Header list of 1l5e.pdb file
Complete list - 23 20 Bytes
HEADER ANTIVIRAL PROTEIN 06-MAR-02 1L5E
TITLE THE DOMAIN-SWAPPED DIMER OF CV-N IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYANOVIRIN-N;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CV-N;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC ELLIPSOSPORUM;
SOURCE 3 ORGANISM_TAXID: 45916;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS 3D DOMAIN-SWAPPING, CYANOVIRIN-N, PROTEIN FOLDING, ANTIVIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR L.G.BARRIENTOS,J.M.LOUIS,I.BOTOS,T.MORI,Z.HAN,B.R.O'KEEFE,M.R.BOYD,
AUTHOR 2 A.WLODAWER,A.M.GRONENBORN
REVDAT 4 23-FEB-22 1L5E 1 REMARK
REVDAT 3 24-FEB-09 1L5E 1 VERSN
REVDAT 2 01-APR-03 1L5E 1 JRNL
REVDAT 1 05-JUN-02 1L5E 0
JRNL AUTH L.G.BARRIENTOS,J.M.LOUIS,I.BOTOS,T.MORI,Z.HAN,B.R.O'KEEFE,
JRNL AUTH 2 M.R.BOYD,A.WLODAWER,A.M.GRONENBORN
JRNL TITL THE DOMAIN-SWAPPED DIMER OF CYANOVIRIN-N IS IN A METASTABLE
JRNL TITL 2 FOLDED STATE: RECONCILIATION OF X-RAY AND NMR STRUCTURES.
JRNL REF STRUCTURE V. 10 673 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12015150
JRNL DOI 10.1016/S0969-2126(02)00758-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, PALES
REMARK 3 AUTHORS : F.DELAGLIO, S.GRZESIEK, G.W.VUISTER, G.ZHU,
REMARK 3 J.PFEIFER, A.BAX (NMRPIPE), M.ZWECKSTETTER, A.BAX
REMARK 3 (PALES)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE COORDINATES OF THE INDIVIDUAL DOMAINS OF THE DOMAIN SWAPPED
REMARK 3 DIMER CV-N WERE TAKEN DIRECTLY FROM THE X-RAY COORDINATES, 3EZM
REMARK 3 AND 1L5B. THE ONLY PROTONS ADDED ARE THE HNE1 OF W(49/150) AND
REMARK 3 ALL THE BACKBONE AMIDE PROTONS (HN), SINCE DOMAIN-DOMAIN
REMARK 3 ORIENTATION WAS BASED ONLY ON HN/HNE1 RESIDUAL DIPOLAR COUPLINGS.
REMARK 3 THE STARTING COORDINATES WERE THOSE OF TWO PSEUDO-MONOMER UNITS
REMARK 3 (AB' AND A'B)
REMARK 3 EXTRACTED FROM THE REFINED TRIGONAL 1.5 X-RAY STRUCTURE, IN WHICH
REMARK 3 PROLINE 51
REMARK 3 AT THE JUNCTION BETWEEN A AND B WAS REMOVED, ALLOWING FOR FREE
REMARK 3 ROTATION AROUND
REMARK 3 THIS JUNCTION. WE THEN TREATED AB' AND A'B AS TWO INDEPENDENT SUB-
REMARK 3 DOMAINS.
REMARK 3 ASSUMING THAT THE ORIENTATION OF THE TWO SUB-DOMAINS IS FIXED IN
REMARK 3 SOLUTION (AT
REMARK 3 LEAST TO A FIRST APPROXIMATION), THE PRINCIPAL AXIS SYSTEMS, OR
REMARK 3 ALIGNMENT FRAMES,
REMARK 3 OF SUB-DOMAINS AB' AND A'B SHOULD BE EQUIVALENT TO THE ALIGNMENT
REMARK 3 SYSTEM OF THE
REMARK 3 ENTIRE MOLECULE AND, VICE VERSA, TO EACH OTHER. USING THE RESIDUAL
REMARK 3 DIPOLAR COUPLINGS
REMARK 3 WE CALCULATED THE ORDER TENSOR PRINCIPAL AXIS SYSTEMS FOR EACH
REMARK 3 DOMAIN. ROTATION OF
REMARK 3 PSEUDO SUB-DOMAIN A'B AROUND THE HINGE AT AMINO ACID POSITION 51
REMARK 3 UNTIL A SUPERPOSITION
REMARK 3 OF THE INDIVIDUAL COORDINATE FRAMES WAS OBTAINED YIELDED THE FINAL
REMARK 3 MODEL OF THE
REMARK 3 SOLUTION DIMER.
REMARK 4
REMARK 4 1L5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015656.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.150 MM PROTEIN IN 25 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, PH 8.0 AND
REMARK 210 0.02 % NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D IPAP [15N-1H]-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PALES
REMARK 210 METHOD USED : DETERMINATION OF THE DOMAIN
REMARK 210 ORIENTATION FOR THE SOLUTION
REMARK 210 STRUCTURE OF THE DIMER WAS
REMARK 210 CARRIED OUT USING A PROCEDURE
REMARK 210 ANALOGOUS TO THE ONE DESCRIBED
REMARK 210 FOR DETERMINING THE RELATIVE
REMARK 210 DOMAIN ORIENTATION IN A TWO-
REMARK 210 DOMAIN PROTEIN FRAGMENT OF A
REMARK 210 LECTIN.
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 : NULL
REMARK 210
REMARK 210 REMARK: RESIDUAL DIPOLAR COUPLINGS WERE MEASURED IN THE PRESENCE
REMARK 210 OF A COLLOIDAL PHAGE SOLUTION OF 11.5 MG/ML PF1.
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 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 VAL A 39 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 GLN A 50 N - CA - CB ANGL. DEV. = -15.8 DEGREES
REMARK 500 VAL B 140 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 GLN B 151 N - CA - CB ANGL. DEV. = -15.8 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 GLN A 50 -155.93 -124.94
REMARK 500 ASN A 53 -174.73 169.59
REMARK 500 SER A 67 5.10 -151.08
REMARK 500 GLN B 151 -155.28 -124.60
REMARK 500 ASN B 154 -174.65 169.40
REMARK 500 SER B 168 5.10 -151.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 39 14.44
REMARK 500 VAL B 140 14.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2EZM RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF CYANOVIRIN-N, RESTRAINED REGULARIZED MEAN
REMARK 900 COORDINATES
REMARK 900 RELATED ID: 3EZM RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF CYANOVIRIN-N; DOMAIN-SWAPPED DIMER
REMARK 900 RELATED ID: 1L5B RELATED DB: PDB
REMARK 900 DOMAIN-SWAPPED CYANOVIRIN-N DIMER
DBREF 1L5E A 1 101 UNP P81180 CVN_NOSEL 1 101
DBREF 1L5E B 102 202 UNP P81180 CVN_NOSEL 1 101
SEQRES 1 A 101 LEU GLY LYS PHE SER GLN THR CYS TYR ASN SER ALA ILE
SEQRES 2 A 101 GLN GLY SER VAL LEU THR SER THR CYS GLU ARG THR ASN
SEQRES 3 A 101 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL
SEQRES 4 A 101 ILE GLU ASN VAL ASP GLY SER LEU LYS TRP GLN PRO SER
SEQRES 5 A 101 ASN PHE ILE GLU THR CYS ARG ASN THR GLN LEU ALA GLY
SEQRES 6 A 101 SER SER GLU LEU ALA ALA GLU CYS LYS THR ARG ALA GLN
SEQRES 7 A 101 GLN PHE VAL SER THR LYS ILE ASN LEU ASP ASP HIS ILE
SEQRES 8 A 101 ALA ASN ILE ASP GLY THR LEU LYS TYR GLU
SEQRES 1 B 101 LEU GLY LYS PHE SER GLN THR CYS TYR ASN SER ALA ILE
SEQRES 2 B 101 GLN GLY SER VAL LEU THR SER THR CYS GLU ARG THR ASN
SEQRES 3 B 101 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL
SEQRES 4 B 101 ILE GLU ASN VAL ASP GLY SER LEU LYS TRP GLN PRO SER
SEQRES 5 B 101 ASN PHE ILE GLU THR CYS ARG ASN THR GLN LEU ALA GLY
SEQRES 6 B 101 SER SER GLU LEU ALA ALA GLU CYS LYS THR ARG ALA GLN
SEQRES 7 B 101 GLN PHE VAL SER THR LYS ILE ASN LEU ASP ASP HIS ILE
SEQRES 8 B 101 ALA ASN ILE ASP GLY THR LEU LYS TYR GLU
HELIX 1 1 LYS A 3 GLN A 6 5 4
HELIX 2 2 LYS B 104 GLN B 107 5 4
SHEET 1 A 3 CYS A 8 GLN A 14 0
SHEET 2 A 3 VAL A 17 GLU A 23 -1 O THR A 19 N ALA A 12
SHEET 3 A 3 TYR A 29 ASP A 35 -1 O ASN A 30 N CYS A 22
SHEET 1 B 2 ILE A 40 VAL A 43 0
SHEET 2 B 2 SER A 46 TRP A 49 -1 O LYS A 48 N GLU A 41
SHEET 1 C 3 CYS A 58 ALA A 64 0
SHEET 2 C 3 GLU A 68 LYS A 74 -1 O GLU A 68 N ALA A 64
SHEET 3 C 3 PHE A 80 ASN A 86 -1 O ILE A 85 N LEU A 69
SHEET 1 D 2 ILE A 91 ILE A 94 0
SHEET 2 D 2 THR A 97 TYR A 100 -1 O LYS A 99 N ALA A 92
SHEET 1 E 3 CYS B 109 GLN B 115 0
SHEET 2 E 3 VAL B 118 GLU B 124 -1 O THR B 120 N ALA B 113
SHEET 3 E 3 TYR B 130 ASP B 136 -1 O ASN B 131 N CYS B 123
SHEET 1 F 2 ILE B 141 VAL B 144 0
SHEET 2 F 2 SER B 147 TRP B 150 -1 O LYS B 149 N GLU B 142
SHEET 1 G 3 CYS B 159 ALA B 165 0
SHEET 2 G 3 GLU B 169 LYS B 175 -1 O GLU B 169 N ALA B 165
SHEET 3 G 3 PHE B 181 ASN B 187 -1 O ILE B 186 N LEU B 170
SHEET 1 H 2 ILE B 192 ILE B 195 0
SHEET 2 H 2 THR B 198 TYR B 201 -1 O LYS B 200 N ALA B 193
SSBOND 1 CYS A 8 CYS A 22 1555 1555 2.03
SSBOND 2 CYS A 58 CYS A 73 1555 1555 2.04
SSBOND 3 CYS B 109 CYS B 123 1555 1555 2.03
SSBOND 4 CYS B 159 CYS B 174 1555 1555 2.04
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