Header list of 1n9j.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE INHIBITOR 25-NOV-02 1N9J
TITLE SOLUTION STRUCTURE OF THE 3D DOMAIN SWAPPED DIMER OF STEFIN A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTATIN A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: STEFIN A, CYSTATIN AS;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS DOMAIN SWAPPED, STEFIN A, CYSTATINS, AMYLOID, HYDROLASE INHIBITOR
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR R.A.STANIFORTH,S.GIANNINI,L.D.HIGGINS,M.J.CONROY,A.M.HOUNSLOW,
AUTHOR 2 R.JERALA,C.J.CRAVEN,J.P.WALTHO
REVDAT 3 23-FEB-22 1N9J 1 REMARK
REVDAT 2 24-FEB-09 1N9J 1 VERSN
REVDAT 1 25-FEB-03 1N9J 0
JRNL AUTH R.A.STANIFORTH,S.GIANNINI,L.D.HIGGINS,M.J.CONROY,
JRNL AUTH 2 A.M.HOUNSLOW,R.JERALA,C.J.CRAVEN,J.P.WALTHO
JRNL TITL THREE-DIMENSIONAL DOMAIN SWAPPING IN THE FOLDED AND
JRNL TITL 2 MOLTEN-GLOBULE STATES OF CYSTATINS, AN AMYLOID-FORMING
JRNL TITL 3 STRUCTURAL SUPERFAMILY
JRNL REF EMBO J. V. 20 4774 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11532941
JRNL DOI 10.1093/EMBOJ/20.17.4774
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DISTANCE RESTRAINTS (NOES AND HYDROGEN BONDS) WERE TAKEN FROM THE
REMARK 3 DATA USED FOR THE STEFIN A MONOMER
REMARK 3 STRUCTURE (MARTIN ET AL., 1995), EXCEPT THOSE INVOLVING RESIDUES
REMARK 3 V48-G50 AND N77-L80 WHERE CHEMICAL
REMARK 3 SHIFT PERTURBATION WAS OBSERVED FOLLOWING RESONANCE ASSIGNMENT.
REMARK 3 THE NOES WERE SPECIFIED AS
REMARK 3 INTERMOLECULAR AND INTRAMOLECULAR ACCORDING TO DOMAIN-SWAPPED
REMARK 3 TOPOLOGY INFERRED FROM ISOTOPE
REMARK 3 FILTERING EXPERIMENTS. AN ADDITIONAL HYDROGEN BOND RESTRAINT WAS
REMARK 3 INCLUDED BETWEEN 48 AND 50 BASED ON
REMARK 3 EVIDENCE FROM PROTECTION EXPERIMENTS ON THE DIMER (JERALA AND
REMARK 3 ZEROVNIK, 1999). DIHEDRAL RESTRAINTS (PHI
REMARK 3 AND PSI) WERE DETERMINED USING THE 1H-ALPHA, 15N, 13C-ALPHA, 13C-
REMARK 3 BETA AND 13C' CHEMICAL SHIFTS AND THE PROGRAM
REMARK 3 TALOS (CORNILESCU ET AL., 1999). WHERE TALOS GAVE A `POOR' MATCH,
REMARK 3 THE EXPERIMENTAL PHI DIHEDRAL ANGLE
REMARK 3 WAS TAKEN FROM THE DATA USED FOR THE STEFIN A MONOMER STRUCTURE
REMARK 3 CALCULATION.
REMARK 4
REMARK 4 1N9J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017687.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM STEFIN A U-15N; 50MM
REMARK 210 PHOSPHATE BUFFER PH 5.5, 100MM
REMARK 210 KCL, 5MM AZIDE; 90% H2O, 10% D2O;
REMARK 210 1MM STEFIN A U-15N,13C,2H; 50MM
REMARK 210 PHOSPHATE BUFFER PH 5.5, 100MM
REMARK 210 KCL, 5MM AZIDE; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HNCO; HN(CA)CB; TOCSY
REMARK 210 -HSQC; NOESY-HSQC; 15N-ISOTOPE-
REMARK 210 FILTERED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 GLU A 8 CD GLU A 8 OE2 0.109
REMARK 500 GLU A 15 CD GLU A 15 OE2 0.110
REMARK 500 GLU A 18 CD GLU A 18 OE2 0.112
REMARK 500 GLU A 28 CD GLU A 28 OE2 0.109
REMARK 500 GLU A 29 CD GLU A 29 OE2 0.111
REMARK 500 GLU A 33 CD GLU A 33 OE2 0.111
REMARK 500 GLU A 39 CD GLU A 39 OE2 0.111
REMARK 500 GLU A 78 CD GLU A 78 OE2 0.109
REMARK 500 GLU A 94 CD GLU A 94 OE2 0.110
REMARK 500 GLU B 8 CD GLU B 8 OE2 0.109
REMARK 500 GLU B 15 CD GLU B 15 OE2 0.111
REMARK 500 GLU B 18 CD GLU B 18 OE2 0.110
REMARK 500 GLU B 28 CD GLU B 28 OE2 0.101
REMARK 500 GLU B 29 CD GLU B 29 OE2 0.111
REMARK 500 GLU B 33 CD GLU B 33 OE2 0.111
REMARK 500 GLU B 39 CD GLU B 39 OE2 0.106
REMARK 500 GLU B 78 CD GLU B 78 OE2 0.110
REMARK 500 GLU B 94 CD GLU B 94 OE2 0.109
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 ASP A 21 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TYR A 35 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR A 43 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 HIS B 66 ND1 - CE1 - NE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASP B 79 CB - CG - OD1 ANGL. DEV. = 6.0 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 PRO A 11 9.19 -66.47
REMARK 500 ALA A 12 135.72 148.15
REMARK 500 VAL A 41 -141.72 -131.83
REMARK 500 ASP A 61 -29.33 -34.07
REMARK 500 SER A 72 -80.54 -109.56
REMARK 500 TYR A 85 126.89 -172.84
REMARK 500 ASP A 88 4.15 -38.25
REMARK 500 SER B 7 -174.62 -66.81
REMARK 500 PRO B 11 6.37 -66.06
REMARK 500 ALA B 12 74.81 150.26
REMARK 500 VAL B 41 -146.65 -138.56
REMARK 500 VAL B 57 117.29 -162.60
REMARK 500 SER B 72 -91.61 -86.90
REMARK 500 ASP B 88 -8.86 -24.35
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 ARG A 58 ALA A 59 134.41
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 ARG A 58 0.31 SIDE CHAIN
REMARK 500 PHE A 98 0.13 SIDE CHAIN
REMARK 500 TYR B 53 0.08 SIDE CHAIN
REMARK 500 TYR B 54 0.08 SIDE CHAIN
REMARK 500 ARG B 58 0.28 SIDE CHAIN
REMARK 500 TYR B 85 0.07 SIDE CHAIN
REMARK 500 PHE B 98 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DVC RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF MONOMERIC HUMAN STEFIN A AT PH 5.5 AND
REMARK 900 308K
DBREF 1N9J A 1 98 UNP P01040 CYTA_HUMAN 1 98
DBREF 1N9J B 1 98 UNP P01040 CYTA_HUMAN 1 98
SEQRES 1 A 98 MET ILE PRO GLY GLY LEU SER GLU ALA LYS PRO ALA THR
SEQRES 2 A 98 PRO GLU ILE GLN GLU ILE VAL ASP LYS VAL LYS PRO GLN
SEQRES 3 A 98 LEU GLU GLU LYS THR ASN GLU THR TYR GLY LYS LEU GLU
SEQRES 4 A 98 ALA VAL GLN TYR LYS THR GLN VAL VAL ALA GLY THR ASN
SEQRES 5 A 98 TYR TYR ILE LYS VAL ARG ALA GLY ASP ASN LYS TYR MET
SEQRES 6 A 98 HIS LEU LYS VAL PHE LYS SER LEU PRO GLY GLN ASN GLU
SEQRES 7 A 98 ASP LEU VAL LEU THR GLY TYR GLN VAL ASP LYS ASN LYS
SEQRES 8 A 98 ASP ASP GLU LEU THR GLY PHE
SEQRES 1 B 98 MET ILE PRO GLY GLY LEU SER GLU ALA LYS PRO ALA THR
SEQRES 2 B 98 PRO GLU ILE GLN GLU ILE VAL ASP LYS VAL LYS PRO GLN
SEQRES 3 B 98 LEU GLU GLU LYS THR ASN GLU THR TYR GLY LYS LEU GLU
SEQRES 4 B 98 ALA VAL GLN TYR LYS THR GLN VAL VAL ALA GLY THR ASN
SEQRES 5 B 98 TYR TYR ILE LYS VAL ARG ALA GLY ASP ASN LYS TYR MET
SEQRES 6 B 98 HIS LEU LYS VAL PHE LYS SER LEU PRO GLY GLN ASN GLU
SEQRES 7 B 98 ASP LEU VAL LEU THR GLY TYR GLN VAL ASP LYS ASN LYS
SEQRES 8 B 98 ASP ASP GLU LEU THR GLY PHE
HELIX 1 1 THR A 13 ASN A 32 1 20
HELIX 2 2 GLN A 76 LEU A 80 5 5
HELIX 3 3 THR B 13 ASN B 32 1 20
SHEET 1 A 2 LYS A 37 ALA A 40 0
SHEET 2 A 2 VAL B 57 GLY B 60 -1 O ARG B 58 N GLU A 39
SHEET 1 B 6 VAL A 81 GLN A 86 0
SHEET 2 B 6 MET A 65 LYS A 71 -1 N PHE A 70 O VAL A 81
SHEET 3 B 6 LYS A 44 ARG A 58 -1 N ILE A 55 O LEU A 67
SHEET 4 B 6 GLU B 39 TYR B 54 -1 O LYS B 44 N TYR A 54
SHEET 5 B 6 LYS B 68 LYS B 71 -1 O LYS B 71 N THR B 51
SHEET 6 B 6 LEU B 80 GLY B 84 -1 O VAL B 81 N PHE B 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
Complete list - 23 20 Bytes