Header list of 1suh.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 30-JAN-96 1SUH TITLE AMINO-TERMINAL DOMAIN OF EPITHELIAL CADHERIN IN THE CALCIUM BOUND TITLE 2 STATE, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: EPITHELIAL CADHERIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: AMINO-TERMINAL DOMAIN RESIDUES 1 - 104; COMPND 5 SYNONYM: UVOMORULIN; COMPND 6 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 TISSUE: EPITHELIAL, NEURAL; SOURCE 6 GENE: X06115 (GENBANK); SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAS; SOURCE 10 EXPRESSION_SYSTEM_GENE: X06115 (GENBANK) KEYWDS CADHERIN, CALCIUM BINDING, CELL ADHESION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.OVERDUIN,K.I.TONG,C.M.KAY,M.IKURA REVDAT 3 02-MAR-22 1SUH 1 REMARK REVDAT 2 24-FEB-09 1SUH 1 VERSN REVDAT 1 11-JUL-96 1SUH 0 JRNL AUTH M.OVERDUIN,K.I.TONG,C.M.KAY,M.IKURA JRNL TITL 1H, 15N AND 13C RESONANCE ASSIGNMENTS AND MONOMERIC JRNL TITL 2 STRUCTURE OF THE AMINO-TERMINAL EXTRACELLULAR DOMAIN OF JRNL TITL 3 EPITHELIAL CADHERIN. JRNL REF J.BIOMOL.NMR V. 7 173 1996 JRNL REFN ISSN 0925-2738 JRNL PMID 8785495 JRNL DOI 10.1007/BF00202035 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.OVERDUIN,T.S.HARVEY,S.BAGBY,K.I.TONG,P.YAU,M.TAKEICHI, REMARK 1 AUTH 2 M.IKURA REMARK 1 TITL SOLUTION STRUCTURE OF THE EPITHELIAL CADHERIN DOMAIN REMARK 1 TITL 2 RESPONSIBLE FOR SELECTIVE CELL ADHESION REMARK 1 REF SCIENCE V. 267 386 1995 REMARK 1 REFN ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1SUH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000176524. 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 : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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: 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 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A -1 REMARK 465 ARG A 0 REMARK 465 ARG A 105 REMARK 465 PRO A 106 REMARK 465 GLU A 107 REMARK 465 PHE A 108 REMARK 465 THR A 109 REMARK 465 GLN A 110 REMARK 465 GLU A 111 REMARK 465 VAL A 112 REMARK 465 PHE A 113 REMARK 465 GLU A 114 REMARK 465 GLY A 115 REMARK 465 SER A 116 REMARK 465 VAL A 117 REMARK 465 ALA A 118 REMARK 465 GLU A 119 REMARK 465 GLY A 120 REMARK 465 ALA A 121 REMARK 465 VAL A 122 REMARK 465 PRO A 123 REMARK 465 GLY A 124 REMARK 465 THR A 125 REMARK 465 SER A 126 REMARK 465 VAL A 127 REMARK 465 MET A 128 REMARK 465 LYS A 129 REMARK 465 VAL A 130 REMARK 465 SER A 131 REMARK 465 ALA A 132 REMARK 465 THR A 133 REMARK 465 ASP A 134 REMARK 465 ALA A 135 REMARK 465 ASP A 136 REMARK 465 ASP A 137 REMARK 465 ASP A 138 REMARK 465 VAL A 139 REMARK 465 ASN A 140 REMARK 465 THR A 141 REMARK 465 TYR A 142 REMARK 465 ASN A 143 REMARK 465 ALA A 144 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 TRP A 2 CG TRP A 2 CD2 -0.115 REMARK 500 1 TRP A 59 CG TRP A 59 CD2 -0.124 REMARK 500 1 HIS A 79 CG HIS A 79 ND1 -0.121 REMARK 500 2 TRP A 2 CG TRP A 2 CD2 -0.116 REMARK 500 2 TRP A 59 CG TRP A 59 CD2 -0.125 REMARK 500 2 HIS A 79 CG HIS A 79 ND1 -0.121 REMARK 500 3 TRP A 2 CG TRP A 2 CD2 -0.119 REMARK 500 3 TRP A 59 CG TRP A 59 CD2 -0.124 REMARK 500 3 HIS A 79 CG HIS A 79 ND1 -0.121 REMARK 500 4 TRP A 2 CG TRP A 2 CD2 -0.112 REMARK 500 4 TRP A 59 CG TRP A 59 CD2 -0.127 REMARK 500 4 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 5 TRP A 2 CG TRP A 2 CD2 -0.125 REMARK 500 5 TRP A 59 CG TRP A 59 CD2 -0.127 REMARK 500 5 HIS A 79 CG HIS A 79 ND1 -0.121 REMARK 500 6 TRP A 2 CG TRP A 2 CD2 -0.118 REMARK 500 6 TRP A 59 CG TRP A 59 CD2 -0.127 REMARK 500 6 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 7 TRP A 2 CG TRP A 2 CD2 -0.113 REMARK 500 7 TRP A 59 CG TRP A 59 CD2 -0.121 REMARK 500 7 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 8 TRP A 2 CG TRP A 2 CD2 -0.118 REMARK 500 8 TRP A 59 CG TRP A 59 CD2 -0.124 REMARK 500 8 HIS A 79 CG HIS A 79 ND1 -0.119 REMARK 500 9 TRP A 2 CG TRP A 2 CD2 -0.118 REMARK 500 9 TRP A 59 CG TRP A 59 CD2 -0.128 REMARK 500 9 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 10 TRP A 2 CG TRP A 2 CD2 -0.121 REMARK 500 10 TRP A 59 CG TRP A 59 CD2 -0.124 REMARK 500 10 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 11 TRP A 2 CG TRP A 2 CD2 -0.122 REMARK 500 11 TRP A 59 CG TRP A 59 CD2 -0.123 REMARK 500 11 HIS A 79 CG HIS A 79 ND1 -0.118 REMARK 500 12 TRP A 2 CG TRP A 2 CD2 -0.116 REMARK 500 12 TRP A 59 CG TRP A 59 CD2 -0.127 REMARK 500 12 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 13 TRP A 2 CG TRP A 2 CD2 -0.113 REMARK 500 13 TRP A 59 CG TRP A 59 CD2 -0.123 REMARK 500 13 HIS A 79 CG HIS A 79 ND1 -0.119 REMARK 500 14 TRP A 2 CG TRP A 2 CD2 -0.122 REMARK 500 14 TRP A 59 CG TRP A 59 CD2 -0.126 REMARK 500 14 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 15 TRP A 2 CG TRP A 2 CD2 -0.125 REMARK 500 15 TRP A 59 CG TRP A 59 CD2 -0.125 REMARK 500 15 HIS A 79 CG HIS A 79 ND1 -0.120 REMARK 500 16 TRP A 2 CG TRP A 2 CD2 -0.125 REMARK 500 16 TRP A 59 CG TRP A 59 CD2 -0.122 REMARK 500 16 HIS A 79 CG HIS A 79 ND1 -0.121 REMARK 500 17 TRP A 2 CG TRP A 2 CD2 -0.108 REMARK 500 17 TRP A 59 CG TRP A 59 CD2 -0.129 REMARK 500 REMARK 500 THIS ENTRY HAS 60 BOND DEVIATIONS. 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 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 1 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES REMARK 500 1 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 1 TRP A 59 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 1 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES REMARK 500 1 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 2 TRP A 2 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES REMARK 500 2 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES REMARK 500 2 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES REMARK 500 2 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES REMARK 500 2 TRP A 59 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES REMARK 500 2 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 2 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES REMARK 500 2 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 3 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES REMARK 500 3 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES REMARK 500 3 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 3 TRP A 59 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 3 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 3 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES REMARK 500 3 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 4 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 4 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES REMARK 500 4 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES REMARK 500 4 TRP A 59 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES REMARK 500 4 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 4 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES REMARK 500 4 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 5 TRP A 2 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES REMARK 500 5 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES REMARK 500 5 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 10.5 DEGREES REMARK 500 5 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.8 DEGREES REMARK 500 5 TRP A 2 CG - CD2 - CE3 ANGL. DEV. = -5.9 DEGREES REMARK 500 5 TRP A 59 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 5 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 5 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES REMARK 500 5 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES REMARK 500 5 TRP A 59 CG - CD2 - CE3 ANGL. DEV. = -5.5 DEGREES REMARK 500 6 TRP A 2 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES REMARK 500 6 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES REMARK 500 6 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES REMARK 500 6 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES REMARK 500 6 TRP A 59 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 6 TRP A 59 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES REMARK 500 6 TRP A 59 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES REMARK 500 6 TRP A 59 CG - CD2 - CE3 ANGL. DEV. = -5.6 DEGREES REMARK 500 7 TRP A 2 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES REMARK 500 7 TRP A 2 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES REMARK 500 7 TRP A 2 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 153 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 VAL A 3 87.12 -156.67 REMARK 500 1 ILE A 4 88.97 -162.33 REMARK 500 1 LEU A 21 -60.32 -127.77 REMARK 500 1 SER A 26 -121.29 -100.28 REMARK 500 1 ASN A 27 -47.84 -158.43 REMARK 500 1 ARG A 28 -8.87 -56.44 REMARK 500 1 ASP A 29 17.54 -65.02 REMARK 500 1 GLU A 31 -30.61 -134.09 REMARK 500 1 LYS A 33 109.13 -48.90 REMARK 500 1 VAL A 50 -55.65 -138.83 REMARK 500 1 SER A 83 1.50 -55.08 REMARK 500 1 PRO A 91 90.30 -53.67 REMARK 500 1 GLN A 101 173.68 -53.70 REMARK 500 2 VAL A 3 89.29 -161.68 REMARK 500 2 ILE A 4 89.13 -161.01 REMARK 500 2 LEU A 21 -67.27 -121.80 REMARK 500 2 SER A 26 -144.67 -99.41 REMARK 500 2 ARG A 28 -9.30 -56.75 REMARK 500 2 ASP A 29 14.39 -65.11 REMARK 500 2 VAL A 50 -53.20 -148.94 REMARK 500 2 GLU A 56 -69.19 -92.41 REMARK 500 2 SER A 83 6.80 -60.93 REMARK 500 2 PRO A 91 85.80 -53.86 REMARK 500 2 ASN A 102 -117.99 -177.57 REMARK 500 2 ASP A 103 123.86 66.69 REMARK 500 3 VAL A 3 89.25 -158.42 REMARK 500 3 ILE A 4 86.48 -159.90 REMARK 500 3 ASN A 12 82.60 43.86 REMARK 500 3 LEU A 21 -62.18 -99.31 REMARK 500 3 SER A 26 -108.06 -102.16 REMARK 500 3 ASN A 27 -49.22 -170.73 REMARK 500 3 ARG A 28 -6.08 -59.43 REMARK 500 3 ASP A 29 15.96 -65.75 REMARK 500 3 LYS A 33 108.88 -49.28 REMARK 500 3 ALA A 43 -78.86 -108.58 REMARK 500 3 VAL A 50 -37.51 -141.17 REMARK 500 3 GLU A 56 -67.31 -92.29 REMARK 500 3 ALA A 72 -19.14 -143.52 REMARK 500 3 SER A 83 0.97 -56.09 REMARK 500 3 PRO A 91 87.56 -51.99 REMARK 500 3 ASP A 100 -165.16 -70.79 REMARK 500 4 VAL A 3 87.56 -162.64 REMARK 500 4 ILE A 4 88.78 -162.46 REMARK 500 4 ASN A 12 -1.84 53.11 REMARK 500 4 SER A 26 -111.92 -104.96 REMARK 500 4 ASN A 27 -50.92 -171.86 REMARK 500 4 ARG A 28 5.64 -69.38 REMARK 500 4 ASP A 29 16.84 -65.05 REMARK 500 4 ALA A 43 -74.28 -123.05 REMARK 500 4 VAL A 50 -43.09 -143.49 REMARK 500 REMARK 500 THIS ENTRY HAS 288 RAMACHANDRAN OUTLIERS. 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 ARG A 28 0.30 SIDE CHAIN REMARK 500 1 ARG A 55 0.20 SIDE CHAIN REMARK 500 1 ARG A 68 0.27 SIDE CHAIN REMARK 500 2 ARG A 28 0.28 SIDE CHAIN REMARK 500 2 ARG A 55 0.31 SIDE CHAIN REMARK 500 2 ARG A 68 0.17 SIDE CHAIN REMARK 500 3 ARG A 28 0.32 SIDE CHAIN REMARK 500 3 ARG A 55 0.28 SIDE CHAIN REMARK 500 3 ARG A 68 0.20 SIDE CHAIN REMARK 500 4 ARG A 28 0.19 SIDE CHAIN REMARK 500 4 ARG A 55 0.27 SIDE CHAIN REMARK 500 4 ARG A 68 0.24 SIDE CHAIN REMARK 500 5 ARG A 28 0.16 SIDE CHAIN REMARK 500 5 ARG A 55 0.29 SIDE CHAIN REMARK 500 5 ARG A 68 0.30 SIDE CHAIN REMARK 500 6 ARG A 55 0.21 SIDE CHAIN REMARK 500 6 ARG A 68 0.27 SIDE CHAIN REMARK 500 7 ARG A 28 0.20 SIDE CHAIN REMARK 500 7 ARG A 55 0.31 SIDE CHAIN REMARK 500 7 ARG A 68 0.29 SIDE CHAIN REMARK 500 8 ARG A 28 0.27 SIDE CHAIN REMARK 500 8 ARG A 55 0.12 SIDE CHAIN REMARK 500 8 ARG A 68 0.08 SIDE CHAIN REMARK 500 9 ARG A 28 0.32 SIDE CHAIN REMARK 500 9 ARG A 55 0.12 SIDE CHAIN REMARK 500 9 ARG A 68 0.32 SIDE CHAIN REMARK 500 10 ARG A 28 0.15 SIDE CHAIN REMARK 500 10 ARG A 55 0.10 SIDE CHAIN REMARK 500 10 ARG A 68 0.25 SIDE CHAIN REMARK 500 11 ARG A 28 0.32 SIDE CHAIN REMARK 500 11 ARG A 55 0.14 SIDE CHAIN REMARK 500 11 ARG A 68 0.26 SIDE CHAIN REMARK 500 12 ARG A 28 0.24 SIDE CHAIN REMARK 500 12 ARG A 55 0.12 SIDE CHAIN REMARK 500 12 ARG A 68 0.10 SIDE CHAIN REMARK 500 13 ARG A 55 0.29 SIDE CHAIN REMARK 500 13 ARG A 68 0.32 SIDE CHAIN REMARK 500 14 ARG A 28 0.32 SIDE CHAIN REMARK 500 14 ARG A 55 0.22 SIDE CHAIN REMARK 500 15 ARG A 28 0.14 SIDE CHAIN REMARK 500 15 ARG A 55 0.17 SIDE CHAIN REMARK 500 15 ARG A 68 0.27 SIDE CHAIN REMARK 500 16 ARG A 28 0.31 SIDE CHAIN REMARK 500 16 ARG A 55 0.21 SIDE CHAIN REMARK 500 16 ARG A 68 0.20 SIDE CHAIN REMARK 500 17 ARG A 28 0.32 SIDE CHAIN REMARK 500 17 ARG A 55 0.31 SIDE CHAIN REMARK 500 17 ARG A 68 0.32 SIDE CHAIN REMARK 500 18 ARG A 28 0.14 SIDE CHAIN REMARK 500 18 ARG A 55 0.31 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 56 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1SUH A 0 144 UNP P09803 CADH1_MOUSE 156 300 SEQRES 1 A 146 MET ARG ASP TRP VAL ILE PRO PRO ILE SER CYS PRO GLU SEQRES 2 A 146 ASN GLU LYS GLY GLU PHE PRO LYS ASN LEU VAL GLN ILE SEQRES 3 A 146 LYS SER ASN ARG ASP LYS GLU THR LYS VAL PHE TYR SER SEQRES 4 A 146 ILE THR GLY GLN GLY ALA ASP LYS PRO PRO VAL GLY VAL SEQRES 5 A 146 PHE ILE ILE GLU ARG GLU THR GLY TRP LEU LYS VAL THR SEQRES 6 A 146 GLN PRO LEU ASP ARG GLU ALA ILE ALA LYS TYR ILE LEU SEQRES 7 A 146 TYR SER HIS ALA VAL SER SER ASN GLY GLU ALA VAL GLU SEQRES 8 A 146 ASP PRO MET GLU ILE VAL ILE THR VAL THR ASP GLN ASN SEQRES 9 A 146 ASP ASN ARG PRO GLU PHE THR GLN GLU VAL PHE GLU GLY SEQRES 10 A 146 SER VAL ALA GLU GLY ALA VAL PRO GLY THR SER VAL MET SEQRES 11 A 146 LYS VAL SER ALA THR ASP ALA ASP ASP ASP VAL ASN THR SEQRES 12 A 146 TYR ASN ALA HELIX 1 1 ASN A 27 GLU A 31 5 5 HELIX 2 2 ASP A 67 ILE A 71 5 5 SHEET 1 A 4 ILE A 4 PRO A 10 0 SHEET 2 A 4 GLU A 86 THR A 99 1 N VAL A 95 O ILE A 7 SHEET 3 A 4 LYS A 73 SER A 82 -1 N SER A 78 O MET A 92 SHEET 4 A 4 VAL A 34 THR A 39 -1 N THR A 39 O TYR A 77 SHEET 1 B 3 PHE A 51 GLU A 54 0 SHEET 2 B 3 GLY A 58 THR A 63 -1 N LYS A 61 O ILE A 52 SHEET 3 B 3 LYS A 19 ILE A 24 -1 N VAL A 22 O LEU A 60 CISPEP 1 PHE A 17 PRO A 18 1 -1.14 CISPEP 2 PRO A 46 PRO A 47 1 -2.65 CISPEP 3 PHE A 17 PRO A 18 2 -0.78 CISPEP 4 PRO A 46 PRO A 47 2 -2.56 CISPEP 5 PHE A 17 PRO A 18 3 -2.34 CISPEP 6 PRO A 46 PRO A 47 3 -3.08 CISPEP 7 PHE A 17 PRO A 18 4 -2.25 CISPEP 8 PRO A 46 PRO A 47 4 -0.77 CISPEP 9 PHE A 17 PRO A 18 5 -1.94 CISPEP 10 PRO A 46 PRO A 47 5 -1.44 CISPEP 11 PHE A 17 PRO A 18 6 -1.38 CISPEP 12 PRO A 46 PRO A 47 6 -2.91 CISPEP 13 PHE A 17 PRO A 18 7 -1.97 CISPEP 14 PRO A 46 PRO A 47 7 -1.39 CISPEP 15 PHE A 17 PRO A 18 8 0.07 CISPEP 16 PRO A 46 PRO A 47 8 -1.84 CISPEP 17 PHE A 17 PRO A 18 9 -1.83 CISPEP 18 PRO A 46 PRO A 47 9 -1.11 CISPEP 19 PHE A 17 PRO A 18 10 -1.15 CISPEP 20 PRO A 46 PRO A 47 10 -2.05 CISPEP 21 PHE A 17 PRO A 18 11 -1.91 CISPEP 22 PRO A 46 PRO A 47 11 -1.58 CISPEP 23 PHE A 17 PRO A 18 12 -1.88 CISPEP 24 PRO A 46 PRO A 47 12 -2.63 CISPEP 25 PHE A 17 PRO A 18 13 -3.56 CISPEP 26 PRO A 46 PRO A 47 13 -1.83 CISPEP 27 PHE A 17 PRO A 18 14 -2.31 CISPEP 28 PRO A 46 PRO A 47 14 -2.84 CISPEP 29 PHE A 17 PRO A 18 15 -1.56 CISPEP 30 PRO A 46 PRO A 47 15 -1.13 CISPEP 31 PHE A 17 PRO A 18 16 0.03 CISPEP 32 PRO A 46 PRO A 47 16 -2.38 CISPEP 33 PHE A 17 PRO A 18 17 -0.79 CISPEP 34 PRO A 46 PRO A 47 17 -1.50 CISPEP 35 PHE A 17 PRO A 18 18 -1.72 CISPEP 36 PRO A 46 PRO A 47 18 -2.41 CISPEP 37 PHE A 17 PRO A 18 19 1.98 CISPEP 38 PRO A 46 PRO A 47 19 -0.86 CISPEP 39 PHE A 17 PRO A 18 20 -0.22 CISPEP 40 PRO A 46 PRO A 47 20 -0.22 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