Header list of 1mak.pdb file
Complete list - v 29 2 Bytes
HEADER IMMUNOGLOBULIN 16-SEP-93 1MAK
TITLE SOLUTION STRUCTURE OF AN ISOLATED ANTIBODY VL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGG2A-KAPPA 26-10 FV (LIGHT CHAIN);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090
KEYWDS IMMUNOGLOBULIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.L.CONSTANTINE,M.S.FRIEDRICHS,W.J.METZLER,M.WITTEKIND,P.HENSLEY,
AUTHOR 2 L.MUELLER
REVDAT 3 29-NOV-17 1MAK 1 REMARK HELIX
REVDAT 2 24-FEB-09 1MAK 1 VERSN
REVDAT 1 31-JAN-94 1MAK 0
JRNL AUTH K.L.CONSTANTINE,M.S.FRIEDRICHS,W.J.METZLER,M.WITTEKIND,
JRNL AUTH 2 P.HENSLEY,L.MUELLER
JRNL TITL SOLUTION STRUCTURE OF AN ISOLATED ANTIBODY VL DOMAIN.
JRNL REF J.MOL.BIOL. V. 236 310 1994
JRNL REFN ISSN 0022-2836
JRNL PMID 8107112
JRNL DOI 10.1006/JMBI.1994.1137
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.D.JEFFREY,R.K.STRONG,L.C.SIEKER,C.Y.CHANG,R.L.CAMPBELL,
REMARK 1 AUTH 2 G.A.PETSKO,E.HABER,M.N.MARGOLIES,S.SHERIFF
REMARK 1 TITL 26-10 FAB: DIGOXIN COMPLEX-AFFINITY AND SPECIFICITY FROM
REMARK 1 TITL 2 SURFACE COMPLEMENTARITY
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.L.CONSTANTINE,V.GOLDFARB,M.WITTEKIND,M.S.FRIEDRICHS,
REMARK 1 AUTH 2 J.ANTHONY,S.-C.NG,L.MUELLER
REMARK 1 TITL ALIPHATIC 1H AND 13C RESONANCE ASSIGNMENTS FOR THE 26-10
REMARK 1 TITL 2 ANTIBODY VL DOMAIN DERIVED FROM HETERONUCLEAR
REMARK 1 TITL 3 MULTIDIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF J.BIOMOL.NMR V. 3 41 1993
REMARK 1 REFN ISSN 0925-2738
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.L.CONSTANTINE,M.S.FRIEDRICHS,V.GOLDFARB,P.D.JEFFREY,
REMARK 1 AUTH 2 S.SHERIFF,L.MUELLER
REMARK 1 TITL CHARACTERIZATION OF THE BACKBONE DYNAMICS OF AN ANTI-DIGOXIN
REMARK 1 TITL 2 ANTIBODY VL DOMAIN BY INVERSE DETECTED 1H-15N NMR:
REMARK 1 TITL 3 COMPARISONS WITH X-RAY DATA FOR THE FAB
REMARK 1 REF PROTEINS V. 15 290 1993
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 4
REMARK 1 AUTH V.GOLDFARB,M.WITTEKIND,P.D.JEFFREY,L.MUELLER,K.L.CONSTANTINE
REMARK 1 TITL PRODUCTION AND CHARACTERIZATION OF AN ANTIBODY FV FRAGMENT
REMARK 1 TITL 2 15N-LABELLED IN THE VL DOMAIN ONLY
REMARK 1 REF J.MOL.BIOL. V. 232 15 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH K.L.CONSTANTINE,V.GOLDFARB,M.WITTEKIND,J.ANTHONY,S.-C.NG,
REMARK 1 AUTH 2 L.MUELLER
REMARK 1 TITL SEQUENTIAL 1H AND 15N NMR ASSIGNMENTS AND SECONDARY
REMARK 1 TITL 2 STRUCTURE OF A RECOMBINANT ANTI-DIGOXIN ANTIBODY VL DOMAIN
REMARK 1 REF BIOCHEMISTRY V. 31 5033 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : GUNTERT,WUTHRICH (DIANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MAK 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_1000174903.
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 : 15
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 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 HIS A 31 CG HIS A 31 ND1 -0.093
REMARK 500 1 HIS A 98 CG HIS A 98 ND1 -0.092
REMARK 500 2 HIS A 31 CG HIS A 31 ND1 -0.091
REMARK 500 2 HIS A 98 CG HIS A 98 ND1 -0.094
REMARK 500 3 HIS A 31 CG HIS A 31 ND1 -0.093
REMARK 500 3 TRP A 40 CG TRP A 40 CD2 -0.103
REMARK 500 3 HIS A 98 CG HIS A 98 ND1 -0.094
REMARK 500 4 HIS A 31 CG HIS A 31 ND1 -0.093
REMARK 500 4 HIS A 98 CG HIS A 98 ND1 -0.094
REMARK 500 5 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 5 TRP A 40 CG TRP A 40 CD2 -0.105
REMARK 500 5 HIS A 98 CG HIS A 98 ND1 -0.091
REMARK 500 6 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 6 HIS A 98 CG HIS A 98 ND1 -0.092
REMARK 500 7 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 7 HIS A 98 CG HIS A 98 ND1 -0.091
REMARK 500 8 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 8 TRP A 40 CG TRP A 40 CD2 -0.104
REMARK 500 8 HIS A 98 CG HIS A 98 ND1 -0.093
REMARK 500 9 HIS A 31 CG HIS A 31 ND1 -0.093
REMARK 500 9 TRP A 40 CG TRP A 40 CD2 -0.104
REMARK 500 9 HIS A 98 CG HIS A 98 ND1 -0.093
REMARK 500 10 HIS A 31 CG HIS A 31 ND1 -0.093
REMARK 500 10 HIS A 98 CG HIS A 98 ND1 -0.092
REMARK 500 11 HIS A 31 CG HIS A 31 ND1 -0.093
REMARK 500 11 HIS A 98 CG HIS A 98 ND1 -0.093
REMARK 500 12 HIS A 31 CG HIS A 31 ND1 -0.091
REMARK 500 12 HIS A 98 CG HIS A 98 ND1 -0.094
REMARK 500 13 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 13 HIS A 98 CG HIS A 98 ND1 -0.094
REMARK 500 14 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 14 HIS A 98 CG HIS A 98 ND1 -0.094
REMARK 500 15 HIS A 31 CG HIS A 31 ND1 -0.092
REMARK 500 15 HIS A 98 CG HIS A 98 ND1 -0.093
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 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 2 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 2 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 3 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 3 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 3 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 4 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 5 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 5 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 5 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 5 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 6 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 6 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 6 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 6 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 7 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 7 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 7 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 7 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 8 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 8 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 8 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 8 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 9 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 9 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 9 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 9 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 10 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 10 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 10 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 10 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 11 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 11 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 11 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 11 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 12 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 12 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 12 TRP A 40 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 12 TRP A 40 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 13 TRP A 40 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 13 TRP A 40 CD1 - NE1 - CE2 ANGL. DEV. = 6.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 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 LEU A 15 89.24 -68.13
REMARK 500 1 ASP A 17 -168.89 -79.83
REMARK 500 1 SER A 20 76.18 -162.35
REMARK 500 1 LEU A 29 32.49 -79.68
REMARK 500 1 LYS A 44 -128.90 -109.67
REMARK 500 1 VAL A 56 -71.00 42.06
REMARK 500 1 ASN A 58 106.80 -47.40
REMARK 500 1 SER A 61 85.65 -64.53
REMARK 500 1 ASP A 65 -7.72 -58.74
REMARK 500 2 LEU A 15 86.36 -67.48
REMARK 500 2 LEU A 29 33.43 -85.23
REMARK 500 2 HIS A 31 -121.19 -77.88
REMARK 500 2 ASN A 33 54.62 34.96
REMARK 500 2 LEU A 42 111.14 -160.51
REMARK 500 2 LYS A 44 -169.81 -128.36
REMARK 500 2 VAL A 56 -85.96 29.70
REMARK 500 2 SER A 61 98.05 -59.11
REMARK 500 2 SER A 72 -99.32 -90.83
REMARK 500 2 THR A 102 -92.20 -87.43
REMARK 500 2 PHE A 103 116.66 61.99
REMARK 500 3 SER A 20 96.54 -160.64
REMARK 500 3 LEU A 29 30.32 -97.89
REMARK 500 3 HIS A 31 -124.77 -83.43
REMARK 500 3 ASN A 33 21.06 -170.35
REMARK 500 3 LYS A 44 -146.49 -113.98
REMARK 500 3 ALA A 45 -76.94 -72.20
REMARK 500 3 LYS A 55 -67.07 74.40
REMARK 500 3 VAL A 56 -32.81 -171.07
REMARK 500 3 SER A 57 -28.76 -152.43
REMARK 500 3 SER A 61 104.07 -59.39
REMARK 500 3 SER A 72 -82.73 -91.21
REMARK 500 4 SER A 20 79.89 -162.03
REMARK 500 4 CYS A 23 89.31 -161.41
REMARK 500 4 LEU A 29 32.62 -85.28
REMARK 500 4 HIS A 31 -130.79 -89.60
REMARK 500 4 ASN A 33 -86.28 -115.08
REMARK 500 4 LYS A 44 -135.26 -114.19
REMARK 500 4 PRO A 49 108.88 -58.80
REMARK 500 4 LEU A 52 -81.13 -111.03
REMARK 500 4 LYS A 55 -150.87 58.09
REMARK 500 4 SER A 57 65.99 -179.57
REMARK 500 4 SER A 81 -73.19 -69.81
REMARK 500 4 THR A 96 20.41 -144.46
REMARK 500 4 PHE A 103 118.63 65.86
REMARK 500 5 SER A 20 89.95 -159.48
REMARK 500 5 LEU A 29 28.47 -77.73
REMARK 500 5 LEU A 38 135.14 -173.89
REMARK 500 5 LYS A 44 -114.97 -122.62
REMARK 500 5 LEU A 52 -73.80 -116.08
REMARK 500 5 LYS A 55 44.38 -147.70
REMARK 500
REMARK 500 THIS ENTRY HAS 146 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 24 0.32 SIDE CHAIN
REMARK 500 1 ARG A 59 0.23 SIDE CHAIN
REMARK 500 1 ARG A 66 0.29 SIDE CHAIN
REMARK 500 1 ARG A 82 0.32 SIDE CHAIN
REMARK 500 1 ARG A 113 0.29 SIDE CHAIN
REMARK 500 2 ARG A 24 0.32 SIDE CHAIN
REMARK 500 2 ARG A 59 0.30 SIDE CHAIN
REMARK 500 2 ARG A 66 0.29 SIDE CHAIN
REMARK 500 2 ARG A 82 0.23 SIDE CHAIN
REMARK 500 2 ARG A 113 0.32 SIDE CHAIN
REMARK 500 3 ARG A 24 0.32 SIDE CHAIN
REMARK 500 3 ARG A 59 0.31 SIDE CHAIN
REMARK 500 3 ARG A 66 0.29 SIDE CHAIN
REMARK 500 3 ARG A 82 0.28 SIDE CHAIN
REMARK 500 3 ARG A 113 0.32 SIDE CHAIN
REMARK 500 4 ARG A 24 0.29 SIDE CHAIN
REMARK 500 4 ARG A 59 0.26 SIDE CHAIN
REMARK 500 4 ARG A 66 0.29 SIDE CHAIN
REMARK 500 4 ARG A 82 0.32 SIDE CHAIN
REMARK 500 4 ARG A 113 0.32 SIDE CHAIN
REMARK 500 5 ARG A 24 0.31 SIDE CHAIN
REMARK 500 5 ARG A 59 0.31 SIDE CHAIN
REMARK 500 5 ARG A 66 0.32 SIDE CHAIN
REMARK 500 5 ARG A 82 0.30 SIDE CHAIN
REMARK 500 5 ARG A 113 0.32 SIDE CHAIN
REMARK 500 6 ARG A 24 0.18 SIDE CHAIN
REMARK 500 6 ARG A 59 0.26 SIDE CHAIN
REMARK 500 6 ARG A 66 0.32 SIDE CHAIN
REMARK 500 6 ARG A 82 0.29 SIDE CHAIN
REMARK 500 6 ARG A 113 0.30 SIDE CHAIN
REMARK 500 7 ARG A 24 0.10 SIDE CHAIN
REMARK 500 7 ARG A 59 0.26 SIDE CHAIN
REMARK 500 7 ARG A 66 0.32 SIDE CHAIN
REMARK 500 7 ARG A 82 0.29 SIDE CHAIN
REMARK 500 7 ARG A 113 0.31 SIDE CHAIN
REMARK 500 8 ARG A 24 0.31 SIDE CHAIN
REMARK 500 8 ARG A 59 0.32 SIDE CHAIN
REMARK 500 8 ARG A 66 0.30 SIDE CHAIN
REMARK 500 8 ARG A 82 0.30 SIDE CHAIN
REMARK 500 8 ARG A 113 0.29 SIDE CHAIN
REMARK 500 9 ARG A 24 0.28 SIDE CHAIN
REMARK 500 9 ARG A 59 0.28 SIDE CHAIN
REMARK 500 9 ARG A 66 0.25 SIDE CHAIN
REMARK 500 9 ARG A 82 0.28 SIDE CHAIN
REMARK 500 9 ARG A 113 0.31 SIDE CHAIN
REMARK 500 10 ARG A 24 0.32 SIDE CHAIN
REMARK 500 10 ARG A 59 0.23 SIDE CHAIN
REMARK 500 10 ARG A 66 0.29 SIDE CHAIN
REMARK 500 10 ARG A 82 0.32 SIDE CHAIN
REMARK 500 10 ARG A 113 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 75 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CD1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CD2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CD3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1MAK A 1 113 UNP P01631 KV2G_MOUSE 1 113
SEQRES 1 A 113 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 A 113 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER
SEQRES 3 A 113 GLN SER LEU VAL HIS SER ASN GLY ASN THR TYR LEU ASN
SEQRES 4 A 113 TRP TYR LEU GLN LYS ALA GLY GLN SER PRO LYS LEU LEU
SEQRES 5 A 113 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP
SEQRES 6 A 113 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 A 113 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY ILE TYR
SEQRES 8 A 113 PHE CYS SER GLN THR THR HIS VAL PRO PRO THR PHE GLY
SEQRES 9 A 113 GLY GLY THR LYS LEU GLU ILE LYS ARG
SHEET 1 S1 4 VAL A 3 THR A 7 0
SHEET 2 S1 4 ASP A 17 SER A 26 -1 N SER A 26 O VAL A 3
SHEET 3 S1 4 ASP A 75 VAL A 83 -1 O PHE A 76 N CYS A 23
SHEET 4 S1 4 ARG A 66 SER A 72 -1 O ARG A 66 N SER A 81
SHEET 1 S2 5 LEU A 9 VAL A 13 0
SHEET 2 S2 5 THR A 102 ILE A 111 1 N LYS A 108 O LEU A 9
SHEET 3 S2 5 GLY A 89 SER A 94 -1 O GLY A 89 N LEU A 109
SHEET 4 S2 5 LEU A 38 GLN A 43 -1 O ASN A 39 N SER A 94
SHEET 5 S2 5 LYS A 50 VAL A 56 -1 N LYS A 50 O LEU A 42
SSBOND 1 CYS A 23 CYS A 93 1555 1555 2.02
CISPEP 1 THR A 7 PRO A 8 1 -2.10
CISPEP 2 VAL A 99 PRO A 100 1 -1.12
CISPEP 3 THR A 7 PRO A 8 2 -1.76
CISPEP 4 VAL A 99 PRO A 100 2 -0.84
CISPEP 5 THR A 7 PRO A 8 3 -1.06
CISPEP 6 VAL A 99 PRO A 100 3 -0.86
CISPEP 7 THR A 7 PRO A 8 4 -1.66
CISPEP 8 VAL A 99 PRO A 100 4 -0.44
CISPEP 9 THR A 7 PRO A 8 5 -2.19
CISPEP 10 VAL A 99 PRO A 100 5 -0.77
CISPEP 11 THR A 7 PRO A 8 6 -1.36
CISPEP 12 VAL A 99 PRO A 100 6 -0.88
CISPEP 13 THR A 7 PRO A 8 7 -2.22
CISPEP 14 VAL A 99 PRO A 100 7 -0.33
CISPEP 15 THR A 7 PRO A 8 8 -1.21
CISPEP 16 VAL A 99 PRO A 100 8 -0.73
CISPEP 17 THR A 7 PRO A 8 9 -1.16
CISPEP 18 VAL A 99 PRO A 100 9 -0.42
CISPEP 19 THR A 7 PRO A 8 10 -2.10
CISPEP 20 VAL A 99 PRO A 100 10 -1.12
CISPEP 21 THR A 7 PRO A 8 11 -1.54
CISPEP 22 VAL A 99 PRO A 100 11 -0.60
CISPEP 23 THR A 7 PRO A 8 12 -2.04
CISPEP 24 VAL A 99 PRO A 100 12 -0.19
CISPEP 25 THR A 7 PRO A 8 13 -0.95
CISPEP 26 VAL A 99 PRO A 100 13 -0.27
CISPEP 27 THR A 7 PRO A 8 14 -1.50
CISPEP 28 VAL A 99 PRO A 100 14 -0.78
CISPEP 29 THR A 7 PRO A 8 15 -1.03
CISPEP 30 VAL A 99 PRO A 100 15 -0.21
SITE 1 CD1 13 GLN A 27 SER A 28 LEU A 29 VAL A 30
SITE 2 CD1 13 HIS A 31 SER A 32 ASN A 33 GLY A 34
SITE 3 CD1 13 ASN A 35 THR A 36 TYR A 37 LEU A 38
SITE 4 CD1 13 ASN A 39
SITE 1 CD2 7 LYS A 55 VAL A 56 SER A 57 ASN A 58
SITE 2 CD2 7 ARG A 59 PHE A 60 SER A 61
SITE 1 CD3 9 SER A 94 GLN A 95 THR A 96 THR A 97
SITE 2 CD3 9 HIS A 98 VAL A 99 PRO A 100 PRO A 101
SITE 3 CD3 9 THR A 102
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 - v 29 2 Bytes