Header list of 3ci2.pdb file
Complete list - v 29 2 Bytes
HEADER SERINE PROTEASE INHIBITOR 10-SEP-91 3CI2
TITLE REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF BARLEY
TITLE 2 SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE STRUCTURES IN
TITLE 3 CRYSTALS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHYMOTRYPSIN INHIBITOR 2;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE;
SOURCE 3 ORGANISM_TAXID: 4513
KEYWDS SERINE PROTEASE INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.M.POULSEN
REVDAT 4 29-NOV-17 3CI2 1 REMARK HELIX
REVDAT 3 24-FEB-09 3CI2 1 VERSN
REVDAT 2 01-APR-03 3CI2 1 JRNL
REVDAT 1 31-OCT-93 3CI2 0
JRNL AUTH S.LUDVIGSEN,H.Y.SHEN,M.KJAER,J.C.MADSEN,F.M.POULSEN
JRNL TITL REFINEMENT OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF
JRNL TITL 2 BARLEY SERINE PROTEINASE INHIBITOR 2 AND COMPARISON WITH THE
JRNL TITL 3 STRUCTURES IN CRYSTALS.
JRNL REF J.MOL.BIOL. V. 222 621 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1748996
JRNL DOI 10.1016/0022-2836(91)90500-6
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.LUDVIGSEN,K.V.ANDERSEN,F.M.POULSEN
REMARK 1 TITL ACCURATE MEASUREMENTS OF COUPLING CONSTANTS FROM
REMARK 1 TITL 2 TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE SPECTRA OF
REMARK 1 TITL 3 PROTEINS AND DETERMINATION OF PHI-ANGLES
REMARK 1 REF J.MOL.BIOL. V. 217 731 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.SHEN,S.LUDVIGSEN,F.M.POULSEN
REMARK 1 TITL APPLICATION OF SYMMETRY PROJECTION OPERATORS TO MEASUREMENTS
REMARK 1 TITL 2 OF COUPLING CONSTANTS IN 2D NMR SPECTRA OF PROTEINS
REMARK 1 REF J.MAGN.RESON. V. 90 346 1990
REMARK 1 REFN ISSN 0022-2364
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.M.POULSEN,M.KJAER,G.M.CLORE,A.M.GRONENBORN
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF BARLEY SERINE PROTEINASE
REMARK 1 TITL 2 INHIBITOR-2 IN SOLUTION AS DETERMINED BY PROTON NUCLEAR
REMARK 1 TITL 3 MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF ALFRED BENZON SYMP. V. 26 234 1988
REMARK 1 REFN ISSN 0105-3639
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.M.CLORE,A.M.GRONENBORN,M.KJAER,F.M.POULSEN
REMARK 1 TITL THE DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF
REMARK 1 TITL 2 BARLEY SERINE PROTEINASE INHIBITOR 2 BY NUCLEAR MAGNETIC
REMARK 1 TITL 3 RESONANCE, DISTANCE GEOMETRY AND RESTRAINED MOLECULAR
REMARK 1 TITL 4 DYNAMICS
REMARK 1 REF PROTEIN ENG. V. 1 305 1987
REMARK 1 REFN ISSN 0269-2139
REMARK 1 REFERENCE 5
REMARK 1 AUTH G.M.CLORE,A.M.GRONENBORN,M.N.G.JAMES,M.KJAER,C.A.MCPHALEN,
REMARK 1 AUTH 2 F.M.POULSEN
REMARK 1 TITL COMPARISON OF THE SOLUTION AND X-RAY STRUCTURES OF BARLEY
REMARK 1 TITL 2 SERINE PROTEINASE INHIBITOR 2
REMARK 1 REF PROTEIN ENG. V. 1 313 1987
REMARK 1 REFN ISSN 0269-2139
REMARK 1 REFERENCE 6
REMARK 1 AUTH M.KJAER,F.M.POULSEN
REMARK 1 TITL SECONDARY STRUCTURE OF BARLEY SERINE PROTEINASE INHIBITOR 2
REMARK 1 TITL 2 DETERMINED BY PROTON NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF CARLSBERG RES.COMMUN. V. 52 355 1987
REMARK 1 REFN ISSN 0105-1938
REMARK 1 REFERENCE 7
REMARK 1 AUTH M.KJAER,S.LUDVIGSEN,O.W.SORENSEN,L.A.DENYS,J.KINDTLER,
REMARK 1 AUTH 2 F.M.POULSEN
REMARK 1 TITL SEQUENCE SPECIFIC ASSIGNMENT OF THE PROTON NUCLEAR MAGNETIC
REMARK 1 TITL 2 RESONANCE SPECTRUM OF BARLEY SERINE PROTEINASE INHIBITOR 2
REMARK 1 REF CARLSBERG RES.COMMUN. V. 52 327 1987
REMARK 1 REFN ISSN 0105-1938
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 3CI2 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_1000178912.
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 HIS A 18
REMARK 465 ASN A 19
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LEU A 20 N
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 24 CG TRP A 24 CD2 -0.106
REMARK 500 4 TRP A 24 CG TRP A 24 CD2 -0.113
REMARK 500 6 ARG A 81 CZ ARG A 81 NH2 -0.079
REMARK 500 7 TRP A 24 CG TRP A 24 CD2 -0.104
REMARK 500 8 TRP A 24 CG TRP A 24 CD2 -0.124
REMARK 500 9 TRP A 24 CG TRP A 24 CD2 -0.109
REMARK 500 12 TRP A 24 CG TRP A 24 CD2 -0.117
REMARK 500 13 TRP A 24 CG TRP A 24 CD2 -0.124
REMARK 500 15 TRP A 24 CG TRP A 24 CD2 -0.106
REMARK 500 16 TRP A 24 CG TRP A 24 CD2 -0.113
REMARK 500 17 TRP A 24 CG TRP A 24 CD2 -0.106
REMARK 500 18 TRP A 24 CG TRP A 24 CD2 -0.110
REMARK 500 19 TRP A 24 CG TRP A 24 CD2 -0.124
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 24 CB - CG - CD1 ANGL. DEV. = -9.1 DEGREES
REMARK 500 1 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 1 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 1 TRP A 24 NE1 - CE2 - CZ2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 1 ASP A 42 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 1 TYR A 61 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 1 TYR A 61 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 1 ARG A 65 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 ARG A 65 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 VAL A 66 CG1 - CB - CG2 ANGL. DEV. = -11.9 DEGREES
REMARK 500 1 ARG A 67 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ARG A 67 NE - CZ - NH2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 1 PHE A 69 CA - CB - CG ANGL. DEV. = -14.7 DEGREES
REMARK 500 1 PHE A 69 CB - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 1 PHE A 69 CB - CG - CD1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 1 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ILE A 76 CA - CB - CG1 ANGL. DEV. = -13.9 DEGREES
REMARK 500 1 ILE A 76 CA - C - N ANGL. DEV. = -16.9 DEGREES
REMARK 500 1 ALA A 77 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 1 VAL A 79 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 1 GLY A 83 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 2 TRP A 24 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 2 TRP A 24 CB - CG - CD1 ANGL. DEV. = -10.4 DEGREES
REMARK 500 2 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 2 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 2 TRP A 24 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 ARG A 62 NH1 - CZ - NH2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 2 ARG A 62 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 VAL A 66 CG1 - CB - CG2 ANGL. DEV. = -13.5 DEGREES
REMARK 500 2 ARG A 67 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 ASP A 71 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 2 ILE A 76 CA - CB - CG1 ANGL. DEV. = -14.3 DEGREES
REMARK 500 2 ALA A 77 CB - CA - C ANGL. DEV. = 13.3 DEGREES
REMARK 500 2 ALA A 77 N - CA - CB ANGL. DEV. = -17.0 DEGREES
REMARK 500 2 ARG A 81 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 TRP A 24 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 TRP A 24 CB - CG - CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500 3 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -7.3 DEGREES
REMARK 500 3 TRP A 24 CD1 - NE1 - CE2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 3 TRP A 24 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 3 ASP A 42 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 3 TYR A 61 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 ARG A 62 NH1 - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 3 ARG A 62 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 3 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 VAL A 66 CG1 - CB - CG2 ANGL. DEV. = -12.0 DEGREES
REMARK 500 3 PHE A 69 CA - CB - CG ANGL. DEV. = -17.2 DEGREES
REMARK 500 3 PHE A 69 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 399 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 LYS A 21 56.13 -100.47
REMARK 500 1 PRO A 44 -43.47 -14.72
REMARK 500 1 ALA A 46 96.90 -46.60
REMARK 500 1 THR A 55 66.16 -60.04
REMARK 500 1 VAL A 57 -147.83 -123.01
REMARK 500 1 MET A 59 34.70 -93.86
REMARK 500 1 ASP A 71 -146.89 -88.69
REMARK 500 1 ASP A 74 27.29 35.71
REMARK 500 1 VAL A 82 -111.42 -82.58
REMARK 500 2 TRP A 24 72.94 -117.00
REMARK 500 2 LYS A 43 78.69 -115.54
REMARK 500 2 PRO A 44 -52.67 -22.71
REMARK 500 2 ALA A 46 96.17 -65.15
REMARK 500 2 VAL A 53 142.31 -39.81
REMARK 500 2 THR A 55 -179.62 -54.39
REMARK 500 2 ILE A 56 99.77 -63.32
REMARK 500 2 GLU A 60 -163.23 -78.53
REMARK 500 2 ASP A 71 -138.39 -96.75
REMARK 500 2 ASP A 74 22.12 36.42
REMARK 500 3 PRO A 44 -54.18 -24.49
REMARK 500 3 ALA A 46 87.66 -60.22
REMARK 500 3 VAL A 53 130.65 -39.55
REMARK 500 3 VAL A 57 -51.31 -128.62
REMARK 500 3 MET A 59 -117.55 -94.11
REMARK 500 3 GLU A 60 -167.29 -76.54
REMARK 500 3 ASP A 71 -140.87 -97.35
REMARK 500 3 ASP A 74 19.00 37.49
REMARK 500 4 LYS A 21 45.63 -102.19
REMARK 500 4 THR A 22 31.22 -98.41
REMARK 500 4 LYS A 43 76.69 -116.70
REMARK 500 4 PRO A 44 -45.82 -24.24
REMARK 500 4 ALA A 46 88.20 -57.60
REMARK 500 4 THR A 55 62.95 -68.25
REMARK 500 4 ARG A 62 62.10 -116.43
REMARK 500 4 ASP A 71 -142.40 -95.43
REMARK 500 4 LEU A 73 38.05 -142.71
REMARK 500 4 ASP A 74 20.45 37.69
REMARK 500 5 PRO A 44 -57.41 -9.83
REMARK 500 5 ALA A 46 84.76 -57.74
REMARK 500 5 THR A 55 168.66 -47.61
REMARK 500 5 VAL A 57 -77.23 -114.91
REMARK 500 5 MET A 59 -128.31 -98.99
REMARK 500 5 ASP A 71 -140.62 -93.43
REMARK 500 5 ASP A 74 32.04 34.96
REMARK 500 6 LYS A 21 76.90 -100.45
REMARK 500 6 TRP A 24 71.93 -118.87
REMARK 500 6 GLU A 26 2.97 -66.06
REMARK 500 6 PRO A 44 -55.55 -9.79
REMARK 500 6 ALA A 46 97.75 -42.27
REMARK 500 6 THR A 55 85.53 -48.62
REMARK 500
REMARK 500 THIS ENTRY HAS 187 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 62 0.21 SIDE CHAIN
REMARK 500 1 ARG A 65 0.29 SIDE CHAIN
REMARK 500 1 ARG A 67 0.23 SIDE CHAIN
REMARK 500 1 ARG A 81 0.25 SIDE CHAIN
REMARK 500 2 ARG A 62 0.26 SIDE CHAIN
REMARK 500 2 ARG A 65 0.09 SIDE CHAIN
REMARK 500 2 ARG A 67 0.31 SIDE CHAIN
REMARK 500 2 ARG A 81 0.20 SIDE CHAIN
REMARK 500 3 ARG A 62 0.30 SIDE CHAIN
REMARK 500 3 ARG A 65 0.25 SIDE CHAIN
REMARK 500 3 ARG A 67 0.31 SIDE CHAIN
REMARK 500 3 ARG A 81 0.29 SIDE CHAIN
REMARK 500 4 ARG A 62 0.21 SIDE CHAIN
REMARK 500 4 ARG A 65 0.29 SIDE CHAIN
REMARK 500 4 ARG A 67 0.26 SIDE CHAIN
REMARK 500 4 ARG A 81 0.11 SIDE CHAIN
REMARK 500 5 ARG A 62 0.30 SIDE CHAIN
REMARK 500 5 ARG A 65 0.30 SIDE CHAIN
REMARK 500 5 ARG A 67 0.19 SIDE CHAIN
REMARK 500 6 ARG A 62 0.18 SIDE CHAIN
REMARK 500 6 ARG A 65 0.27 SIDE CHAIN
REMARK 500 6 ARG A 81 0.24 SIDE CHAIN
REMARK 500 7 ARG A 62 0.27 SIDE CHAIN
REMARK 500 7 ARG A 67 0.21 SIDE CHAIN
REMARK 500 7 ARG A 81 0.28 SIDE CHAIN
REMARK 500 8 ARG A 62 0.19 SIDE CHAIN
REMARK 500 8 ARG A 65 0.20 SIDE CHAIN
REMARK 500 8 ARG A 67 0.26 SIDE CHAIN
REMARK 500 8 ARG A 81 0.27 SIDE CHAIN
REMARK 500 9 ARG A 62 0.17 SIDE CHAIN
REMARK 500 9 ARG A 65 0.18 SIDE CHAIN
REMARK 500 9 ARG A 67 0.29 SIDE CHAIN
REMARK 500 9 ARG A 81 0.30 SIDE CHAIN
REMARK 500 10 ARG A 62 0.30 SIDE CHAIN
REMARK 500 10 ARG A 65 0.34 SIDE CHAIN
REMARK 500 10 ARG A 81 0.28 SIDE CHAIN
REMARK 500 11 ARG A 62 0.22 SIDE CHAIN
REMARK 500 11 ARG A 65 0.28 SIDE CHAIN
REMARK 500 11 ARG A 67 0.20 SIDE CHAIN
REMARK 500 11 ARG A 81 0.31 SIDE CHAIN
REMARK 500 12 ARG A 62 0.29 SIDE CHAIN
REMARK 500 12 ARG A 65 0.27 SIDE CHAIN
REMARK 500 12 ARG A 67 0.26 SIDE CHAIN
REMARK 500 13 ARG A 62 0.32 SIDE CHAIN
REMARK 500 13 ARG A 65 0.30 SIDE CHAIN
REMARK 500 13 ARG A 67 0.22 SIDE CHAIN
REMARK 500 13 ARG A 81 0.25 SIDE CHAIN
REMARK 500 14 ARG A 62 0.20 SIDE CHAIN
REMARK 500 14 ARG A 65 0.15 SIDE CHAIN
REMARK 500 14 ARG A 67 0.19 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 74 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3CI2 A 18 83 UNP P01053 ICI2_HORVU 18 83
SEQRES 1 A 66 HIS ASN LEU LYS THR GLU TRP PRO GLU LEU VAL GLY LYS
SEQRES 2 A 66 SER VAL GLU GLU ALA LYS LYS VAL ILE LEU GLN ASP LYS
SEQRES 3 A 66 PRO GLU ALA GLN ILE ILE VAL LEU PRO VAL GLY THR ILE
SEQRES 4 A 66 VAL THR MET GLU TYR ARG ILE ASP ARG VAL ARG LEU PHE
SEQRES 5 A 66 VAL ASP LYS LEU ASP ASN ILE ALA GLN VAL PRO ARG VAL
SEQRES 6 A 66 GLY
HELIX 1 A SER A 31 ASP A 42 1 12
SHEET 1 1A 4 THR A 22 TRP A 24 0
SHEET 2 1A 4 PRO A 80 VAL A 82 -1 N VAL A 82 O THR A 22
SHEET 3 1A 4 ASP A 64 ASP A 71 -1 O ARG A 67 N ARG A 81
SHEET 4 1A 4 GLN A 47 VAL A 53 1 N GLN A 47 O ASP A 64
SHEET 1 1B 4 LYS A 30 VAL A 32 0
SHEET 2 1B 4 ASP A 74 ILE A 76 -1 N ILE A 76 O LYS A 30
SHEET 3 1B 4 ASP A 64 ASP A 71 -1 N ASP A 71 O ASN A 75
SHEET 4 1B 4 GLN A 47 VAL A 53 1 N VAL A 53 O VAL A 70
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