HEADER CELL ADHESION 04-MAR-03 1OP4
TITLE SOLUTION STRUCTURE OF NEURAL CADHERIN PRODOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURAL-CADHERIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: N-CADHERIN, CADHERIN-2;
COMPND 5 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: CDH2;
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: PET-19B
KEYWDS BETA SANDWICH, CADHERIN-LIKE DOMAIN, CELL ADHESION
EXPDTA SOLUTION NMR
AUTHOR A.W.KOCH,A.FAROOQ,W.SHAN,L.ZENG,D.R.COLMAN,M.-M.ZHOU
REVDAT 4 23-FEB-22 1OP4 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1OP4 1 VERSN
REVDAT 2 25-MAY-04 1OP4 1 JRNL
REVDAT 1 16-MAR-04 1OP4 0
JRNL AUTH A.W.KOCH,A.FAROOQ,W.SHAN,L.ZENG,D.R.COLMAN,M.-M.ZHOU
JRNL TITL STRUCTURE OF THE NEURAL (N-) CADHERIN PRODOMAIN REVEALS A
JRNL TITL 2 CADHERIN EXTRACELLULAR DOMAIN-LIKE FOLD WITHOUT ADHESIVE
JRNL TITL 3 CHARACTERISTICS
JRNL REF STRUCTURE V. 12 793 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15130472
JRNL DOI 10.1016/J.STR.2004.02.034
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018527.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM N-CADHERIN PRODOMAIN
REMARK 210 (15N,13C), 50MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR, XWINNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY 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 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 SER A 12
REMARK 465 SER A 13
REMARK 465 GLY A 14
REMARK 465 HIS A 15
REMARK 465 ILE A 16
REMARK 465 ASP A 17
REMARK 465 ASP A 18
REMARK 465 ASP A 19
REMARK 465 ASP A 20
REMARK 465 LYS A 21
REMARK 465 HIS A 22
REMARK 465 MET A 23
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 O ASP A 82 H GLY A 85 1.59
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 ALA A 25 31.52 -170.28
REMARK 500 GLU A 28 -78.77 -133.08
REMARK 500 ALA A 30 19.00 -150.75
REMARK 500 PRO A 37 33.70 -86.81
REMARK 500 ASP A 39 -159.21 -132.22
REMARK 500 PRO A 54 175.84 -54.18
REMARK 500 CYS A 63 -178.09 -174.11
REMARK 500 ASN A 64 -144.50 53.12
REMARK 500 LYS A 66 115.25 57.79
REMARK 500 ARG A 67 70.43 -156.91
REMARK 500 SER A 74 35.73 -159.35
REMARK 500 ALA A 77 -156.23 -61.32
REMARK 500 ARG A 91 135.38 61.52
REMARK 500 SER A 92 64.70 -108.59
REMARK 500 LEU A 95 71.91 51.60
REMARK 500 THR A 96 -80.59 -161.22
REMARK 500 GLU A 124 66.08 -117.53
REMARK 500 MET A 132 -67.42 -94.07
REMARK 500 GLU A 134 62.79 -161.87
REMARK 500 GLU A 137 34.16 -154.30
REMARK 500 ILE A 141 -67.69 -95.64
REMARK 500 PHE A 143 85.16 52.58
REMARK 500 PRO A 144 175.94 -57.04
REMARK 500 ARG A 145 54.53 -141.75
REMARK 500 LEU A 147 57.86 -154.02
REMARK 500 ARG A 156 20.78 -150.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OP4 A 24 159 UNP P15116 CADH2_MOUSE 24 159
SEQADV 1OP4 GLY A 1 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 2 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 3 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 4 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 5 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 6 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 7 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 8 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 9 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 10 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 11 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 SER A 12 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 SER A 13 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 GLY A 14 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 15 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 ILE A 16 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 ASP A 17 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 ASP A 18 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 ASP A 19 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 ASP A 20 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 LYS A 21 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 HIS A 22 UNP P15116 EXPRESSION TAG
SEQADV 1OP4 MET A 23 UNP P15116 EXPRESSION TAG
SEQRES 1 A 159 GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 A 159 GLY HIS ILE ASP ASP ASP ASP LYS HIS MET GLU ALA SER
SEQRES 3 A 159 GLY GLU ILE ALA LEU CYS LYS THR GLY PHE PRO GLU ASP
SEQRES 4 A 159 VAL TYR SER ALA VAL LEU PRO LYS ASP VAL HIS GLU GLY
SEQRES 5 A 159 GLN PRO LEU LEU ASN VAL LYS PHE SER ASN CYS ASN ARG
SEQRES 6 A 159 LYS ARG LYS VAL GLN TYR GLU SER SER GLU PRO ALA ASP
SEQRES 7 A 159 PHE LYS VAL ASP GLU ASP GLY THR VAL TYR ALA VAL ARG
SEQRES 8 A 159 SER PHE PRO LEU THR ALA GLU GLN ALA LYS PHE LEU ILE
SEQRES 9 A 159 TYR ALA GLN ASP LYS GLU THR GLN GLU LYS TRP GLN VAL
SEQRES 10 A 159 ALA VAL ASN LEU SER ARG GLU PRO THR LEU THR GLU GLU
SEQRES 11 A 159 PRO MET LYS GLU PRO HIS GLU ILE GLU GLU ILE VAL PHE
SEQRES 12 A 159 PRO ARG GLN LEU ALA LYS HIS SER GLY ALA LEU GLN ARG
SEQRES 13 A 159 GLN LYS ARG
SHEET 1 A 4 VAL A 40 ALA A 43 0
SHEET 2 A 4 GLU A 113 LEU A 121 1 O ASN A 120 N TYR A 41
SHEET 3 A 4 ALA A 100 ASP A 108 -1 N ALA A 100 O LEU A 121
SHEET 4 A 4 VAL A 69 GLU A 72 -1 N GLN A 70 O GLN A 107
SHEET 1 B 3 LEU A 55 ASN A 57 0
SHEET 2 B 3 THR A 86 VAL A 90 -1 O VAL A 87 N LEU A 56
SHEET 3 B 3 ASP A 78 ASP A 82 -1 N ASP A 82 O THR A 86
SSBOND 1 CYS A 32 CYS A 63 1555 1555 2.02
CISPEP 1 PHE A 93 PRO A 94 0 -0.35
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
(ATOM LINES ARE NOT SHOWN.)
END
