Header list of 1vj6.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE/SIGNALING PROTEIN 03-FEB-04 1VJ6
TITLE PDZ2 FROM PTP-BL IN COMPLEX WITH THE C-TERMINAL LIGAND FROM THE APC
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN-TYROSINE-PHOSPHATASE (NONRECEPTOR TYPE 13);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ2 DOMAIN;
COMPND 5 EC: 3.1.3.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ADENOMATOUS POLYPOSIS COLI PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: C-TERMINUS OF APC;
COMPND 11 SYNONYM: APC PROTEIN, MAPC;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTP-BL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS PROTEIN HAS BEEN CHEMICALLY SYNTHESIZED. IT IS
SOURCE 14 PRESENT IN MOUSE.
KEYWDS PDZ, COMPLEX, APC, PROTEIN-PROTEIN INTERACTION, PTP-BL, C-TERMINUS,
KEYWDS 2 HYDROLASE-SIGNALING PROTEIN COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR T.WALMA,G.W.VUISTER
REVDAT 5 02-MAR-22 1VJ6 1 REMARK SEQADV
REVDAT 4 09-JUN-09 1VJ6 1 REVDAT
REVDAT 3 24-FEB-09 1VJ6 1 VERSN
REVDAT 2 20-JAN-09 1VJ6 1 JRNL
REVDAT 1 01-NOV-05 1VJ6 0
JRNL AUTH S.GIANNI,T.WALMA,A.ARCOVITO,N.CALOSCI,A.BELLELLI,A.ENGSTROM,
JRNL AUTH 2 C.TRAVAGLINI-ALLOCATELLI,M.BRUNORI,P.JEMTH,G.W.VUISTER
JRNL TITL DEMONSTRATION OF LONG-RANGE INTERACTIONS IN A PDZ DOMAIN BY
JRNL TITL 2 NMR, KINETICS, AND PROTEIN ENGINEERING.
JRNL REF STRUCTURE V. 14 1801 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 17161370
JRNL DOI 10.1016/J.STR.2006.10.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2003, X-PLOR 3.851, CHARMM 22
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (X-PLOR), MACKERELL
REMARK 3 (CHARMM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 1470 DISTANCE RESTRAINTS (INTRA/SEQUENTIAL/MEDIUM/LONG/INTER)
REMARK 3 (529/323/166/378/74), 28 HYDROGEN BONDS, DIHEDRAL ANGLE RESTRAINTS
REMARK 3 (PHI/PSI/CHI) (69/72/13)
REMARK 4
REMARK 4 1VJ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021508.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM PDZ2 PROTEIN, U-15N,13C; 3MM
REMARK 210 APC PEPTIDE, UNLABELLED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : INITIAL CALCULATIONS WITH XPLOR
REMARK 210 VERSION 3.851, FOLLOWED BY
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210 PROTOCOL UNDER A CHARMM22
REMARK 210 FORCEFIELD.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 1-35
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 LYS B 199
REMARK 465 ARG B 200
REMARK 465 HIS B 201
REMARK 465 SER B 202
REMARK 465 GLY B 203
REMARK 465 SER B 204
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 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 38 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 TYR B 205 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 11 TYR B 205 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 12 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 12 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 13 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 14 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 15 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 15 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 17 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 SER A 24 N - CA - CB ANGL. DEV. = 9.8 DEGREES
REMARK 500 18 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 19 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 20 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 20 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 20 TYR B 205 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 20 TYR B 205 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 22 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 23 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 23 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 24 SER A 36 N - CA - CB ANGL. DEV. = 10.1 DEGREES
REMARK 500 24 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 25 PHE A 14 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 25 PHE A 14 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 25 TYR B 205 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 27 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 31 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 33 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 34 SER A 24 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 34 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 34 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 35 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.3 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 1 SER A 24 111.57 -178.24
REMARK 500 1 ARG A 38 43.85 -81.03
REMARK 500 1 PRO A 49 93.88 -69.04
REMARK 500 1 LYS A 50 53.32 82.57
REMARK 500 1 ASP A 56 -71.57 -70.74
REMARK 500 1 LYS A 61 45.45 -88.30
REMARK 500 1 LEU A 73 47.62 -81.08
REMARK 500 1 THR A 77 -164.92 -110.46
REMARK 500 1 ASN A 87 37.32 -90.88
REMARK 500 1 GLN A 90 -51.78 68.27
REMARK 500 1 LEU B 206 179.80 61.37
REMARK 500 1 VAL B 207 89.49 33.12
REMARK 500 2 ASP A 22 -18.82 66.50
REMARK 500 2 SER A 24 119.64 -179.97
REMARK 500 2 HIS A 39 31.00 30.64
REMARK 500 2 PRO A 49 96.57 -59.18
REMARK 500 2 ASP A 56 -70.52 -72.69
REMARK 500 2 LEU A 73 30.74 -87.93
REMARK 500 2 THR A 77 -161.59 -108.73
REMARK 500 2 ASN A 87 43.03 -84.59
REMARK 500 2 VAL B 207 98.83 61.92
REMARK 500 3 GLU A 15 68.49 -115.21
REMARK 500 3 SER A 24 99.62 167.97
REMARK 500 3 SER A 36 87.62 96.04
REMARK 500 3 VAL A 37 -156.55 -119.75
REMARK 500 3 HIS A 39 -80.05 71.80
REMARK 500 3 LYS A 50 70.72 50.50
REMARK 500 3 ASP A 56 -96.98 -73.69
REMARK 500 3 LEU A 73 49.95 -80.71
REMARK 500 3 ASN A 87 37.75 -91.63
REMARK 500 3 GLN A 90 -57.70 -137.75
REMARK 500 3 LEU B 206 -148.69 54.73
REMARK 500 3 VAL B 207 94.21 38.22
REMARK 500 4 SER A 24 99.01 -172.75
REMARK 500 4 SER A 36 -21.02 85.74
REMARK 500 4 HIS A 39 5.18 -165.83
REMARK 500 4 LYS A 50 45.76 152.29
REMARK 500 4 ASP A 56 -79.35 -62.18
REMARK 500 4 ASN A 69 18.97 52.61
REMARK 500 4 LEU A 73 43.88 -82.16
REMARK 500 4 ASN A 87 52.23 -92.19
REMARK 500 4 GLN A 90 -60.21 -150.60
REMARK 500 4 LEU B 206 -149.57 -149.53
REMARK 500 4 VAL B 207 104.68 67.79
REMARK 500 5 SER A 24 108.59 -177.54
REMARK 500 5 VAL A 37 54.25 -146.21
REMARK 500 5 ARG A 38 -72.41 70.73
REMARK 500 5 HIS A 39 -85.25 -138.23
REMARK 500 5 LYS A 50 -87.12 -117.28
REMARK 500 5 ALA A 52 -77.07 -109.46
REMARK 500
REMARK 500 THIS ENTRY HAS 397 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 ASP A 63 ARG A 64 6 149.10
REMARK 500 GLY A 99 GLN A 100 14 149.07
REMARK 500 SER A 55 ASP A 56 15 149.58
REMARK 500 PRO A 10 GLY A 11 16 -149.63
REMARK 500 LYS A 50 GLY A 51 16 148.51
REMARK 500 SER A 55 ASP A 56 23 149.95
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 2 ARG A 58 0.08 SIDE CHAIN
REMARK 500 3 ARG A 38 0.11 SIDE CHAIN
REMARK 500 4 ARG A 58 0.10 SIDE CHAIN
REMARK 500 5 ARG A 38 0.10 SIDE CHAIN
REMARK 500 5 ARG A 64 0.12 SIDE CHAIN
REMARK 500 6 ARG A 64 0.10 SIDE CHAIN
REMARK 500 8 ARG A 38 0.09 SIDE CHAIN
REMARK 500 8 TYR A 43 0.07 SIDE CHAIN
REMARK 500 9 ARG A 86 0.08 SIDE CHAIN
REMARK 500 11 ARG A 38 0.09 SIDE CHAIN
REMARK 500 11 ARG A 58 0.12 SIDE CHAIN
REMARK 500 13 ARG A 86 0.15 SIDE CHAIN
REMARK 500 16 ARG A 58 0.11 SIDE CHAIN
REMARK 500 17 ARG A 64 0.09 SIDE CHAIN
REMARK 500 20 ARG A 38 0.09 SIDE CHAIN
REMARK 500 20 ARG A 86 0.10 SIDE CHAIN
REMARK 500 21 ARG A 38 0.08 SIDE CHAIN
REMARK 500 21 ARG A 58 0.19 SIDE CHAIN
REMARK 500 25 ARG A 64 0.10 SIDE CHAIN
REMARK 500 25 ARG A 86 0.11 SIDE CHAIN
REMARK 500 26 ARG A 64 0.10 SIDE CHAIN
REMARK 500 26 ARG A 86 0.12 SIDE CHAIN
REMARK 500 27 ARG A 64 0.09 SIDE CHAIN
REMARK 500 28 ARG A 38 0.10 SIDE CHAIN
REMARK 500 28 ARG A 58 0.09 SIDE CHAIN
REMARK 500 28 TYR B 205 0.07 SIDE CHAIN
REMARK 500 29 TYR A 43 0.10 SIDE CHAIN
REMARK 500 29 ARG A 58 0.10 SIDE CHAIN
REMARK 500 30 ARG A 38 0.17 SIDE CHAIN
REMARK 500 30 ARG A 58 0.08 SIDE CHAIN
REMARK 500 30 ARG A 64 0.12 SIDE CHAIN
REMARK 500 31 ARG A 58 0.15 SIDE CHAIN
REMARK 500 32 ARG A 38 0.14 SIDE CHAIN
REMARK 500 32 ARG A 86 0.08 SIDE CHAIN
REMARK 500 33 ARG A 58 0.16 SIDE CHAIN
REMARK 500 34 ARG A 86 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6060 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS OF PDZ2-APC COMPLEX
REMARK 900 RELATED ID: 5131 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS OF FREE PDZ2 PROTEIN
REMARK 900 RELATED ID: 1GM1 RELATED DB: PDB
REMARK 900 STRUCTURE OF FREE PDZ2 PROTEIN
REMARK 900 RELATED ID: 1OZI RELATED DB: PDB
REMARK 900 STRUCTURE OF ALTERNATIVELY SPLICED PDZ2
DBREF 1VJ6 A 9 102 UNP Q64512 PTN13_MOUSE 1350 1443
DBREF 1VJ6 B 199 210 UNP Q61315 APC_MOUSE 2834 2845
SEQADV 1VJ6 MET A 1 UNP Q64512 CLONING ARTIFACT
SEQADV 1VJ6 HIS A 2 UNP Q64512 EXPRESSION TAG
SEQADV 1VJ6 HIS A 3 UNP Q64512 EXPRESSION TAG
SEQADV 1VJ6 HIS A 4 UNP Q64512 EXPRESSION TAG
SEQADV 1VJ6 HIS A 5 UNP Q64512 EXPRESSION TAG
SEQADV 1VJ6 HIS A 6 UNP Q64512 EXPRESSION TAG
SEQADV 1VJ6 HIS A 7 UNP Q64512 EXPRESSION TAG
SEQADV 1VJ6 MET A 8 UNP Q64512 CLONING ARTIFACT
SEQRES 1 A 102 MET HIS HIS HIS HIS HIS HIS MET LYS PRO GLY ASP THR
SEQRES 2 A 102 PHE GLU VAL GLU LEU ALA LYS THR ASP GLY SER LEU GLY
SEQRES 3 A 102 ILE SER VAL THR GLY GLY VAL ASN THR SER VAL ARG HIS
SEQRES 4 A 102 GLY GLY ILE TYR VAL LYS ALA ILE ILE PRO LYS GLY ALA
SEQRES 5 A 102 ALA GLU SER ASP GLY ARG ILE HIS LYS GLY ASP ARG VAL
SEQRES 6 A 102 LEU ALA VAL ASN GLY VAL SER LEU GLU GLY ALA THR HIS
SEQRES 7 A 102 LYS GLN ALA VAL GLU THR LEU ARG ASN THR GLY GLN VAL
SEQRES 8 A 102 VAL HIS LEU LEU LEU GLU LYS GLY GLN VAL PRO
SEQRES 1 B 12 LYS ARG HIS SER GLY SER TYR LEU VAL THR SER VAL
HELIX 1 1 GLY A 51 GLY A 57 1 7
HELIX 2 2 THR A 77 ASN A 87 1 11
SHEET 1 A 4 THR A 13 ALA A 19 0
SHEET 2 A 4 VAL A 91 GLU A 97 -1 O LEU A 94 N VAL A 16
SHEET 3 A 4 ARG A 64 VAL A 68 -1 N ARG A 64 O GLU A 97
SHEET 4 A 4 VAL A 71 SER A 72 -1 O VAL A 71 N VAL A 68
SHEET 1 B 6 THR A 13 ALA A 19 0
SHEET 2 B 6 VAL A 91 GLU A 97 -1 O LEU A 94 N VAL A 16
SHEET 3 B 6 ARG A 64 VAL A 68 -1 N ARG A 64 O GLU A 97
SHEET 4 B 6 ILE A 42 ILE A 47 -1 N ILE A 42 O VAL A 65
SHEET 5 B 6 ILE A 27 GLY A 31 -1 N SER A 28 O LYS A 45
SHEET 6 B 6 SER B 209 VAL B 210 -1 O VAL B 210 N ILE A 27
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 - r 2 2 Bytes