Header list of 1kun.pdb file
Complete list - b 23 2 Bytes
HEADER EXTRACELLULAR MATRIX 04-MAR-97 1KUN
TITLE SOLUTION STRUCTURE OF THE HUMAN ALPHA3-CHAIN TYPE VI COLLAGEN C-
TITLE 2 TERMINAL KUNITZ DOMAIN, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA3-CHAIN TYPE VI COLLAGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL KUNITZ DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POTENTIAL;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: MT-663
KEYWDS COLLAGEN TYPE VI FRAGMENT, KUNITZ-TYPE DOMAIN, EXTRACELLULAR MATRIX,
KEYWDS 2 CONNECTIVE TISSUE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.D.SORENSEN,S.BJORN,K.NORRIS,O.OLSEN,L.PETERSEN,T.L.JAMES,J.J.LED
REVDAT 3 23-FEB-22 1KUN 1 REMARK
REVDAT 2 24-FEB-09 1KUN 1 VERSN
REVDAT 1 12-NOV-97 1KUN 0
JRNL AUTH M.D.SORENSEN,S.BJORN,K.NORRIS,O.OLSEN,L.PETERSEN,T.L.JAMES,
JRNL AUTH 2 J.J.LED
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE HUMAN
JRNL TITL 2 ALPHA3-CHAIN TYPE VI COLLAGEN C-TERMINAL KUNITZ DOMAIN,.
JRNL REF BIOCHEMISTRY V. 36 10439 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9265624
JRNL DOI 10.1021/BI9705570
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.D.SORENSEN,S.M.KRISTENSEN,S.BJORN,K.NORRIS,O.OLSEN,J.J.LED
REMARK 1 TITL ELUCIDATION OF THE ORIGIN OF MULTIPLE CONFORMATIONS OF THE
REMARK 1 TITL 2 HUMAN ALPHA 3-CHAIN TYPE VI COLLAGEN C-TERMINAL KUNITZ
REMARK 1 TITL 3 DOMAIN. THE REORIENTATION OF THE TRP21 RING
REMARK 1 REF J.BIOMOL.NMR V. 8 391 1996
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THREE-DIMENSIONAL STRUCTURE IN AQUEOUS
REMARK 3 SOLUTION AS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, DISTANCE
REMARK 3 GEOMETRY AND SIMULATED ANNEALING.
REMARK 4
REMARK 4 1KUN 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_1000174498.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3.0
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 : 500.13 MHZ
REMARK 210 SPECTROMETER MODEL : AM500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 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 2 ARG A 15 CZ ARG A 15 NH1 -0.079
REMARK 500 2 ARG A 15 CZ ARG A 15 NH2 -0.087
REMARK 500 3 ARG A 15 CZ ARG A 15 NH1 -0.080
REMARK 500 3 ARG A 15 CZ ARG A 15 NH2 -0.083
REMARK 500 4 ARG A 15 CZ ARG A 15 NH1 -0.079
REMARK 500 4 ARG A 32 CZ ARG A 32 NH2 -0.079
REMARK 500 5 ARG A 15 CZ ARG A 15 NH1 -0.087
REMARK 500 5 ARG A 15 CZ ARG A 15 NH2 -0.083
REMARK 500 7 ARG A 32 CZ ARG A 32 NH2 -0.087
REMARK 500 8 ARG A 32 CZ ARG A 32 NH1 -0.083
REMARK 500 9 ARG A 32 CZ ARG A 32 NH1 -0.078
REMARK 500 10 ARG A 15 CZ ARG A 15 NH1 -0.093
REMARK 500 10 ARG A 15 CZ ARG A 15 NH2 -0.079
REMARK 500 11 ARG A 15 CZ ARG A 15 NH2 -0.080
REMARK 500 12 ARG A 15 CZ ARG A 15 NH1 -0.080
REMARK 500 12 ARG A 15 CZ ARG A 15 NH2 -0.079
REMARK 500 13 ARG A 15 CZ ARG A 15 NH1 -0.079
REMARK 500 14 GLU A 1 CB GLU A 1 CG 0.124
REMARK 500 15 ARG A 15 CZ ARG A 15 NH2 -0.084
REMARK 500 16 ARG A 15 CZ ARG A 15 NH2 -0.079
REMARK 500 18 ARG A 15 CZ ARG A 15 NH2 -0.087
REMARK 500 18 ARG A 32 CZ ARG A 32 NH1 -0.082
REMARK 500 18 ARG A 32 CZ ARG A 32 NH2 -0.078
REMARK 500 19 ARG A 15 CZ ARG A 15 NH1 -0.084
REMARK 500 20 ARG A 15 CZ ARG A 15 NH1 -0.083
REMARK 500 20 ARG A 15 CZ ARG A 15 NH2 -0.082
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 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 1 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 1 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 1 TYR A 22 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 TYR A 22 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 TRP A 34 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 TRP A 34 CB - CG - CD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 1 TRP A 34 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 TRP A 34 CD1 - NE1 - CE2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 1 TRP A 34 NE1 - CE2 - CZ2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 2 GLU A 1 OE1 - CD - OE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ASP A 3 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 2 ASP A 3 N - CA - CB ANGL. DEV. = -16.9 DEGREES
REMARK 500 2 ASP A 3 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 2 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 2 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 2 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 2 ARG A 32 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 TRP A 34 CB - CG - CD1 ANGL. DEV. = -8.9 DEGREES
REMARK 500 2 TRP A 34 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 TRP A 34 CD1 - NE1 - CE2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 TRP A 34 NE1 - CE2 - CZ2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 ASP A 3 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 3 THR A 13 OG1 - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 3 ARG A 15 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 3 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 3 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 3 TRP A 34 CB - CG - CD1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 3 TRP A 34 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 3 TRP A 34 CD1 - NE1 - CE2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 ASN A 43 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 4 ASP A 3 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 4 CYS A 5 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 4 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 4 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 4 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 CYS A 30 CA - CB - SG ANGL. DEV. = 11.2 DEGREES
REMARK 500 4 ARG A 32 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 4 TRP A 34 CB - CG - CD1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 4 TRP A 34 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 4 TRP A 34 CD1 - NE1 - CE2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 5 ASP A 10 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 5 TRP A 21 CG - CD1 - NE1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 5 TRP A 21 CD1 - NE1 - CE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 5 TRP A 21 NE1 - CE2 - CZ2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 5 TRP A 34 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 5 TRP A 34 CD1 - NE1 - CE2 ANGL. DEV. = 7.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 193 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 ILE A 4 -29.79 -36.87
REMARK 500 1 GLU A 11 45.73 -89.58
REMARK 500 1 THR A 13 56.09 5.20
REMARK 500 1 CYS A 14 -144.30 -120.45
REMARK 500 1 PHE A 17 96.05 -33.75
REMARK 500 1 PRO A 25 -29.86 -34.83
REMARK 500 1 LYS A 28 36.71 93.82
REMARK 500 1 SER A 29 -158.49 -133.39
REMARK 500 1 ALA A 56 166.55 67.92
REMARK 500 2 ASP A 3 43.70 -107.07
REMARK 500 2 GLU A 11 49.74 -87.82
REMARK 500 2 CYS A 14 -170.25 -66.75
REMARK 500 2 PHE A 17 -70.01 -8.09
REMARK 500 2 ILE A 18 160.41 41.23
REMARK 500 2 LYS A 28 29.75 97.90
REMARK 500 2 SER A 29 -152.66 -135.60
REMARK 500 2 GLU A 42 -39.58 -35.94
REMARK 500 2 ASN A 43 74.68 -68.25
REMARK 500 2 LYS A 44 85.67 -150.06
REMARK 500 2 PRO A 57 62.80 -59.74
REMARK 500 3 THR A 2 40.01 20.06
REMARK 500 3 ASP A 3 -31.77 -26.59
REMARK 500 3 PRO A 8 -174.93 -69.72
REMARK 500 3 GLU A 11 -67.66 -120.21
REMARK 500 3 THR A 13 63.76 120.66
REMARK 500 3 CYS A 14 -69.24 -122.80
REMARK 500 3 ARG A 15 -32.03 127.43
REMARK 500 3 PRO A 25 -9.48 -43.42
REMARK 500 3 LYS A 28 33.22 85.06
REMARK 500 3 SER A 29 -155.96 -138.24
REMARK 500 3 CYS A 38 52.96 -98.67
REMARK 500 3 ASN A 41 -136.57 -111.22
REMARK 500 3 PRO A 57 62.67 -68.85
REMARK 500 4 ASP A 3 71.49 -119.41
REMARK 500 4 ILE A 4 -31.63 -39.86
REMARK 500 4 PRO A 8 -175.78 -54.57
REMARK 500 4 THR A 13 43.09 -90.49
REMARK 500 4 PHE A 17 101.54 -23.84
REMARK 500 4 PRO A 25 -31.55 -29.63
REMARK 500 4 SER A 29 -149.44 -131.57
REMARK 500 4 CYS A 38 -66.23 -132.82
REMARK 500 4 GLU A 42 -18.42 -48.69
REMARK 500 4 ALA A 56 42.29 -106.30
REMARK 500 5 THR A 2 34.86 -169.23
REMARK 500 5 ASP A 3 34.64 -57.69
REMARK 500 5 GLU A 11 -80.63 -120.30
REMARK 500 5 THR A 13 -73.38 -127.11
REMARK 500 5 PHE A 17 93.82 -22.31
REMARK 500 5 PRO A 25 -35.57 -32.65
REMARK 500 5 LYS A 28 28.63 91.78
REMARK 500
REMARK 500 THIS ENTRY HAS 252 RAMACHANDRAN OUTLIERS.
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 ALA A 56 PRO A 57 9 -147.48
REMARK 500 ALA A 56 PRO A 57 10 -144.15
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 15 0.30 SIDE CHAIN
REMARK 500 1 ARG A 32 0.29 SIDE CHAIN
REMARK 500 2 ARG A 15 0.31 SIDE CHAIN
REMARK 500 2 ARG A 32 0.29 SIDE CHAIN
REMARK 500 3 ARG A 15 0.26 SIDE CHAIN
REMARK 500 3 ARG A 32 0.30 SIDE CHAIN
REMARK 500 4 ARG A 15 0.09 SIDE CHAIN
REMARK 500 4 ARG A 32 0.29 SIDE CHAIN
REMARK 500 5 ARG A 15 0.24 SIDE CHAIN
REMARK 500 5 ARG A 32 0.29 SIDE CHAIN
REMARK 500 6 ARG A 15 0.30 SIDE CHAIN
REMARK 500 6 ARG A 32 0.26 SIDE CHAIN
REMARK 500 7 ARG A 15 0.30 SIDE CHAIN
REMARK 500 7 ARG A 32 0.30 SIDE CHAIN
REMARK 500 8 ARG A 15 0.30 SIDE CHAIN
REMARK 500 8 ARG A 32 0.22 SIDE CHAIN
REMARK 500 9 ARG A 15 0.30 SIDE CHAIN
REMARK 500 9 ARG A 32 0.29 SIDE CHAIN
REMARK 500 10 ARG A 15 0.27 SIDE CHAIN
REMARK 500 10 ARG A 32 0.30 SIDE CHAIN
REMARK 500 11 ARG A 15 0.30 SIDE CHAIN
REMARK 500 11 ARG A 32 0.23 SIDE CHAIN
REMARK 500 12 ARG A 15 0.30 SIDE CHAIN
REMARK 500 12 ARG A 32 0.28 SIDE CHAIN
REMARK 500 13 ARG A 32 0.29 SIDE CHAIN
REMARK 500 14 ARG A 15 0.30 SIDE CHAIN
REMARK 500 14 ARG A 32 0.29 SIDE CHAIN
REMARK 500 15 ARG A 15 0.17 SIDE CHAIN
REMARK 500 15 ARG A 32 0.30 SIDE CHAIN
REMARK 500 16 ARG A 15 0.28 SIDE CHAIN
REMARK 500 16 ARG A 32 0.24 SIDE CHAIN
REMARK 500 17 ARG A 15 0.21 SIDE CHAIN
REMARK 500 17 ARG A 32 0.28 SIDE CHAIN
REMARK 500 18 ARG A 15 0.20 SIDE CHAIN
REMARK 500 18 ARG A 32 0.22 SIDE CHAIN
REMARK 500 19 ARG A 15 0.28 SIDE CHAIN
REMARK 500 19 ARG A 32 0.28 SIDE CHAIN
REMARK 500 20 ARG A 15 0.27 SIDE CHAIN
REMARK 500 20 ARG A 32 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KUN A 1 58 UNP P12111 CO6A3_HUMAN 3107 3164
SEQRES 1 A 58 GLU THR ASP ILE CYS LYS LEU PRO LYS ASP GLU GLY THR
SEQRES 2 A 58 CYS ARG ASP PHE ILE LEU LYS TRP TYR TYR ASP PRO ASN
SEQRES 3 A 58 THR LYS SER CYS ALA ARG PHE TRP TYR GLY GLY CYS GLY
SEQRES 4 A 58 GLY ASN GLU ASN LYS PHE GLY SER GLN LYS GLU CYS GLU
SEQRES 5 A 58 LYS VAL CYS ALA PRO VAL
HELIX 1 H1 THR A 2 LEU A 7 5 6
HELIX 2 H2 SER A 47 CYS A 55 1 9
SHEET 1 S1 3 SER A 29 TYR A 35 0
SHEET 2 S1 3 ILE A 18 ASP A 24 -1 N LYS A 20 O PHE A 33
SHEET 3 S1 3 PHE A 45 PHE A 45 -1 N PHE A 45 O TRP A 21
SSBOND 1 CYS A 5 CYS A 55 1555 1555 2.02
SSBOND 2 CYS A 14 CYS A 38 1555 1555 2.02
SSBOND 3 CYS A 30 CYS A 51 1555 1555 2.01
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 - b 23 2 Bytes