Header list of 1n02.pdb file
Complete list - b 5 2 Bytes
HEADER VIRAL PROTEIN INHIBITOR 10-OCT-02 1N02
TITLE SOLUTION STRUCTURE OF A CIRCULAR-PERMUTED VARIANT OF THE POTENT HIV-
TITLE 2 INACTIVATING PROTEIN CYANOVIRIN-N
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYANOVIRIN-N;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CPCV-N;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CIRCULAR-PERMUTED VARIANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC ELLIPSOSPORUM;
SOURCE 3 ORGANISM_TAXID: 45916;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS VIRUS/VIRAL PROTEIN INHIBITOR, VIRAL PROTEIN INHIBITOR
EXPDTA SOLUTION NMR
NUMMDL 26
MDLTYP MINIMIZED AVERAGE
AUTHOR L.G.BARRIENTOS,A.M.GRONENBORN
REVDAT 3 05-FEB-20 1N02 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1N02 1 VERSN
REVDAT 1 18-DEC-02 1N02 0
JRNL AUTH L.G.BARRIENTOS,J.M.LOUIS,D.M.RATNER,P.H.SEEBERGER,
JRNL AUTH 2 A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE OF A CIRCULAR-PERMUTED VARIANT OF THE
JRNL TITL 2 POTENT HIV-INACTIVATING PROTEIN CYANOVIRIN-N: STRUCTURAL
JRNL TITL 3 BASIS FOR PROTEIN STABILITY AND OLIGOSACCHARIDE INTERACTION
JRNL REF J.MOL.BIOL. V. 325 211 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12473463
JRNL DOI 10.1016/S0022-2836(02)01205-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER, WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N02 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017350.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N HSQC; 1H-13C HMQC; HNHA;
REMARK 210 HCCH-TOCSY; (H)C(CCO)NH-TOCSY;
REMARK 210 NOESY; 4D 13C/13C SEPARATED NOE
REMARK 210 HNHB; 2D HN(CO)CG; HNCG
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DRX600; DMX750; DMX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, CNS
REMARK 210 METHOD USED : FOR DYANA, STANDARD TARGET
REMARK 210 FUNCTION-SIMULATED ANNEALING
REMARK 210 PROTOCOL. FOR CNS, SIMULATED-
REMARK 210 ANNEALING IN CARTESIAN SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE MINIMIZED AVERAGE STRUCTURE IS MODEL 1. MODELS 2-26
REMARK 210 ARE THE THE FINAL 25 CONFORMER ENSEMBLE. DYANA AND CNS WERE USED
REMARK 210 FOR REFINEMENT. VIRTUALLY COMPLETE RESONANCE ASSIGNMENTS WERE
REMARK 210 REPORTED I (2001) J.BIOM.NMR, 19: 289-90; HTTP://
REMARK 210 WWW.BMRB.WISC.EDU. STEREO-SPECIFIC ASSIGNMENTS FOR ALL THE
REMARK 210 METHYL GROUPS OF OF THE EIGHT LEU RESIDUES AND FOR THE ALPHA-
REMARK 210 METHYLENE PR EIGHT GLY, 46 BETA-METHYLENE PROTONS AND THE GAMMA-
REMARK 210 METHY OF THE SEVEN ILE WERE AVAILABLE. IN TOTAL, 1879 EXPERIM
REMARK 210 WERE EMPLOYED, REPRESENTING ~19 CONSTRAINTS PER RESIDUE.
REMARK 210 STRUCTURES WAS FIRST CALCULATED WITH DYANA, BASED ON 114 92
REMARK 210 HYDROGEN BOND DISTANCES AND 193 DIHEDRAL ANGLES. REF VALUES
REMARK 210 YIELDED AN ESEMBLE OF 50 STRUCTURES EXHIBITING AT 0.26+/-0.06 A
REMARK 210 AND 0.64+/-0.08A WITH RESPECT TO THE MEAN BACKBONE (N,CA,C') AND
REMARK 210 ALL HEAVY ATOMS, RESPECTIVELY, AN 0.81+/-0.10A^2. THIS INITIAL
REMARK 210 ENSEMBLE OF STRUCTURES WAS RESIDUAL DIPOLAR COUPLINGS (80) AND
REMARK 210 CHEMICAL SHIFTS (291 PROGRAMS CNS. OVERALL, EXCELLENT AGREEMENT
REMARK 210 WITH THE EXP GOOD COVALENT GEOMETRY WAS MAINTAINED THROUGHOUT.
REMARK 210 THE F WAS SELECTED AND ARE PRESENTED HERE AS MODELS2-26, AND A
REMARK 210 MEAN STRUCTURE OF THIS ENSEMBLE IS PRESENTED HERE AS MOD.
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 H ALA A 14 O GLU A 18 1.54
REMARK 500 H THR A 25 O GLN A 29 1.58
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 LEU A 1 30.52 -144.73
REMARK 500 1 LYS A 3 80.57 65.95
REMARK 500 1 HIS A 40 -64.21 -97.32
REMARK 500 1 GLN A 51 141.22 -174.90
REMARK 500 1 PRO A 52 70.18 -66.07
REMARK 500 2 LYS A 3 84.38 -154.12
REMARK 500 2 SER A 17 35.74 -140.86
REMARK 500 2 HIS A 40 -66.34 -96.69
REMARK 500 2 GLN A 51 143.06 -174.89
REMARK 500 2 PRO A 52 68.37 -62.98
REMARK 500 2 SER A 56 -19.04 -49.92
REMARK 500 3 LEU A 1 -47.30 -153.78
REMARK 500 3 LYS A 3 84.39 -151.89
REMARK 500 3 SER A 17 35.36 -141.63
REMARK 500 3 HIS A 40 -62.98 -95.21
REMARK 500 3 GLN A 51 147.17 -172.17
REMARK 500 3 PRO A 52 63.70 -69.65
REMARK 500 3 SER A 56 -17.89 -48.31
REMARK 500 4 LYS A 3 66.46 62.48
REMARK 500 4 SER A 17 36.23 -141.43
REMARK 500 4 HIS A 40 -63.33 -98.33
REMARK 500 4 GLN A 51 143.14 -174.66
REMARK 500 4 PRO A 52 74.67 -64.55
REMARK 500 4 SER A 56 -16.99 -49.32
REMARK 500 5 LYS A 3 83.77 -151.72
REMARK 500 5 SER A 17 36.11 -140.81
REMARK 500 5 HIS A 40 -64.92 -96.65
REMARK 500 5 GLN A 51 142.25 -173.04
REMARK 500 5 PRO A 52 73.29 -64.97
REMARK 500 5 SER A 56 -17.82 -49.14
REMARK 500 6 LYS A 3 70.71 65.92
REMARK 500 6 SER A 17 35.44 -140.54
REMARK 500 6 HIS A 40 -68.43 -97.87
REMARK 500 6 GLN A 51 143.39 -175.06
REMARK 500 6 PRO A 52 69.43 -62.41
REMARK 500 6 SER A 56 -16.25 -47.78
REMARK 500 7 LYS A 3 85.37 -154.90
REMARK 500 7 SER A 17 35.07 -140.69
REMARK 500 7 SER A 56 -18.12 -48.58
REMARK 500 8 LYS A 3 70.01 62.99
REMARK 500 8 SER A 17 36.23 -141.04
REMARK 500 8 HIS A 40 -65.56 -98.12
REMARK 500 8 GLN A 51 141.56 -175.51
REMARK 500 8 PRO A 52 76.17 -61.47
REMARK 500 8 SER A 56 -16.77 -48.90
REMARK 500 9 LEU A 1 -78.37 62.56
REMARK 500 9 LYS A 3 71.15 63.30
REMARK 500 9 SER A 17 34.96 -140.90
REMARK 500 9 HIS A 40 -65.95 -97.61
REMARK 500 9 GLN A 51 144.75 -175.60
REMARK 500
REMARK 500 THIS ENTRY HAS 146 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4927 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS FOR THE CONSTRAINTS TABLES AND FOR TALOS
REMARK 900 CALCULATIONS
REMARK 900 RELATED ID: 2EZM RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF WILD-TYPE CYANOVIRIN-N (NMR, RESTRAINED
REMARK 900 REGULARIZED MEAN STRUCTURE)
DBREF 1N02 A 1 3 UNP P81180 CVN_NOSEL 1 3
DBREF 1N02 A 4 49 UNP P81180 CVN_NOSEL 54 99
DBREF 1N02 A 50 54 UNP P81180 CVN_NOSEL 49 53
DBREF 1N02 A 55 99 UNP P81180 CVN_NOSEL 4 48
DBREF 1N02 A 100 101 UNP P81180 CVN_NOSEL 100 101
SEQADV 1N02 GLY A -1 UNP P81180 CLONING ARTIFACT
SEQRES 1 A 102 GLY LEU GLY LYS PHE ILE GLU THR CYS ARG ASN THR GLN
SEQRES 2 A 102 LEU ALA GLY SER SER GLU LEU ALA ALA GLU CYS LYS THR
SEQRES 3 A 102 ARG ALA GLN GLN PHE VAL SER THR LYS ILE ASN LEU ASP
SEQRES 4 A 102 ASP HIS ILE ALA ASN ILE ASP GLY THR LEU LYS TRP GLN
SEQRES 5 A 102 PRO SER ASN PHE SER GLN THR CYS TYR ASN SER ALA ILE
SEQRES 6 A 102 GLN GLY SER VAL LEU THR SER THR CYS GLU ARG THR ASN
SEQRES 7 A 102 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL
SEQRES 8 A 102 ILE GLU ASN VAL ASP GLY SER LEU LYS TYR GLU
HELIX 1 1 ASN A 54 GLN A 57 5 4
SHEET 1 A 3 CYS A 8 ALA A 14 0
SHEET 2 A 3 GLU A 18 LYS A 24 -1 O GLU A 18 N ALA A 14
SHEET 3 A 3 PHE A 30 ASN A 36 -1 O ILE A 35 N LEU A 19
SHEET 1 B 2 ILE A 41 ILE A 44 0
SHEET 2 B 2 THR A 47 TRP A 50 -1 O THR A 47 N ILE A 44
SHEET 1 C 3 CYS A 59 GLN A 65 0
SHEET 2 C 3 VAL A 68 GLU A 74 -1 O THR A 70 N ALA A 63
SHEET 3 C 3 TYR A 80 ASP A 86 -1 O ASN A 81 N CYS A 73
SHEET 1 D 2 ILE A 91 ASN A 93 0
SHEET 2 D 2 LEU A 98 TYR A 100 -1 O LYS A 99 N GLU A 92
SSBOND 1 CYS A 8 CYS A 23 1555 1555 2.03
SSBOND 2 CYS A 59 CYS A 73 1555 1555 2.03
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 5 2 Bytes