HEADER CELL ADHESION 02-FEB-10 3LNG
TITLE CRYSTAL STRUCTURE OF E-CADHERIN EC12 AA EXTENSION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CADHERIN-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 157-369;
COMPND 5 SYNONYM: EPITHELIAL CADHERIN, E-CADHERIN, UVOMORULIN, ARC-1, E-
COMPND 6 CAD/CTF1, E-CAD/CTF2, E-CAD/CTF3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CDH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CADHERIN, CALCIUM, CELL ADHESION, CELL JUNCTION, CELL MEMBRANE,
KEYWDS 2 CLEAVAGE ON PAIR OF BASIC RESIDUES, GLYCOPROTEIN, MEMBRANE,
KEYWDS 3 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.HARRISON,X.JIN,L.SHAPIRO
REVDAT 3 06-SEP-23 3LNG 1 REMARK SEQADV LINK
REVDAT 2 16-MAR-10 3LNG 1 JRNL
REVDAT 1 02-MAR-10 3LNG 0
JRNL AUTH O.J.HARRISON,F.BAHNA,P.S.KATSAMBA,X.JIN,J.BRASCH,J.VENDOME,
JRNL AUTH 2 G.AHLSEN,K.J.CARROLL,S.R.PRICE,B.HONIG,L.SHAPIRO
JRNL TITL TWO-STEP ADHESIVE BINDING BY CLASSICAL CADHERINS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 17 348 2010
JRNL REFN ISSN 1545-9993
JRNL PMID 20190754
JRNL DOI 10.1038/NSMB.1784
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.5
REMARK 3 NUMBER OF REFLECTIONS : 12996
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 702
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 799
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.3540
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 75
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.92000
REMARK 3 B22 (A**2) : -1.38000
REMARK 3 B33 (A**2) : 3.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.78000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.393
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3316 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4526 ; 1.343 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 422 ; 6.798 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 146 ;40.256 ;26.027
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 546 ;14.145 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;19.390 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 532 ; 0.321 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2512 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2118 ; 0.698 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3468 ; 1.307 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1198 ; 1.659 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1058 ; 3.024 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3LNG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000057494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13698
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.4
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1EDH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, PH 8.5, 1.3M AMMONIUM
REMARK 280 SULFATE, 15% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.76800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.05400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.76800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.05400
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: 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. (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 ALA A -1
REMARK 465 ALA A 0
REMARK 465 ASP A 1
REMARK 465 ALA B -1
REMARK 465 ALA B 0
REMARK 465 ASP B 1
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 C ASP A 213 O HOH A 256 1.53
REMARK 500 N GLU A 156 O HOH A 248 1.73
REMARK 500 NH1 ARG A 28 O VAL A 88 1.86
REMARK 500 NH1 ARG B 105 O HOH B 215 1.94
REMARK 500 N GLU A 56 O HOH A 233 1.97
REMARK 500 OD1 ASP B 138 O HOH B 235 2.01
REMARK 500 OE1 GLU A 119 O HOH A 217 2.01
REMARK 500 N ALA A 87 O HOH A 238 2.02
REMARK 500 OG SER B 82 OD1 ASN B 84 2.05
REMARK 500 OE2 GLU B 156 CD LYS B 160 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 31 OE2 GLU B 31 2556 1.33
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 TRP A 2 C VAL A 3 N -0.232
REMARK 500 TRP B 2 C VAL B 3 N -0.234
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 2 O - C - N ANGL. DEV. = -14.7 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 PRO A 5 153.76 -48.33
REMARK 500 LEU A 21 -61.29 -106.17
REMARK 500 ARG A 28 -1.12 -54.01
REMARK 500 ALA A 43 -78.94 -114.90
REMARK 500 ALA A 70 -60.57 -91.39
REMARK 500 GLU A 156 34.89 -91.67
REMARK 500 ASN A 161 61.56 -116.18
REMARK 500 ARG B 28 -2.37 -53.90
REMARK 500 ALA B 43 -85.66 -124.98
REMARK 500 GLU B 156 43.33 -87.91
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 TRP B 2 VAL B 3 149.73
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 TRP A 2 13.17
REMARK 500 TRP B 2 20.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 11 OE2
REMARK 620 2 GLU A 69 OE2 106.6
REMARK 620 3 ASP A 100 OD1 87.6 79.2
REMARK 620 4 GLN A 101 O 86.8 160.3 87.2
REMARK 620 5 ASP A 103 OD1 91.7 111.6 168.8 81.7
REMARK 620 6 ASP A 136 OD1 171.2 81.6 97.3 86.2 82.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 11 OE1
REMARK 620 2 ASP A 67 OD1 90.1
REMARK 620 3 GLU A 69 OE1 91.4 83.2
REMARK 620 4 ASP A 103 OD2 98.2 161.2 113.2
REMARK 620 5 HOH A 234 O 172.7 93.7 82.9 80.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 102 OD1
REMARK 620 2 ASN A 104 O 113.1
REMARK 620 3 ASP A 134 OD2 143.2 94.5
REMARK 620 4 ASP A 134 OD1 148.1 86.2 51.7
REMARK 620 5 ASP A 136 OD2 77.1 81.9 132.9 81.2
REMARK 620 6 ASN A 143 O 70.7 175.5 83.1 89.3 96.9
REMARK 620 7 ASP A 195 OD2 73.0 102.2 77.9 129.6 148.9 81.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 11 OE2
REMARK 620 2 GLU B 69 OE2 101.9
REMARK 620 3 ASP B 100 OD1 79.9 82.3
REMARK 620 4 GLN B 101 O 85.3 159.5 80.1
REMARK 620 5 ASP B 103 OD1 87.6 115.6 160.1 83.6
REMARK 620 6 ASP B 136 OD1 171.6 83.0 107.7 92.4 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 11 OE1
REMARK 620 2 ASP B 67 OD1 88.2
REMARK 620 3 GLU B 69 OE1 91.1 89.3
REMARK 620 4 ASP B 103 OD2 97.2 148.5 121.4
REMARK 620 5 HOH B 217 O 176.5 95.3 88.7 80.0
REMARK 620 6 HOH B 236 O 81.5 67.9 156.1 82.2 100.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 102 OD1
REMARK 620 2 ASN B 104 O 103.2
REMARK 620 3 ASP B 134 OD2 157.7 85.3
REMARK 620 4 ASP B 134 OD1 148.0 89.5 50.7
REMARK 620 5 ASP B 136 OD2 76.9 78.5 125.2 77.0
REMARK 620 6 ASN B 143 O 83.1 173.3 89.6 83.9 101.0
REMARK 620 7 ASP B 195 OD2 81.8 89.3 77.7 128.3 152.2 93.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LND RELATED DB: PDB
REMARK 900 RELATED ID: 3LNE RELATED DB: PDB
REMARK 900 RELATED ID: 3LNF RELATED DB: PDB
REMARK 900 RELATED ID: 3LNH RELATED DB: PDB
REMARK 900 RELATED ID: 3LNI RELATED DB: PDB
DBREF 3LNG A 1 213 UNP P09803 CADH1_MOUSE 157 369
DBREF 3LNG B 1 213 UNP P09803 CADH1_MOUSE 157 369
SEQADV 3LNG ALA A -1 UNP P09803 INSERTION
SEQADV 3LNG ALA A 0 UNP P09803 INSERTION
SEQADV 3LNG ALA B -1 UNP P09803 INSERTION
SEQADV 3LNG ALA B 0 UNP P09803 INSERTION
SEQRES 1 A 215 ALA ALA ASP TRP VAL ILE PRO PRO ILE SER CYS PRO GLU
SEQRES 2 A 215 ASN GLU LYS GLY GLU PHE PRO LYS ASN LEU VAL GLN ILE
SEQRES 3 A 215 LYS SER ASN ARG ASP LYS GLU THR LYS VAL PHE TYR SER
SEQRES 4 A 215 ILE THR GLY GLN GLY ALA ASP LYS PRO PRO VAL GLY VAL
SEQRES 5 A 215 PHE ILE ILE GLU ARG GLU THR GLY TRP LEU LYS VAL THR
SEQRES 6 A 215 GLN PRO LEU ASP ARG GLU ALA ILE ALA LYS TYR ILE LEU
SEQRES 7 A 215 TYR SER HIS ALA VAL SER SER ASN GLY GLU ALA VAL GLU
SEQRES 8 A 215 ASP PRO MET GLU ILE VAL ILE THR VAL THR ASP GLN ASN
SEQRES 9 A 215 ASP ASN ARG PRO GLU PHE THR GLN GLU VAL PHE GLU GLY
SEQRES 10 A 215 SER VAL ALA GLU GLY ALA VAL PRO GLY THR SER VAL MET
SEQRES 11 A 215 LYS VAL SER ALA THR ASP ALA ASP ASP ASP VAL ASN THR
SEQRES 12 A 215 TYR ASN ALA ALA ILE ALA TYR THR ILE VAL SER GLN ASP
SEQRES 13 A 215 PRO GLU LEU PRO HIS LYS ASN MET PHE THR VAL ASN ARG
SEQRES 14 A 215 ASP THR GLY VAL ILE SER VAL LEU THR SER GLY LEU ASP
SEQRES 15 A 215 ARG GLU SER TYR PRO THR TYR THR LEU VAL VAL GLN ALA
SEQRES 16 A 215 ALA ASP LEU GLN GLY GLU GLY LEU SER THR THR ALA LYS
SEQRES 17 A 215 ALA VAL ILE THR VAL LYS ASP
SEQRES 1 B 215 ALA ALA ASP TRP VAL ILE PRO PRO ILE SER CYS PRO GLU
SEQRES 2 B 215 ASN GLU LYS GLY GLU PHE PRO LYS ASN LEU VAL GLN ILE
SEQRES 3 B 215 LYS SER ASN ARG ASP LYS GLU THR LYS VAL PHE TYR SER
SEQRES 4 B 215 ILE THR GLY GLN GLY ALA ASP LYS PRO PRO VAL GLY VAL
SEQRES 5 B 215 PHE ILE ILE GLU ARG GLU THR GLY TRP LEU LYS VAL THR
SEQRES 6 B 215 GLN PRO LEU ASP ARG GLU ALA ILE ALA LYS TYR ILE LEU
SEQRES 7 B 215 TYR SER HIS ALA VAL SER SER ASN GLY GLU ALA VAL GLU
SEQRES 8 B 215 ASP PRO MET GLU ILE VAL ILE THR VAL THR ASP GLN ASN
SEQRES 9 B 215 ASP ASN ARG PRO GLU PHE THR GLN GLU VAL PHE GLU GLY
SEQRES 10 B 215 SER VAL ALA GLU GLY ALA VAL PRO GLY THR SER VAL MET
SEQRES 11 B 215 LYS VAL SER ALA THR ASP ALA ASP ASP ASP VAL ASN THR
SEQRES 12 B 215 TYR ASN ALA ALA ILE ALA TYR THR ILE VAL SER GLN ASP
SEQRES 13 B 215 PRO GLU LEU PRO HIS LYS ASN MET PHE THR VAL ASN ARG
SEQRES 14 B 215 ASP THR GLY VAL ILE SER VAL LEU THR SER GLY LEU ASP
SEQRES 15 B 215 ARG GLU SER TYR PRO THR TYR THR LEU VAL VAL GLN ALA
SEQRES 16 B 215 ALA ASP LEU GLN GLY GLU GLY LEU SER THR THR ALA LYS
SEQRES 17 B 215 ALA VAL ILE THR VAL LYS ASP
HET CA A 301 1
HET CA A 302 1
HET CA A 303 1
HET CA B 301 1
HET CA B 302 1
HET CA B 303 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 6(CA 2+)
FORMUL 9 HOH *75(H2 O)
HELIX 1 1 SER A 26 LYS A 30 5 5
HELIX 2 2 SER B 26 LYS B 30 5 5
SHEET 1 A 4 ILE A 7 PRO A 10 0
SHEET 2 A 4 ALA A 87 THR A 99 1 O THR A 97 N ILE A 7
SHEET 3 A 4 LYS A 73 SER A 82 -1 N LEU A 76 O ILE A 94
SHEET 4 A 4 VAL A 34 GLY A 40 -1 N PHE A 35 O VAL A 81
SHEET 1 B 3 LYS A 19 GLN A 23 0
SHEET 2 B 3 TRP A 59 VAL A 62 -1 O LEU A 60 N VAL A 22
SHEET 3 B 3 PHE A 51 ILE A 53 -1 N ILE A 52 O LYS A 61
SHEET 1 C 2 GLU A 107 PHE A 108 0
SHEET 2 C 2 ALA A 132 THR A 133 -1 O THR A 133 N GLU A 107
SHEET 1 D 4 VAL A 112 ALA A 118 0
SHEET 2 D 4 SER A 202 LYS A 212 1 O LYS A 212 N VAL A 117
SHEET 3 D 4 THR A 186 ALA A 194 -1 N LEU A 189 O ALA A 207
SHEET 4 D 4 ALA A 147 ASP A 154 -1 N VAL A 151 O VAL A 190
SHEET 1 E 3 SER A 126 LYS A 129 0
SHEET 2 E 3 VAL A 171 VAL A 174 -1 O ILE A 172 N VAL A 127
SHEET 3 E 3 PHE A 163 VAL A 165 -1 N THR A 164 O SER A 173
SHEET 1 F 4 ILE B 7 PRO B 10 0
SHEET 2 F 4 MET B 92 THR B 99 1 O THR B 97 N ILE B 7
SHEET 3 F 4 LYS B 73 SER B 82 -1 N LEU B 76 O ILE B 94
SHEET 4 F 4 VAL B 34 THR B 39 -1 N PHE B 35 O VAL B 81
SHEET 1 G 3 LYS B 19 GLN B 23 0
SHEET 2 G 3 TRP B 59 VAL B 62 -1 O LEU B 60 N VAL B 22
SHEET 3 G 3 PHE B 51 ILE B 53 -1 N ILE B 52 O LYS B 61
SHEET 1 H 2 GLU B 107 PHE B 108 0
SHEET 2 H 2 ALA B 132 THR B 133 -1 O THR B 133 N GLU B 107
SHEET 1 I 4 VAL B 112 ALA B 118 0
SHEET 2 I 4 SER B 202 LYS B 212 1 O LYS B 206 N PHE B 113
SHEET 3 I 4 THR B 186 ALA B 194 -1 N LEU B 189 O ALA B 207
SHEET 4 I 4 ALA B 147 ASP B 154 -1 N VAL B 151 O VAL B 190
SHEET 1 J 3 SER B 126 LYS B 129 0
SHEET 2 J 3 VAL B 171 VAL B 174 -1 O ILE B 172 N VAL B 127
SHEET 3 J 3 PHE B 163 VAL B 165 -1 N THR B 164 O SER B 173
LINK OE2 GLU A 11 CA CA A 302 1555 1555 2.34
LINK OE1 GLU A 11 CA CA A 303 1555 1555 2.47
LINK OD1 ASP A 67 CA CA A 303 1555 1555 2.49
LINK OE2 GLU A 69 CA CA A 302 1555 1555 2.00
LINK OE1 GLU A 69 CA CA A 303 1555 1555 2.15
LINK OD1 ASP A 100 CA CA A 302 1555 1555 2.21
LINK O GLN A 101 CA CA A 302 1555 1555 2.24
LINK OD1 ASN A 102 CA CA A 301 1555 1555 2.38
LINK OD1 ASP A 103 CA CA A 302 1555 1555 2.30
LINK OD2 ASP A 103 CA CA A 303 1555 1555 2.40
LINK O ASN A 104 CA CA A 301 1555 1555 2.25
LINK OD2 ASP A 134 CA CA A 301 1555 1555 2.41
LINK OD1 ASP A 134 CA CA A 301 1555 1555 2.53
LINK OD2 ASP A 136 CA CA A 301 1555 1555 2.37
LINK OD1 ASP A 136 CA CA A 302 1555 1555 2.40
LINK O ASN A 143 CA CA A 301 1555 1555 2.41
LINK OD2 ASP A 195 CA CA A 301 1555 1555 2.38
LINK O HOH A 234 CA CA A 303 1555 1555 1.88
LINK OE2 GLU B 11 CA CA B 302 1555 1555 2.37
LINK OE1 GLU B 11 CA CA B 303 1555 1555 2.48
LINK OD1 ASP B 67 CA CA B 303 1555 1555 2.19
LINK OE2 GLU B 69 CA CA B 302 1555 1555 2.28
LINK OE1 GLU B 69 CA CA B 303 1555 1555 2.00
LINK OD1 ASP B 100 CA CA B 302 1555 1555 2.29
LINK O GLN B 101 CA CA B 302 1555 1555 2.39
LINK OD1 ASN B 102 CA CA B 301 1555 1555 2.24
LINK OD1 ASP B 103 CA CA B 302 1555 1555 2.38
LINK OD2 ASP B 103 CA CA B 303 1555 1555 2.54
LINK O ASN B 104 CA CA B 301 1555 1555 2.42
LINK OD2 ASP B 134 CA CA B 301 1555 1555 2.50
LINK OD1 ASP B 134 CA CA B 301 1555 1555 2.65
LINK OD2 ASP B 136 CA CA B 301 1555 1555 2.54
LINK OD1 ASP B 136 CA CA B 302 1555 1555 2.36
LINK O ASN B 143 CA CA B 301 1555 1555 2.21
LINK OD2 ASP B 195 CA CA B 301 1555 1555 2.48
LINK O HOH B 217 CA CA B 303 1555 1555 2.22
LINK O HOH B 236 CA CA B 303 1555 1555 1.96
CISPEP 1 PHE A 17 PRO A 18 0 5.37
CISPEP 2 PRO A 46 PRO A 47 0 1.40
CISPEP 3 ASP A 154 PRO A 155 0 6.76
CISPEP 4 LEU A 157 PRO A 158 0 -3.44
CISPEP 5 PHE B 17 PRO B 18 0 -4.76
CISPEP 6 PRO B 46 PRO B 47 0 -1.82
CISPEP 7 ASP B 154 PRO B 155 0 4.58
CISPEP 8 LEU B 157 PRO B 158 0 2.87
SITE 1 AC1 6 ASN A 102 ASN A 104 ASP A 134 ASP A 136
SITE 2 AC1 6 ASN A 143 ASP A 195
SITE 1 AC2 6 GLU A 11 GLU A 69 ASP A 100 GLN A 101
SITE 2 AC2 6 ASP A 103 ASP A 136
SITE 1 AC3 6 GLU A 11 ASP A 67 GLU A 69 ASP A 103
SITE 2 AC3 6 HOH A 214 HOH A 234
SITE 1 AC4 6 ASN B 102 ASN B 104 ASP B 134 ASP B 136
SITE 2 AC4 6 ASN B 143 ASP B 195
SITE 1 AC5 6 GLU B 11 GLU B 69 ASP B 100 GLN B 101
SITE 2 AC5 6 ASP B 103 ASP B 136
SITE 1 AC6 6 GLU B 11 ASP B 67 GLU B 69 ASP B 103
SITE 2 AC6 6 HOH B 217 HOH B 236
CRYST1 121.536 80.108 72.691 90.00 118.76 90.00 C 1 2 1 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 0.008228 0.000000 0.004516 0.00000
SCALE2 0.000000 0.012483 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015693 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
