Header list of 1mhj.pdb file
Complete list - v 29 2 Bytes
HEADER HORMONE 30-NOV-94 1MHJ
TITLE SOLUTION STRUCTURE OF THE SUPERACTIVE MONOMERIC DES-[PHE(B25)] HUMAN
TITLE 2 INSULIN MUTANT. ELUCIDATION OF THE STRUCTURAL BASIS FOR THE
TITLE 3 MONOMERIZATION OF THE DES-[PHE(B25)] INSULIN AND THE DIMERIZATION OF
TITLE 4 NATIVE INSULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INSULIN;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HORMONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.M.M.JORGENSEN,H.B.OLSEN,J.J.LED,P.BALSCHMIDT
REVDAT 3 29-NOV-17 1MHJ 1 REMARK HELIX
REVDAT 2 24-FEB-09 1MHJ 1 VERSN
REVDAT 1 15-OCT-95 1MHJ 0
JRNL AUTH A.M.JORGENSEN,H.B.OLSEN,P.BALSCHMIDT,J.J.LED
JRNL TITL SOLUTION STRUCTURE OF THE SUPERACTIVE MONOMERIC
JRNL TITL 2 DES-[PHE(B25)] HUMAN INSULIN MUTANT: ELUCIDATION OF THE
JRNL TITL 3 STRUCTURAL BASIS FOR THE MONOMERIZATION OF DES-[PHE(B25)]
JRNL TITL 4 INSULIN AND THE DIMERIZATION OF NATIVE INSULIN.
JRNL REF J.MOL.BIOL. V. 257 684 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8648633
JRNL DOI 10.1006/JMBI.1996.0194
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.M.KRISTENSEN,J.J.LED
REMARK 1 TITL A CARBON-13 NMR STUDY OF THE B9(ASP) MUTANT OF HUMAN INSULIN
REMARK 1 REF MAGN.RESON.CHEM. V. 33 461 1995
REMARK 1 REFN ISSN 0749-1581
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.D.SORENSEN,J.J.LED
REMARK 1 TITL STRUCTURAL DETAILS OF ASP(B9) HUMAN INSULIN AT LOW PH FROM
REMARK 1 TITL 2 2D NMR TITRATION STUDIES
REMARK 1 REF BIOCHEMISTRY V. 33 13727 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.MOSS,H.GESMAR,J.J.LED
REMARK 1 TITL A NEW LINEAR PREDICTION MODEL METHOD FOR THE DETERMINATION
REMARK 1 TITL 2 OF SLOW AMIDE PROTON EXCHANGE RATES FROM A SERIES OF
REMARK 1 TITL 3 ONE-DIMENSIONAL 1H NMR SPECTRA
REMARK 1 REF J.AM.CHEM.SOC. V. 116 747 1994
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 4
REMARK 1 AUTH H.B.OLSEN,H.GESMAR,J.J.LED
REMARK 1 TITL SLOW AMIDE PROTON EXCHANGE RATES FROM THE LINE WIDTHS IN A
REMARK 1 TITL 2 SINGLE TWO-DIMENSIONAL 1H NMR SPECTRUM
REMARK 1 REF J.AM.CHEM.SOC. V. 115 1457 1993
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 5
REMARK 1 AUTH A.M.M.JORGENSEN,S.M.KRISTENSEN,J.J.LED,P.BALSCHMIDT
REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN INSULIN DIMER. A
REMARK 1 TITL 2 STUDY OF THE B9(ASP) MUTANT OF HUMAN INSULIN USING NUCLEAR
REMARK 1 TITL 3 MAGNETIC RESONANCE DISTANCE GEOMETRY AND RESTRAINED
REMARK 1 TITL 4 MOLECULAR DYNAMICS
REMARK 1 REF J.MOL.BIOL. V. 227 1146 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 6
REMARK 1 AUTH S.M.KRISTENSEN,A.M.M.JORGENSEN,J.J.LED,P.BALSCHMIDT,
REMARK 1 AUTH 2 F.B.HANSEN
REMARK 1 TITL PROTON NUCLEAR MAGNETIC RESONANCE STUDY OF THE B9(ASP)
REMARK 1 TITL 2 MUTANT OF HUMAN INSULIN. SEQUENTIAL ASSIGNMENT AND SECONDARY
REMARK 1 TITL 3 STRUCTURE
REMARK 1 REF J.MOL.BIOL. V. 218 221 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISGEO, X-PLOR 2.1
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MHJ 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_1000175003.
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: DIMERIC
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: 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 B 5 CG HIS B 5 ND1 -0.098
REMARK 500 1 ARG B 22 NE ARG B 22 CZ -0.087
REMARK 500 1 ARG B 22 CZ ARG B 22 NH2 -0.081
REMARK 500 2 HIS B 5 CG HIS B 5 ND1 -0.092
REMARK 500 3 HIS B 5 CG HIS B 5 ND1 -0.094
REMARK 500 3 GLY B 20 N GLY B 20 CA 0.094
REMARK 500 3 ARG B 22 CZ ARG B 22 NH1 -0.098
REMARK 500 3 ARG B 22 CZ ARG B 22 NH2 -0.079
REMARK 500 4 HIS B 5 CG HIS B 5 ND1 -0.099
REMARK 500 4 ARG B 22 CZ ARG B 22 NH1 -0.081
REMARK 500 4 ARG B 22 CZ ARG B 22 NH2 -0.085
REMARK 500 5 HIS B 5 CG HIS B 5 ND1 -0.093
REMARK 500 5 ARG B 22 CZ ARG B 22 NH1 -0.091
REMARK 500 6 HIS B 5 CG HIS B 5 ND1 -0.098
REMARK 500 6 ARG B 22 CZ ARG B 22 NH1 -0.083
REMARK 500 7 HIS B 5 CG HIS B 5 ND1 -0.104
REMARK 500 7 ARG B 22 CZ ARG B 22 NH2 -0.079
REMARK 500 8 HIS B 5 CG HIS B 5 ND1 -0.099
REMARK 500 8 ARG B 22 CZ ARG B 22 NH1 -0.084
REMARK 500 8 ARG B 22 CZ ARG B 22 NH2 -0.082
REMARK 500 9 HIS B 5 CG HIS B 5 ND1 -0.097
REMARK 500 9 ARG B 22 CZ ARG B 22 NH1 -0.081
REMARK 500 9 ARG B 22 CZ ARG B 22 NH2 -0.078
REMARK 500 10 HIS B 5 CG HIS B 5 ND1 -0.094
REMARK 500 10 ARG B 22 CZ ARG B 22 NH1 -0.090
REMARK 500 10 ARG B 22 CZ ARG B 22 NH2 -0.087
REMARK 500 11 HIS B 5 NE2 HIS B 5 CD2 -0.077
REMARK 500 11 ARG B 22 CZ ARG B 22 NH1 -0.085
REMARK 500 11 ARG B 22 CZ ARG B 22 NH2 -0.084
REMARK 500 12 HIS B 5 CG HIS B 5 ND1 -0.095
REMARK 500 12 ARG B 22 CZ ARG B 22 NH1 -0.089
REMARK 500 12 ARG B 22 CZ ARG B 22 NH2 -0.078
REMARK 500 13 HIS B 5 CG HIS B 5 ND1 -0.092
REMARK 500 13 ARG B 22 CZ ARG B 22 NH1 -0.080
REMARK 500 13 ARG B 22 CZ ARG B 22 NH2 -0.078
REMARK 500 14 HIS B 5 CG HIS B 5 ND1 -0.090
REMARK 500 15 HIS B 5 CG HIS B 5 ND1 -0.092
REMARK 500 15 ARG B 22 CZ ARG B 22 NH1 -0.081
REMARK 500 15 ARG B 22 CZ ARG B 22 NH2 -0.086
REMARK 500 16 HIS B 5 CG HIS B 5 ND1 -0.099
REMARK 500 16 ARG B 22 CZ ARG B 22 NH1 -0.080
REMARK 500 18 HIS B 5 CG HIS B 5 ND1 -0.097
REMARK 500 18 ARG B 22 CZ ARG B 22 NH1 -0.080
REMARK 500 18 ARG B 22 CZ ARG B 22 NH2 -0.079
REMARK 500 19 HIS B 5 CG HIS B 5 ND1 -0.097
REMARK 500 19 ARG B 22 CZ ARG B 22 NH2 -0.078
REMARK 500 20 HIS B 5 CG HIS B 5 ND1 -0.104
REMARK 500 20 ARG B 22 CZ ARG B 22 NH2 -0.085
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 CYS A 7 CA - CB - SG ANGL. DEV. = 12.0 DEGREES
REMARK 500 1 ARG B 22 NH1 - CZ - NH2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 1 ARG B 22 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 PHE B 24 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 PHE B 24 N - CA - C ANGL. DEV. = 19.7 DEGREES
REMARK 500 2 PHE B 24 CA - CB - CG ANGL. DEV. = -14.5 DEGREES
REMARK 500 3 THR A 8 OG1 - CB - CG2 ANGL. DEV. = -15.0 DEGREES
REMARK 500 3 CYS A 20 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 3 ARG B 22 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 PHE B 24 CA - CB - CG ANGL. DEV. = -15.5 DEGREES
REMARK 500 4 CYS A 11 CA - CB - SG ANGL. DEV. = 13.9 DEGREES
REMARK 500 4 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 4 TYR A 19 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 4 CYS A 20 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 4 TYR B 25 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 4 TYR B 25 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 5 CYS A 7 CA - CB - SG ANGL. DEV. = 9.4 DEGREES
REMARK 500 5 CYS A 11 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 5 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 5 TYR B 16 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 6 CYS A 11 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 6 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 6 TYR A 19 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 CYS A 20 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 6 ARG B 22 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 6 PHE B 24 CA - CB - CG ANGL. DEV. = -15.6 DEGREES
REMARK 500 6 PHE B 24 N - CA - C ANGL. DEV. = 17.3 DEGREES
REMARK 500 6 TYR B 25 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 TYR A 19 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 7 LEU B 15 CB - CG - CD1 ANGL. DEV. = -10.7 DEGREES
REMARK 500 7 TYR B 16 CA - CB - CG ANGL. DEV. = -14.8 DEGREES
REMARK 500 7 GLU B 21 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 7 PHE B 24 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 9 CYS A 7 CA - CB - SG ANGL. DEV. = 11.1 DEGREES
REMARK 500 9 CYS A 11 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 9 TYR A 19 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 9 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 9 CYS A 20 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 9 TYR B 16 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 9 TYR B 16 CA - CB - CG ANGL. DEV. = 12.6 DEGREES
REMARK 500 9 TYR B 16 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 9 ARG B 22 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 9 PHE B 24 CA - CB - CG ANGL. DEV. = -14.4 DEGREES
REMARK 500 9 PHE B 24 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 10 THR A 8 OG1 - CB - CG2 ANGL. DEV. = -13.9 DEGREES
REMARK 500 10 CYS A 11 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 10 TYR B 16 CB - CG - CD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 10 TYR B 16 CB - CG - CD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 11 SER A 9 CA - C - N ANGL. DEV. = -14.6 DEGREES
REMARK 500 11 ILE A 10 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 2 -48.71 -12.42
REMARK 500 1 ILE A 10 8.96 38.33
REMARK 500 1 CYS A 11 93.00 3.69
REMARK 500 1 SER A 12 -158.80 -126.70
REMARK 500 1 LEU A 13 -72.91 -42.18
REMARK 500 1 TYR A 14 -39.54 -39.10
REMARK 500 1 GLN A 15 -74.12 -60.63
REMARK 500 1 CYS A 20 92.97 -23.96
REMARK 500 1 ASN B 3 57.90 10.78
REMARK 500 1 HIS B 5 163.34 59.56
REMARK 500 1 ALA B 14 -72.49 -39.83
REMARK 500 1 CYS B 19 25.36 -167.98
REMARK 500 1 PHE B 24 163.61 -22.68
REMARK 500 1 TYR B 25 -3.19 107.07
REMARK 500 1 THR B 26 60.47 -115.53
REMARK 500 2 THR A 8 -111.07 -108.21
REMARK 500 2 SER A 9 -56.91 -1.72
REMARK 500 2 ILE A 10 157.47 127.90
REMARK 500 2 CYS A 11 -158.53 -105.91
REMARK 500 2 SER A 12 162.74 172.67
REMARK 500 2 CYS A 20 -87.24 -18.29
REMARK 500 2 VAL B 2 60.03 128.44
REMARK 500 2 ASN B 3 76.72 -54.40
REMARK 500 2 GLN B 4 -25.32 172.49
REMARK 500 2 HIS B 5 162.66 80.92
REMARK 500 2 CYS B 7 -58.65 34.23
REMARK 500 2 TYR B 16 -50.87 -29.94
REMARK 500 2 CYS B 19 -31.53 -140.93
REMARK 500 2 GLU B 21 -37.94 -23.51
REMARK 500 2 PHE B 24 61.32 -155.16
REMARK 500 2 TYR B 25 -43.45 -8.21
REMARK 500 2 THR B 26 143.09 87.90
REMARK 500 2 LYS B 28 130.08 133.58
REMARK 500 3 ILE A 2 -63.40 1.93
REMARK 500 3 VAL A 3 -90.53 -40.32
REMARK 500 3 SER A 12 -166.27 -129.57
REMARK 500 3 LEU A 13 -90.44 -13.79
REMARK 500 3 CYS A 20 -128.18 -86.25
REMARK 500 3 GLN B 4 -34.51 -140.98
REMARK 500 3 HIS B 5 113.16 3.84
REMARK 500 3 CYS B 7 79.50 -9.22
REMARK 500 3 SER B 9 -77.01 -37.56
REMARK 500 3 HIS B 10 -46.49 -27.13
REMARK 500 3 GLU B 21 74.34 -57.71
REMARK 500 3 ARG B 22 -77.63 172.95
REMARK 500 3 PHE B 24 86.51 -151.38
REMARK 500 3 TYR B 25 23.88 -60.20
REMARK 500 3 THR B 26 58.99 30.68
REMARK 500 3 PRO B 27 116.07 -11.33
REMARK 500 3 LYS B 28 -165.98 -125.60
REMARK 500
REMARK 500 THIS ENTRY HAS 301 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 THR B 26 PRO B 27 19 -148.44
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 B 22 0.27 SIDE CHAIN
REMARK 500 2 ARG B 22 0.26 SIDE CHAIN
REMARK 500 3 ARG B 22 0.21 SIDE CHAIN
REMARK 500 4 ARG B 22 0.29 SIDE CHAIN
REMARK 500 5 ARG B 22 0.20 SIDE CHAIN
REMARK 500 6 ARG B 22 0.22 SIDE CHAIN
REMARK 500 7 ARG B 22 0.27 SIDE CHAIN
REMARK 500 8 ARG B 22 0.30 SIDE CHAIN
REMARK 500 9 ARG B 22 0.16 SIDE CHAIN
REMARK 500 10 ARG B 22 0.21 SIDE CHAIN
REMARK 500 11 ARG B 22 0.31 SIDE CHAIN
REMARK 500 12 ARG B 22 0.28 SIDE CHAIN
REMARK 500 13 ARG B 22 0.29 SIDE CHAIN
REMARK 500 14 ARG B 22 0.13 SIDE CHAIN
REMARK 500 15 ARG B 22 0.12 SIDE CHAIN
REMARK 500 16 ARG B 22 0.29 SIDE CHAIN
REMARK 500 17 ARG B 22 0.13 SIDE CHAIN
REMARK 500 18 ARG B 22 0.30 SIDE CHAIN
REMARK 500 19 ARG B 22 0.26 SIDE CHAIN
REMARK 500 20 ARG B 22 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MHJ A 1 21 UNP P01308 INS_HUMAN 90 110
DBREF 1MHJ B 1 29 UNP P01308 INS_HUMAN 25 48
SEQADV 1MHJ B UNP P01308 PHE 48 DELETION
SEQRES 1 A 21 GLY ILE VAL GLU GLN CYS CYS THR SER ILE CYS SER LEU
SEQRES 2 A 21 TYR GLN LEU GLU ASN TYR CYS ASN
SEQRES 1 B 29 PHE VAL ASN GLN HIS LEU CYS GLY SER HIS LEU VAL GLU
SEQRES 2 B 29 ALA LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE TYR THR
SEQRES 3 B 29 PRO LYS THR
HELIX 1 A1 ILE A 2 THR A 8 1ALPHA HELIX 7
HELIX 2 A2 LEU A 13 CYS A 20 1ALPHA HELIX 8
HELIX 3 B1 GLY B 8 CYS B 19 1ALPHA HELIX 12
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.02
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.02
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