87 CD2 0.056
REMARK 500 13 HIS A 87 CG HIS A 87 CD2 0.055
REMARK 500 13 HIS A 130 CG HIS A 130 CD2 0.056
REMARK 500 14 HIS A 130 CG HIS A 130 CD2 0.054
REMARK 500 15 HIS A 87 CG HIS A 87 CD2 0.056
REMARK 500 16 HIS A 87 CG HIS A 87 CD2 0.057
REMARK 500 19 HIS A 87 CG HIS A 87 CD2 0.057
REMARK 500 20 HIS A 87 CG HIS A 87 CD2 0.057
REMARK 500 21 HIS A 87 CG HIS A 87 CD2 0.056
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 1 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 HIS A 87 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 1 ARG A 110 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 1 ARG A 126 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 1 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 110 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 VAL A 113 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 2 HIS A 130 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 2 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 3 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 HIS A 87 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 3 ARG A 110 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 HIS A 130 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 3 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 VAL B 6 CA - CB - CG1 ANGL. DEV. = 11.5 DEGREES
REMARK 500 4 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 PRO A 92 N - CA - CB ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 ARG A 110 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 HIS A 130 ND1 - CE1 - NE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 4 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 4 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 5 ARG A 110 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 HIS A 130 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 5 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG A 150 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 HIS A 87 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 6 PRO A 92 N - CA - CB ANGL. DEV. = -7.4 DEGREES
REMARK 500 6 ARG A 110 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 6 ARG A 112 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 VAL A 113 CA - CB - CG2 ANGL. DEV. = 9.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 191 ANGLE DEVIATIONS.
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 ASN A 72 -71.42 -61.41
REMARK 500 1 LEU A 75 -86.88 -76.50
REMARK 500 1 ASP A 91 89.89 -155.50
REMARK 500 1 ARG A 110 59.94 -164.88
REMARK 500 1 LEU A 111 -164.06 -79.23
REMARK 500 1 ASN A 114 -18.34 -39.54
REMARK 500 1 ASP A 115 99.71 -34.92
REMARK 500 1 ILE A 117 104.07 -57.93
REMARK 500 1 ASN A 121 -78.89 77.70
REMARK 500 1 GLU A 122 -12.94 -159.50
REMARK 500 1 VAL A 125 -142.49 -97.11
REMARK 500 1 ARG A 126 -83.66 71.82
REMARK 500 2 ASN A 72 -85.22 -166.39
REMARK 500 2 ASN A 85 87.84 -163.27
REMARK 500 2 ASP A 91 -88.14 92.59
REMARK 500 2 ARG A 112 -146.94 -74.41
REMARK 500 2 VAL A 113 -76.48 -37.31
REMARK 500 2 ASN A 114 -16.16 -160.72
REMARK 500 2 ASP A 115 -84.69 74.27
REMARK 500 2 ASN A 121 -80.65 80.88
REMARK 500 2 GLU A 122 -17.37 -163.69
REMARK 500 2 VAL A 125 -106.19 -87.03
REMARK 500 2 ARG A 126 -88.87 52.04
REMARK 500 2 ALA A 140 -6.75 -57.71
REMARK 500 3 LEU A 75 -85.43 -79.12
REMARK 500 3 ASN A 85 82.00 -150.31
REMARK 500 3 ASP A 91 -81.88 100.79
REMARK 500 3 ARG A 110 73.67 -173.82
REMARK 500 3 LEU A 111 -166.70 -104.34
REMARK 500 3 ASN A 114 85.77 -33.48
REMARK 500 3 ASN A 121 -74.65 79.83
REMARK 500 3 GLU A 122 -16.74 -167.54
REMARK 500 3 VAL A 125 -101.19 -95.93
REMARK 500 3 ARG A 126 -90.89 50.97
REMARK 500 3 SER A 142 -5.09 -59.83
REMARK 500 4 ASN A 72 -100.67 -154.43
REMARK 500 4 ASP A 91 -85.32 91.57
REMARK 500 4 PRO A 92 -139.60 -108.39
REMARK 500 4 SER A 93 106.87 78.30
REMARK 500 4 ASN A 114 68.95 -55.30
REMARK 500 4 ASN A 121 -74.45 79.67
REMARK 500 4 GLU A 122 -10.88 -164.49
REMARK 500 4 VAL A 125 -96.86 -96.97
REMARK 500 4 ARG A 126 -89.37 46.79
REMARK 500 5 ARG A 70 -102.73 -116.22
REMARK 500 5 ASN A 85 69.74 -155.17
REMARK 500 5 ASP A 91 88.38 -154.51
REMARK 500 5 PRO A 92 96.10 -62.61
REMARK 500 5 ARG A 112 129.30 65.01
REMARK 500 5 VAL A 113 -71.09 -46.80
REMARK 500
REMARK 500 THIS ENTRY HAS 255 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 ALA A 80 GLY A 81 1 -149.00
REMARK 500 ALA A 80 GLY A 81 2 -137.05
REMARK 500 ALA A 80 GLY A 81 3 -142.78
REMARK 500 HIS A 87 ILE A 88 3 -148.32
REMARK 500 ALA A 80 GLY A 81 4 -136.38
REMARK 500 ALA A 80 GLY A 81 5 -142.71
REMARK 500 ALA A 80 GLY A 81 6 -136.52
REMARK 500 ALA A 80 GLY A 81 7 -141.80
REMARK 500 ALA A 80 GLY A 81 8 -146.42
REMARK 500 ALA A 80 GLY A 81 9 -138.84
REMARK 500 ALA A 80 GLY A 81 10 -145.24
REMARK 500 ALA A 80 GLY A 81 11 -137.56
REMARK 500 ALA A 80 GLY A 81 12 -141.02
REMARK 500 PHE A 95 ILE A 96 12 149.81
REMARK 500 ALA A 80 GLY A 81 13 -140.61
REMARK 500 ALA A 80 GLY A 81 14 -140.10
REMARK 500 ARG A 112 VAL A 113 14 146.81
REMARK 500 ALA A 80 GLY A 81 15 -140.50
REMARK 500 ALA A 80 GLY A 81 16 -143.58
REMARK 500 ALA A 80 GLY A 81 17 -136.81
REMARK 500 VAL A 128 THR A 129 17 149.48
REMARK 500 ALA A 80 GLY A 81 18 -138.32
REMARK 500 ARG A 112 VAL A 113 18 146.82
REMARK 500 ALA A 80 GLY A 81 19 -144.96
REMARK 500 HIS A 87 ILE A 88 19 -147.77
REMARK 500 PHE A 95 ILE A 96 19 148.36
REMARK 500 ALA A 80 GLY A 81 20 -142.98
REMARK 500 HIS A 87 ILE A 88 20 -147.79
REMARK 500 ALA A 80 GLY A 81 21 -143.41
REMARK 500 ALA A 80 GLY A 81 22 -145.78
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 HIS A 130 0.10 SIDE CHAIN
REMARK 500 1 ARG A 150 0.08 SIDE CHAIN
REMARK 500 2 HIS A 130 0.10 SIDE CHAIN
REMARK 500 3 HIS A 130 0.08 SIDE CHAIN
REMARK 500 5 TYR B 1 0.07 SIDE CHAIN
REMARK 500 7 HIS A 130 0.08 SIDE CHAIN
REMARK 500 11 HIS A 130 0.08 SIDE CHAIN
REMARK 500 13 TYR A 63 0.06 SIDE CHAIN
REMARK 500 14 TYR B 1 0.06 SIDE CHAIN
REMARK 500 15 HIS A 130 0.10 SIDE CHAIN
REMARK 500 16 HIS A 130 0.08 SIDE CHAIN
REMARK 500 20 ARG A 70 0.10 SIDE CHAIN
REMARK 500 21 HIS A 130 0.09 SIDE CHAIN
REMARK 500 22 HIS A 130 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 BAL B 7
DBREF 1RGR A 62 154 UNP P31016 DLG4_RAT 62 154
DBREF 1RGR B 1 6 GB 3098551 AAC40102 552 557
SEQADV 1RGR HIS A 155 UNP P31016 EXPRESSION TAG
SEQADV 1RGR HIS A 156 UNP P31016 EXPRESSION TAG
SEQADV 1RGR HIS A 157 UNP P31016 EXPRESSION TAG
SEQADV 1RGR HIS A 158 UNP P31016 EXPRESSION TAG
SEQADV 1RGR HIS A 159 UNP P31016 EXPRESSION TAG
SEQADV 1RGR HIS A 160 UNP P31016 EXPRESSION TAG
SEQADV 1RGR LYS B 3 GB 3098551 GLN 98 ENGINEERED MUTATION
SEQADV 1RGR GLU B 5 GB 3098551 SER 100 ENGINEERED MUTATION
SEQRES 1 A 99 GLU TYR GLU GLU ILE THR LEU GLU ARG GLY ASN SER GLY
SEQRES 2 A 99 LEU GLY PHE SER ILE ALA GLY GLY THR ASP ASN PRO HIS
SEQRES 3 A 99 ILE GLY ASP ASP PRO SER ILE PHE ILE THR LYS ILE ILE
SEQRES 4 A 99 PRO GLY GLY ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL
SEQRES 5 A 99 ASN ASP SER ILE LEU PHE VAL ASN GLU VAL ASP VAL ARG
SEQRES 6 A 99 GLU VAL THR HIS SER ALA ALA VAL GLU ALA LEU LYS GLU
SEQRES 7 A 99 ALA GLY SER ILE VAL ARG LEU TYR VAL MET ARG ARG LYS
SEQRES 8 A 99 PRO PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 B 6 TYR LYS LYS THR GLU VAL
HET BAL B 7 10
HETNAM BAL BETA-ALANINE
FORMUL 3 BAL C3 H7 N O2
HELIX 1 1 GLY A 103 GLY A 109 1 7
HELIX 2 2 THR A 129 ALA A 140 1 12
SHEET 1 A 4 TYR A 63 GLU A 69 0
SHEET 2 A 4 ILE A 143 MET A 149 -1 O LEU A 146 N ILE A 66
SHEET 3 A 4 SER A 116 VAL A 120 -1 N PHE A 119 O TYR A 147
SHEET 4 A 4 VAL A 123 ASP A 124 -1 N VAL A 123 O VAL A 120
SHEET 1 B 3 ILE A 96 ILE A 99 0
SHEET 2 B 3 PHE A 77 ILE A 79 -1 N SER A 78 O LYS A 98
SHEET 3 B 3 THR B 4 VAL B 6 -1 O VAL B 6 N PHE A 77
LINK NZ LYS B 3 C BAL B 7 1555 1555 1.34
LINK CD GLU B 5 N BAL B 7 1555 1555 1.34
SITE 1 AC1 4 SER A 78 LYS A 98 LYS B 3 GLU B 5
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
Complete list - t 27 2 Bytes