Header list of 1rmj.pdb file
Complete list - r 2 2 Bytes
HEADER HORMONE/GROWTH FACTOR 28-NOV-03 1RMJ
TITLE C-TERMINAL DOMAIN OF INSULIN-LIKE GROWTH FACTOR (IGF) BINDING PROTEIN-
TITLE 2 6: STRUCTURE AND INTERACTION WITH IGF-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, SEQUENCE DATABASE RESIUDE 161-240;
COMPND 5 SYNONYM: IGFBP-6, IBP-6, IGF-BINDING PROTEIN 6;
COMPND 6 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: IGFBP6, IBP6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB
KEYWDS INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN, HORMONE-GROWTH FACTOR
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.J.HEADEY,D.W.KEIZER,S.YAO,G.BRASIER,P.KANTHARIDIS,L.A.BACH,
AUTHOR 2 R.S.NORTON
REVDAT 4 02-MAR-22 1RMJ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1RMJ 1 VERSN
REVDAT 2 09-NOV-04 1RMJ 1 JRNL AUTHOR
REVDAT 1 14-SEP-04 1RMJ 0
JRNL AUTH S.J.HEADEY,D.W.KEIZER,S.YAO,G.BRASIER,P.KANTHARIDIS,
JRNL AUTH 2 L.A.BACH,R.S.NORTON
JRNL TITL C-TERMINAL DOMAIN OF INSULIN-LIKE GROWTH FACTOR (IGF)
JRNL TITL 2 BINDING PROTEIN-6: STRUCTURE AND INTERACTION WITH IGF-II.
JRNL REF MOL.ENDOCRINOL. V. 18 2740 2004
JRNL REFN ISSN 0888-8809
JRNL PMID 15308688
JRNL DOI 10.1210/ME.2004-0248
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.HEADEY,S.YAO,N.J.PARKER,P.KANTHARIDIS,L.A.BACH,
REMARK 1 AUTH 2 R.S.NORTON
REMARK 1 TITL 1H, 13C AND 15N RESONANCE ASSIGNMENTS OF THE C-TERMINAL
REMARK 1 TITL 2 DOMAIN OF INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN-6
REMARK 1 TITL 3 (IGFBP-6).
REMARK 1 REF J.BIOMOL.NMR V. 25 251 2003
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1022880328909
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.J.HEADEY,D.W.KEIZER,S.YAO,J.C.WALLACE,L.A.BACH,R.S.NORTON
REMARK 1 TITL BINDING SITE FOR THE C-DOMAIN OF INSULIN-LIKE GROWTH FACTOR
REMARK 1 TITL 2 (IGF) BINDING PROTEIN-6 ON IGF-II; IMPLICATIONS FOR
REMARK 1 TITL 3 INHIBITION OF IGF ACTIONS.
REMARK 1 REF FEBS LETT. V. 568 19 2004
REMARK 1 REFN ISSN 0014-5793
REMARK 1 PMID 15196913
REMARK 1 DOI 10.1016/J.FEBSLET.2004.04.091
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.YAO,S.J.HEADEY,D.W.KEIZER,L.A.BACH,R.S.NORTON
REMARK 1 TITL C-TERMINAL DOMAIN OF INSULIN-LIKE GROWTH FACTOR (IGF)
REMARK 1 TITL 2 BINDING PROTEIN 6: CONFORMATIONAL EXCHANGE AND ITS
REMARK 1 TITL 3 CORRELATION WITH IGF-II BINDING
REMARK 1 REF BIOCHEMISTRY V. 43 11187 2004
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI049456+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 1.0.3
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1067 RESTRAINTS, 912 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 145 DIHEDRAL ANGLE RESTRAINTS,10 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1RMJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020883.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 10 MM SODIUM ACETATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM PROTEIN 10 MM SODIUM
REMARK 210 ACETATE 0.02 % SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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 O GLN A 15 HH22 ARG A 20 1.52
REMARK 500 HE ARG A 37 O SER A 72 1.52
REMARK 500 O ARG A 5 HG SER A 9 1.53
REMARK 500 HH TYR A 19 OG SER A 43 1.55
REMARK 500 O LEU A 7 H LEU A 11 1.57
REMARK 500 OD2 ASP A 56 HE ARG A 57 1.57
REMARK 500 O THR A 24 HE ARG A 42 1.58
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 15 GLY A 34 N GLY A 34 CA 0.095
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 8 TYR A 19 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
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 HIS A -22 50.01 -118.08
REMARK 500 1 HIS A -20 -69.44 -91.00
REMARK 500 1 HIS A -19 -91.84 40.14
REMARK 500 1 TYR A -17 -82.16 -122.10
REMARK 500 1 ASP A -16 48.59 -164.56
REMARK 500 1 PRO A -14 86.36 -69.38
REMARK 500 1 GLN A -6 105.81 -54.96
REMARK 500 1 MET A -3 -153.35 -108.33
REMARK 500 1 VAL A 18 -64.05 -102.85
REMARK 500 1 ALA A 22 -86.31 -79.74
REMARK 500 1 GLN A 23 -72.46 -140.21
REMARK 500 1 THR A 24 47.60 -167.63
REMARK 500 1 SER A 73 -64.80 -96.28
REMARK 500 1 PRO A 75 -70.45 -65.04
REMARK 500 2 TYR A -25 53.35 26.75
REMARK 500 2 HIS A -20 -169.08 67.47
REMARK 500 2 HIS A -19 -163.34 -108.35
REMARK 500 2 PRO A -14 85.22 -69.61
REMARK 500 2 PHE A -7 95.03 -61.40
REMARK 500 2 SER A -1 71.52 30.58
REMARK 500 2 ALA A 22 -88.96 -80.38
REMARK 500 2 GLN A 23 -72.63 -139.72
REMARK 500 2 THR A 24 49.71 -170.12
REMARK 500 2 ARG A 49 90.38 -1.48
REMARK 500 2 SER A 73 -61.18 -99.37
REMARK 500 2 PRO A 75 -83.91 -78.16
REMARK 500 2 SER A 79 -72.66 -92.14
REMARK 500 3 HIS A -24 -60.64 -101.23
REMARK 500 3 HIS A -21 85.73 -156.08
REMARK 500 3 HIS A -19 98.14 178.94
REMARK 500 3 PRO A -14 74.49 -68.26
REMARK 500 3 ALA A -4 -94.64 -76.99
REMARK 500 3 SER A -1 50.38 34.58
REMARK 500 3 VAL A 18 -72.59 -89.09
REMARK 500 3 ALA A 22 -86.20 -94.87
REMARK 500 3 GLN A 23 -64.19 -141.44
REMARK 500 3 THR A 24 50.35 -147.00
REMARK 500 3 ARG A 49 97.86 -13.05
REMARK 500 3 PRO A 63 -81.28 -79.52
REMARK 500 4 TYR A -26 94.62 59.24
REMARK 500 4 HIS A -21 56.57 -92.06
REMARK 500 4 ASP A -16 -138.95 -86.84
REMARK 500 4 MET A -3 -124.15 -86.99
REMARK 500 4 SER A -1 16.95 59.60
REMARK 500 4 THR A 24 40.01 -160.11
REMARK 500 4 TYR A 36 93.04 -68.22
REMARK 500 4 GLN A 47 -159.68 -88.82
REMARK 500 4 ASN A 69 58.27 -69.15
REMARK 500 4 PRO A 75 -92.60 -83.03
REMARK 500 5 TYR A -26 92.85 58.20
REMARK 500
REMARK 500 THIS ENTRY HAS 242 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 4 0.32 SIDE CHAIN
REMARK 500 1 ARG A 5 0.28 SIDE CHAIN
REMARK 500 1 ARG A 20 0.30 SIDE CHAIN
REMARK 500 1 ARG A 33 0.29 SIDE CHAIN
REMARK 500 1 ARG A 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 39 0.32 SIDE CHAIN
REMARK 500 1 ARG A 42 0.29 SIDE CHAIN
REMARK 500 1 ARG A 48 0.32 SIDE CHAIN
REMARK 500 1 ARG A 49 0.31 SIDE CHAIN
REMARK 500 1 ARG A 57 0.29 SIDE CHAIN
REMARK 500 2 ARG A 4 0.30 SIDE CHAIN
REMARK 500 2 ARG A 5 0.32 SIDE CHAIN
REMARK 500 2 ARG A 20 0.21 SIDE CHAIN
REMARK 500 2 ARG A 33 0.32 SIDE CHAIN
REMARK 500 2 ARG A 37 0.28 SIDE CHAIN
REMARK 500 2 ARG A 39 0.31 SIDE CHAIN
REMARK 500 2 ARG A 42 0.23 SIDE CHAIN
REMARK 500 2 ARG A 48 0.28 SIDE CHAIN
REMARK 500 2 ARG A 49 0.32 SIDE CHAIN
REMARK 500 2 ARG A 57 0.32 SIDE CHAIN
REMARK 500 3 ARG A 4 0.29 SIDE CHAIN
REMARK 500 3 ARG A 5 0.29 SIDE CHAIN
REMARK 500 3 ARG A 20 0.28 SIDE CHAIN
REMARK 500 3 ARG A 33 0.32 SIDE CHAIN
REMARK 500 3 ARG A 37 0.29 SIDE CHAIN
REMARK 500 3 ARG A 39 0.31 SIDE CHAIN
REMARK 500 3 ARG A 42 0.30 SIDE CHAIN
REMARK 500 3 ARG A 48 0.30 SIDE CHAIN
REMARK 500 3 ARG A 49 0.31 SIDE CHAIN
REMARK 500 3 ARG A 57 0.32 SIDE CHAIN
REMARK 500 4 ARG A 4 0.32 SIDE CHAIN
REMARK 500 4 ARG A 5 0.28 SIDE CHAIN
REMARK 500 4 ARG A 20 0.31 SIDE CHAIN
REMARK 500 4 ARG A 33 0.30 SIDE CHAIN
REMARK 500 4 ARG A 37 0.28 SIDE CHAIN
REMARK 500 4 ARG A 39 0.29 SIDE CHAIN
REMARK 500 4 ARG A 42 0.31 SIDE CHAIN
REMARK 500 4 ARG A 48 0.32 SIDE CHAIN
REMARK 500 4 ARG A 49 0.32 SIDE CHAIN
REMARK 500 4 ARG A 57 0.25 SIDE CHAIN
REMARK 500 5 ARG A 4 0.28 SIDE CHAIN
REMARK 500 5 ARG A 5 0.32 SIDE CHAIN
REMARK 500 5 ARG A 20 0.30 SIDE CHAIN
REMARK 500 5 ARG A 33 0.32 SIDE CHAIN
REMARK 500 5 ARG A 37 0.32 SIDE CHAIN
REMARK 500 5 ARG A 39 0.32 SIDE CHAIN
REMARK 500 5 ARG A 42 0.27 SIDE CHAIN
REMARK 500 5 ARG A 48 0.28 SIDE CHAIN
REMARK 500 5 ARG A 49 0.31 SIDE CHAIN
REMARK 500 5 ARG A 57 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 200 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5545 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS FOR THE PROTEIN IN THIS ENTRY
DBREF 1RMJ A 1 80 UNP P24592 IBP6_HUMAN 161 240
SEQADV 1RMJ SER A -27 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ TYR A -26 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ TYR A -25 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ HIS A -24 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ HIS A -23 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ HIS A -22 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ HIS A -21 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ HIS A -20 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ HIS A -19 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ ASP A -18 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ TYR A -17 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ ASP A -16 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ ILE A -15 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ PRO A -14 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ THR A -13 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ THR A -12 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ GLU A -11 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ ASN A -10 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ LEU A -9 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ TYR A -8 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ PHE A -7 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ GLN A -6 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ GLY A -5 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ ALA A -4 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ MET A -3 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ GLY A -2 UNP P24592 CLONING ARTIFACT
SEQADV 1RMJ SER A -1 UNP P24592 CLONING ARTIFACT
SEQRES 1 A 107 SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE
SEQRES 2 A 107 PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET GLY
SEQRES 3 A 107 SER GLY PRO CYS ARG ARG HIS LEU ASP SER VAL LEU GLN
SEQRES 4 A 107 GLN LEU GLN THR GLU VAL TYR ARG GLY ALA GLN THR LEU
SEQRES 5 A 107 TYR VAL PRO ASN CYS ASP HIS ARG GLY PHE TYR ARG LYS
SEQRES 6 A 107 ARG GLN CYS ARG SER SER GLN GLY GLN ARG ARG GLY PRO
SEQRES 7 A 107 CYS TRP CYS VAL ASP ARG MET GLY LYS SER LEU PRO GLY
SEQRES 8 A 107 SER PRO ASP GLY ASN GLY SER SER SER CYS PRO THR GLY
SEQRES 9 A 107 SER SER GLY
HELIX 1 1 THR A -13 TYR A -8 1 6
HELIX 2 2 GLY A 1 VAL A 18 1 18
SHEET 1 A 3 THR A 24 PRO A 28 0
SHEET 2 A 3 ARG A 39 SER A 44 -1 O CYS A 41 N VAL A 27
SHEET 3 A 3 CYS A 52 CYS A 54 -1 O TRP A 53 N GLN A 40
SSBOND 1 CYS A 3 CYS A 30 1555 1555 2.02
SSBOND 2 CYS A 41 CYS A 52 1555 1555 2.01
SSBOND 3 CYS A 54 CYS A 74 1555 1555 2.02
CISPEP 1 GLY A 50 PRO A 51 1 0.88
CISPEP 2 GLY A 50 PRO A 51 2 0.02
CISPEP 3 GLY A 50 PRO A 51 3 -1.36
CISPEP 4 GLY A 50 PRO A 51 4 -2.40
CISPEP 5 GLY A 50 PRO A 51 5 0.82
CISPEP 6 GLY A 50 PRO A 51 6 1.06
CISPEP 7 GLY A 50 PRO A 51 7 -5.06
CISPEP 8 GLY A 50 PRO A 51 8 -4.10
CISPEP 9 GLY A 50 PRO A 51 9 -0.07
CISPEP 10 GLY A 50 PRO A 51 10 1.17
CISPEP 11 GLY A 50 PRO A 51 11 -1.06
CISPEP 12 GLY A 50 PRO A 51 12 -5.05
CISPEP 13 GLY A 50 PRO A 51 13 -2.69
CISPEP 14 GLY A 50 PRO A 51 14 -0.02
CISPEP 15 GLY A 50 PRO A 51 15 -0.52
CISPEP 16 GLY A 50 PRO A 51 16 0.89
CISPEP 17 GLY A 50 PRO A 51 17 -0.18
CISPEP 18 GLY A 50 PRO A 51 18 -2.84
CISPEP 19 GLY A 50 PRO A 51 19 -7.37
CISPEP 20 GLY A 50 PRO A 51 20 -1.68
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 - r 2 2 Bytes