Header list of 1gya.pdb file
Complete list - l 29 2 Bytes
HEADER ADHESION GLYCOPROTEIN 26-MAY-95 1GYA TITLE N-GLYCAN AND POLYPEPTIDE NMR SOLUTION STRUCTURES OF THE ADHESION TITLE 2 DOMAIN OF HUMAN CD2 CAVEAT 1GYA MAN B 9 HAS WRONG CHIRALITY AT ATOM C1 BMA B 3 HAS WRONG CAVEAT 2 1GYA CHIRALITY AT ATOM C1 MAN B 4 HAS WRONG CHIRALITY AT ATOM C1 CAVEAT 3 1GYA MAN B 8 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN CD2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ADHESION DOMAIN; COMPND 5 SYNONYM: HSCD2=105=; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: GLYCOSYLATED SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 ORGAN: OVARY; SOURCE 6 GENE: SCD2=182=; SOURCE 7 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PM1; SOURCE 11 EXPRESSION_SYSTEM_GENE: SCD2=182=; SOURCE 12 OTHER_DETAILS: THE ADHESION DOMAIN OF HUMAN CD2 (HSCD2=105=) WAS SOURCE 13 OBTAINED BY CLOSTRIPAIN DIGESTION OF THE TWO-DOMAIN HUMAN CD2 SOURCE 14 (HSCD2=182=) KEYWDS CELL SURFACE ADHESION RECEPTOR, IMMUNOGLOBULIN SUPERFAMILY V-SET KEYWDS 2 DOMAIN, T LYMPHOCYTE ADHESION GLYCOPROTEIN, ADHESION GLYCOPROTEIN EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR D.F.WYSS,J.S.CHOI,G.WAGNER REVDAT 4 29-JUL-20 1GYA 1 CAVEAT COMPND REMARK HETNAM REVDAT 4 2 1 LINK SITE ATOM REVDAT 3 13-JUL-11 1GYA 1 VERSN REVDAT 2 24-FEB-09 1GYA 1 VERSN REVDAT 1 08-NOV-96 1GYA 0 JRNL AUTH D.F.WYSS,J.S.CHOI,J.LI,M.H.KNOPPERS,K.J.WILLIS, JRNL AUTH 2 A.R.ARULANANDAM,A.SMOLYAR,E.L.REINHERZ,G.WAGNER JRNL TITL CONFORMATION AND FUNCTION OF THE N-LINKED GLYCAN IN THE JRNL TITL 2 ADHESION DOMAIN OF HUMAN CD2. JRNL REF SCIENCE V. 269 1273 1995 JRNL REFN ISSN 0036-8075 JRNL PMID 7544493 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.F.WYSS,J.S.CHOI,G.WAGNER REMARK 1 TITL COMPOSITION AND SEQUENCE SPECIFIC RESONANCE ASSIGNMENTS OF REMARK 1 TITL 2 THE HETEROGENEOUS N-LINKED GLYCAN IN THE 13.6 KDA ADHESION REMARK 1 TITL 3 DOMAIN OF HUMAN CD2 AS DETERMINED BY NMR ON THE INTACT REMARK 1 TITL 4 GLYCOPROTEIN REMARK 1 REF BIOCHEMISTRY V. 34 1622 1995 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DGII REMARK 3 AUTHORS : HAVEL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GYA 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_1000173727. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 286 REMARK 210 PH : 4.5 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 : DGII REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 120 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : PROSTAT/STRUCT_CHECK 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, 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 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 HE2 PHE A 63 HB2 LYS A 69 1.14 REMARK 500 HG22 ILE A 21 HD3 PRO A 22 1.14 REMARK 500 HG13 VAL A 83 HE1 PHE A 98 1.21 REMARK 500 HD11 LEU A 73 HD23 LEU A 100 1.26 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 GLU A 2 CD GLU A 2 OE2 0.109 REMARK 500 1 GLU A 8 CD GLU A 8 OE2 0.110 REMARK 500 1 GLU A 36 CD GLU A 36 OE1 0.110 REMARK 500 1 GLU A 50 CD GLU A 50 OE1 0.110 REMARK 500 1 GLU A 52 CD GLU A 52 OE1 0.109 REMARK 500 1 GLU A 56 CD GLU A 56 OE2 0.110 REMARK 500 1 GLU A 95 CD GLU A 95 OE1 0.110 REMARK 500 1 GLU A 104 CD GLU A 104 OE2 0.111 REMARK 500 2 GLU A 2 CD GLU A 2 OE2 0.110 REMARK 500 2 GLU A 8 CD GLU A 8 OE1 0.110 REMARK 500 2 GLU A 36 CD GLU A 36 OE1 0.111 REMARK 500 2 GLU A 50 CD GLU A 50 OE2 0.110 REMARK 500 2 GLU A 52 CD GLU A 52 OE2 0.110 REMARK 500 2 GLU A 56 CD GLU A 56 OE1 0.109 REMARK 500 2 GLU A 95 CD GLU A 95 OE2 0.110 REMARK 500 2 GLU A 104 CD GLU A 104 OE2 0.109 REMARK 500 3 GLU A 2 CD GLU A 2 OE2 0.110 REMARK 500 3 GLU A 8 CD GLU A 8 OE1 0.109 REMARK 500 3 GLU A 36 CD GLU A 36 OE1 0.110 REMARK 500 3 GLU A 50 CD GLU A 50 OE1 0.110 REMARK 500 3 GLU A 52 CD GLU A 52 OE1 0.110 REMARK 500 3 GLU A 56 CD GLU A 56 OE1 0.110 REMARK 500 3 GLU A 95 CD GLU A 95 OE2 0.110 REMARK 500 3 GLU A 104 CD GLU A 104 OE2 0.110 REMARK 500 4 GLU A 2 CD GLU A 2 OE2 0.109 REMARK 500 4 GLU A 8 CD GLU A 8 OE1 0.109 REMARK 500 4 GLU A 36 CD GLU A 36 OE2 0.109 REMARK 500 4 GLU A 50 CD GLU A 50 OE2 0.110 REMARK 500 4 GLU A 52 CD GLU A 52 OE2 0.110 REMARK 500 4 GLU A 56 CD GLU A 56 OE1 0.110 REMARK 500 4 GLU A 95 CD GLU A 95 OE2 0.110 REMARK 500 4 GLU A 104 CD GLU A 104 OE1 0.110 REMARK 500 5 GLU A 2 CD GLU A 2 OE1 0.110 REMARK 500 5 GLU A 8 CD GLU A 8 OE2 0.110 REMARK 500 5 GLU A 36 CD GLU A 36 OE2 0.110 REMARK 500 5 GLU A 50 CD GLU A 50 OE2 0.110 REMARK 500 5 GLU A 52 CD GLU A 52 OE1 0.110 REMARK 500 5 GLU A 56 CD GLU A 56 OE2 0.110 REMARK 500 5 GLU A 95 CD GLU A 95 OE2 0.110 REMARK 500 5 GLU A 104 CD GLU A 104 OE1 0.109 REMARK 500 6 GLU A 2 CD GLU A 2 OE1 0.110 REMARK 500 6 GLU A 8 CD GLU A 8 OE2 0.110 REMARK 500 6 GLU A 36 CD GLU A 36 OE2 0.111 REMARK 500 6 GLU A 50 CD GLU A 50 OE1 0.109 REMARK 500 6 GLU A 52 CD GLU A 52 OE1 0.110 REMARK 500 6 GLU A 56 CD GLU A 56 OE1 0.110 REMARK 500 6 GLU A 95 CD GLU A 95 OE1 0.110 REMARK 500 6 GLU A 104 CD GLU A 104 OE2 0.111 REMARK 500 7 GLU A 2 CD GLU A 2 OE2 0.110 REMARK 500 7 GLU A 8 CD GLU A 8 OE2 0.111 REMARK 500 REMARK 500 THIS ENTRY HAS 144 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 ASP A 16 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 20 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 29 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 31 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 32 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 40 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 1 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 1 ASP A 58 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 77 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 1 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ASP A 87 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 2 ASP A 16 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 20 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 28 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 2 ASP A 29 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 31 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 32 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 40 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 2 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 2 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 77 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 87 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 3 ASP A 16 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 3 ASP A 20 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ASP A 28 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 3 ASP A 29 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ASP A 31 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ASP A 32 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES REMARK 500 3 ASP A 40 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 3 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ASP A 77 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 3 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ASP A 87 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ASP A 99 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 3 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 4 ASP A 16 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ASP A 20 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ASP A 28 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ASP A 29 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 4 ASP A 31 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ASP A 32 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ASP A 40 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ARG A 48 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 4 ASP A 58 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 4 ASP A 76 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 247 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 GLU A 8 91.61 -57.78 REMARK 500 1 SER A 27 -50.69 -167.01 REMARK 500 1 ASP A 31 -63.38 -133.26 REMARK 500 1 LYS A 49 173.70 69.03 REMARK 500 1 GLU A 50 36.87 -81.69 REMARK 500 1 GLU A 52 85.48 -177.92 REMARK 500 1 LYS A 55 100.60 -161.22 REMARK 500 1 HIS A 72 110.57 61.79 REMARK 500 2 ASP A 20 -155.58 -90.39 REMARK 500 2 PRO A 22 179.60 -45.82 REMARK 500 2 SER A 23 30.85 -88.57 REMARK 500 2 SER A 27 -92.48 -169.96 REMARK 500 2 ASP A 28 -76.36 -66.94 REMARK 500 2 ARG A 48 113.63 -161.92 REMARK 500 2 LYS A 49 154.44 66.80 REMARK 500 2 GLU A 50 33.40 -87.54 REMARK 500 2 GLU A 52 160.47 175.13 REMARK 500 2 LYS A 55 118.16 -160.63 REMARK 500 2 HIS A 72 117.62 62.07 REMARK 500 2 LYS A 89 39.50 -95.15 REMARK 500 2 ASP A 99 111.28 -167.32 REMARK 500 2 GLU A 104 86.46 -163.03 REMARK 500 3 GLU A 2 80.79 -171.76 REMARK 500 3 GLU A 8 91.93 -61.22 REMARK 500 3 PRO A 22 -177.19 -48.51 REMARK 500 3 SER A 23 31.07 -88.97 REMARK 500 3 SER A 27 -89.86 -172.20 REMARK 500 3 ASP A 31 -37.01 -134.87 REMARK 500 3 ASP A 40 37.66 -152.99 REMARK 500 3 LYS A 41 71.86 58.34 REMARK 500 3 LYS A 43 101.54 -45.68 REMARK 500 3 LYS A 49 148.74 72.29 REMARK 500 3 GLU A 50 40.83 -89.32 REMARK 500 3 GLU A 52 97.72 169.11 REMARK 500 3 LYS A 55 57.99 -164.94 REMARK 500 3 GLU A 56 32.67 -90.69 REMARK 500 3 LYS A 57 118.81 -170.42 REMARK 500 3 HIS A 72 121.66 61.34 REMARK 500 3 ASN A 92 99.39 -54.31 REMARK 500 3 GLU A 104 53.30 -163.07 REMARK 500 4 ALA A 6 167.75 179.81 REMARK 500 4 GLU A 8 104.26 -47.19 REMARK 500 4 ASP A 20 -151.48 -81.50 REMARK 500 4 PRO A 22 177.15 -40.49 REMARK 500 4 SER A 23 31.60 -87.59 REMARK 500 4 SER A 27 -97.77 -165.82 REMARK 500 4 THR A 38 -120.62 -45.63 REMARK 500 4 LYS A 43 95.90 -49.57 REMARK 500 4 ARG A 48 114.18 -162.75 REMARK 500 4 LYS A 49 146.65 68.13 REMARK 500 REMARK 500 THIS ENTRY HAS 268 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1GYA A 1 105 UNP P06729 CD2_HUMAN 25 129 SEQRES 1 A 105 LYS GLU ILE THR ASN ALA LEU GLU THR TRP GLY ALA LEU SEQRES 2 A 105 GLY GLN ASP ILE ASN LEU ASP ILE PRO SER PHE GLN MET SEQRES 3 A 105 SER ASP ASP ILE ASP ASP ILE LYS TRP GLU LYS THR SER SEQRES 4 A 105 ASP LYS LYS LYS ILE ALA GLN PHE ARG LYS GLU LYS GLU SEQRES 5 A 105 THR PHE LYS GLU LYS ASP THR TYR LYS LEU PHE LYS ASN SEQRES 6 A 105 GLY THR LEU LYS ILE LYS HIS LEU LYS THR ASP ASP GLN SEQRES 7 A 105 ASP ILE TYR LYS VAL SER ILE TYR ASP THR LYS GLY LYS SEQRES 8 A 105 ASN VAL LEU GLU LYS ILE PHE ASP LEU LYS ILE GLN GLU SEQRES 9 A 105 ARG MODRES 1GYA ASN A 65 ASN GLYCOSYLATION SITE HET NAG B 1 27 HET NAG B 2 27 HET BMA B 3 20 HET MAN B 4 20 HET MAN B 5 21 HET MAN B 6 22 HET MAN B 7 22 HET MAN B 8 21 HET MAN B 9 22 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE FORMUL 2 NAG 2(C8 H15 N O6) FORMUL 2 BMA C6 H12 O6 FORMUL 2 MAN 6(C6 H12 O6) HELIX 1 1 GLU A 50 GLU A 52 5 3 SHEET 1 S1 6 LEU A 7 ALA A 12 0 SHEET 2 S1 6 LEU A 94 GLN A 103 1 N ASP A 99 O LEU A 7 SHEET 3 S1 6 ILE A 80 TYR A 86 -1 N TYR A 81 O PHE A 98 SHEET 4 S1 6 ASP A 32 LYS A 37 -1 N ASP A 32 O TYR A 86 SHEET 5 S1 6 LYS A 43 PHE A 47 -1 N ALA A 45 O TRP A 35 SHEET 6 S1 6 THR A 53 LYS A 55 -1 N PHE A 54 O GLN A 46 SHEET 1 S2 3 ASP A 16 ASP A 20 0 SHEET 2 S2 3 THR A 67 LYS A 71 -1 N LEU A 68 O LEU A 19 SHEET 3 S2 3 TYR A 60 PHE A 63 -1 N LYS A 61 O LYS A 69 LINK ND2 ASN A 65 C1 NAG B 1 1555 1555 1.45 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.47 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 LINK O6 BMA B 3 C1 MAN B 4 1555 1555 1.45 LINK O3 BMA B 3 C1 MAN B 8 1555 1555 1.46 LINK O6 MAN B 4 C1 MAN B 5 1555 1555 1.45 LINK O3 MAN B 4 C1 MAN B 7 1555 1555 1.45 LINK O2 MAN B 5 C1 MAN B 6 1555 1555 1.45 LINK O2 MAN B 8 C1 MAN B 9 1555 1555 1.45 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 - l 29 2 Bytes