Header list of 1hmf.pdb file
Complete list - b 23 2 Bytes
HEADER DNA-BINDING 07-MAR-94 1HMF
TITLE STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH MOBILITY GROUP PROTEIN FRAGMENT-B;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116
KEYWDS DNA-BINDING
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR H.M.WEIR,P.J.KRAULIS,C.S.HILL,A.R.C.RAINE,E.D.LAUE,J.O.THOMAS
REVDAT 4 23-FEB-22 1HMF 1 REMARK
REVDAT 3 24-FEB-09 1HMF 1 VERSN
REVDAT 2 01-APR-03 1HMF 1 JRNL
REVDAT 1 31-MAY-94 1HMF 0
JRNL AUTH H.M.WEIR,P.J.KRAULIS,C.S.HILL,A.R.RAINE,E.D.LAUE,J.O.THOMAS
JRNL TITL STRUCTURE OF THE HMG BOX MOTIF IN THE B-DOMAIN OF HMG1.
JRNL REF EMBO J. V. 12 1311 1993
JRNL REFN ISSN 0261-4189
JRNL PMID 8467791
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HMF 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_1000173911.
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 : 30
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: 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
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 HIS A 29 CG HIS A 29 ND1 -0.126
REMARK 500 1 TRP A 45 CG TRP A 45 CD2 -0.115
REMARK 500 2 HIS A 29 CG HIS A 29 ND1 -0.122
REMARK 500 2 TRP A 45 CG TRP A 45 CD2 -0.128
REMARK 500 3 HIS A 29 CG HIS A 29 ND1 -0.123
REMARK 500 3 TRP A 45 CG TRP A 45 CD2 -0.118
REMARK 500 4 HIS A 29 CG HIS A 29 ND1 -0.124
REMARK 500 4 TRP A 45 CG TRP A 45 CD2 -0.116
REMARK 500 5 HIS A 29 CG HIS A 29 ND1 -0.122
REMARK 500 5 TRP A 45 CG TRP A 45 CD2 -0.128
REMARK 500 6 HIS A 29 CG HIS A 29 ND1 -0.122
REMARK 500 6 TRP A 45 CG TRP A 45 CD2 -0.131
REMARK 500 7 HIS A 29 CG HIS A 29 ND1 -0.122
REMARK 500 7 TRP A 45 CG TRP A 45 CD2 -0.121
REMARK 500 8 HIS A 29 CG HIS A 29 ND1 -0.125
REMARK 500 8 TRP A 45 CG TRP A 45 CD2 -0.121
REMARK 500 9 HIS A 29 CG HIS A 29 ND1 -0.123
REMARK 500 9 TRP A 45 CG TRP A 45 CD2 -0.129
REMARK 500 10 HIS A 29 CG HIS A 29 ND1 -0.121
REMARK 500 10 TRP A 45 CG TRP A 45 CD2 -0.127
REMARK 500 11 HIS A 29 CG HIS A 29 ND1 -0.124
REMARK 500 11 TRP A 45 CG TRP A 45 CD2 -0.123
REMARK 500 12 HIS A 29 CG HIS A 29 ND1 -0.120
REMARK 500 12 TRP A 45 CG TRP A 45 CD2 -0.116
REMARK 500 13 HIS A 29 CG HIS A 29 ND1 -0.123
REMARK 500 13 TRP A 45 CG TRP A 45 CD2 -0.125
REMARK 500 14 HIS A 29 CG HIS A 29 ND1 -0.121
REMARK 500 14 TRP A 45 CG TRP A 45 CD2 -0.124
REMARK 500 15 HIS A 29 CG HIS A 29 ND1 -0.121
REMARK 500 15 TRP A 45 CG TRP A 45 CD2 -0.122
REMARK 500 16 HIS A 29 CG HIS A 29 ND1 -0.122
REMARK 500 16 TRP A 45 CG TRP A 45 CD2 -0.130
REMARK 500 17 HIS A 29 CG HIS A 29 ND1 -0.125
REMARK 500 17 TRP A 45 CG TRP A 45 CD2 -0.121
REMARK 500 18 HIS A 29 CG HIS A 29 ND1 -0.124
REMARK 500 18 TRP A 45 CG TRP A 45 CD2 -0.123
REMARK 500 19 HIS A 29 CG HIS A 29 ND1 -0.123
REMARK 500 19 TRP A 45 CG TRP A 45 CD2 -0.122
REMARK 500 20 HIS A 29 CG HIS A 29 ND1 -0.125
REMARK 500 20 TRP A 45 CG TRP A 45 CD2 -0.121
REMARK 500 21 HIS A 29 CG HIS A 29 ND1 -0.123
REMARK 500 21 TRP A 45 CG TRP A 45 CD2 -0.124
REMARK 500 22 HIS A 29 CG HIS A 29 ND1 -0.123
REMARK 500 22 TRP A 45 CG TRP A 45 CD2 -0.122
REMARK 500 23 HIS A 29 CG HIS A 29 ND1 -0.125
REMARK 500 23 TRP A 45 CG TRP A 45 CD2 -0.116
REMARK 500 24 HIS A 29 CG HIS A 29 ND1 -0.126
REMARK 500 24 TRP A 45 CG TRP A 45 CD2 -0.120
REMARK 500 25 HIS A 29 CG HIS A 29 ND1 -0.121
REMARK 500 25 TRP A 45 CG TRP A 45 CD2 -0.128
REMARK 500
REMARK 500 THIS ENTRY HAS 60 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 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 TRP A 45 CD1 - NE1 - CE2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 1 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 2 TRP A 45 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 2 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 2 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 3 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 4 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 4 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 5 TRP A 45 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 5 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 5 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 6 TRP A 45 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 6 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 6 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 6 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 7 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 7 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 7 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 8 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 8 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 8 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 9 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 9 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 9 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 9 TRP A 45 CG - CD2 - CE3 ANGL. DEV. = -5.5 DEGREES
REMARK 500 10 TRP A 45 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 10 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 10 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 10 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 11 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 11 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 11 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 12 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 12 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 12 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 13 TRP A 45 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 13 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 13 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 13 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 14 TRP A 45 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 14 TRP A 45 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 14 TRP A 45 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 14 TRP A 45 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 104 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 ASP A 3 65.36 -154.36
REMARK 500 1 PRO A 4 -91.36 -80.75
REMARK 500 1 ASN A 5 1.48 -69.96
REMARK 500 1 ALA A 6 86.34 -18.80
REMARK 500 1 PRO A 7 -154.20 -86.64
REMARK 500 1 PRO A 11 -151.32 -84.99
REMARK 500 1 PHE A 14 -6.50 -57.41
REMARK 500 1 PRO A 30 74.58 -66.01
REMARK 500 1 TYR A 67 -77.33 -61.06
REMARK 500 1 GLU A 68 -7.55 -48.63
REMARK 500 1 TYR A 74 -143.54 -71.74
REMARK 500 2 LYS A 2 -161.11 -117.40
REMARK 500 2 ASP A 3 156.92 -43.82
REMARK 500 2 PRO A 4 -159.12 -48.50
REMARK 500 2 ALA A 6 140.39 -21.20
REMARK 500 2 PRO A 7 -155.87 -82.29
REMARK 500 2 PRO A 10 164.99 -42.73
REMARK 500 2 PRO A 11 -149.29 -75.21
REMARK 500 2 PRO A 30 82.80 -65.87
REMARK 500 2 TYR A 67 -89.02 -50.68
REMARK 500 2 GLU A 68 -11.94 -43.43
REMARK 500 2 ILE A 71 -23.97 -35.33
REMARK 500 2 TYR A 74 -139.50 -61.73
REMARK 500 2 ARG A 75 51.80 26.44
REMARK 500 2 ALA A 76 178.02 -57.62
REMARK 500 3 LYS A 2 36.44 -163.20
REMARK 500 3 PRO A 4 -83.42 -65.84
REMARK 500 3 ALA A 6 106.86 -51.58
REMARK 500 3 PRO A 7 -155.40 -108.46
REMARK 500 3 PRO A 11 -148.28 -77.55
REMARK 500 3 SER A 19 -34.74 -38.58
REMARK 500 3 PRO A 30 71.61 -68.25
REMARK 500 3 ALA A 49 159.44 -46.58
REMARK 500 3 TYR A 67 -84.74 -47.23
REMARK 500 3 GLU A 68 -6.64 -43.89
REMARK 500 3 ALA A 76 87.70 -169.73
REMARK 500 4 PRO A 4 -155.91 -58.16
REMARK 500 4 ALA A 6 89.47 -23.45
REMARK 500 4 PRO A 7 -155.03 -94.11
REMARK 500 4 PRO A 11 -149.23 -85.69
REMARK 500 4 PRO A 30 76.38 -66.28
REMARK 500 4 TYR A 67 -80.85 -57.70
REMARK 500 4 GLU A 68 -7.54 -47.77
REMARK 500 4 TYR A 74 -133.81 -76.57
REMARK 500 4 ARG A 75 117.08 -36.01
REMARK 500 4 ALA A 76 82.91 -167.43
REMARK 500 5 ASP A 3 164.79 -44.90
REMARK 500 5 PRO A 4 -85.50 -52.34
REMARK 500 5 ALA A 6 100.41 -31.74
REMARK 500 5 PRO A 7 -155.60 -95.87
REMARK 500
REMARK 500 THIS ENTRY HAS 316 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 2 TYR A 67 0.06 SIDE CHAIN
REMARK 500 13 ARG A 9 0.18 SIDE CHAIN
REMARK 500 13 ARG A 22 0.29 SIDE CHAIN
REMARK 500 13 ARG A 75 0.29 SIDE CHAIN
REMARK 500 14 ARG A 9 0.29 SIDE CHAIN
REMARK 500 14 ARG A 22 0.32 SIDE CHAIN
REMARK 500 14 ARG A 75 0.19 SIDE CHAIN
REMARK 500 15 ARG A 9 0.12 SIDE CHAIN
REMARK 500 15 ARG A 22 0.23 SIDE CHAIN
REMARK 500 15 ARG A 75 0.11 SIDE CHAIN
REMARK 500 18 TYR A 74 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HME RELATED DB: PDB
DBREF 1HMF A 1 77 UNP P63159 HMG1_RAT 88 164
SEQRES 1 A 77 PHE LYS ASP PRO ASN ALA PRO LYS ARG PRO PRO SER ALA
SEQRES 2 A 77 PHE PHE LEU PHE CYS SER GLU TYR ARG PRO LYS ILE LYS
SEQRES 3 A 77 GLY GLU HIS PRO GLY LEU SER ILE GLY ASP VAL ALA LYS
SEQRES 4 A 77 LYS LEU GLY GLU MET TRP ASN ASN THR ALA ALA ASP ASP
SEQRES 5 A 77 LYS GLN PRO TYR GLU LYS LYS ALA ALA LYS LEU LYS GLU
SEQRES 6 A 77 LYS TYR GLU LYS ASP ILE ALA ALA TYR ARG ALA LYS
HELIX 1 H1 ALA A 13 HIS A 29 1BENT ROUND H2 17
HELIX 2 H2 ILE A 34 THR A 48 1 15
HELIX 3 H3 ALA A 50 TYR A 74 1 25
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