Header list of 2ezn.pdb file
Complete list - r 9 2 Bytes
HEADER HIV-INACTIVATING PROTEIN 06-MAY-98 2EZN
TITLE SOLUTION NMR STRUCTURE OF CYANOVIRIN-N ENSEMBLE OF 40 SIMULATED
TITLE 2 ANNEALING STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYANOVIRIN-N;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC ELLIPSOSPORUM;
SOURCE 3 ORGANISM_TAXID: 45916
KEYWDS HIV-INACTIVATING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR C.A.BEWLEY,A.M.GRONENBORN,G.M.CLORE
REVDAT 3 09-MAR-22 2EZN 1 REMARK
REVDAT 2 24-FEB-09 2EZN 1 VERSN
REVDAT 1 11-MAY-99 2EZN 0
JRNL AUTH C.A.BEWLEY,K.R.GUSTAFSON,M.R.BOYD,D.G.COVELL,A.BAX,
JRNL AUTH 2 G.M.CLORE,A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE OF CYANOVIRIN-N, A POTENT
JRNL TITL 2 HIV-INACTIVATING PROTEIN.
JRNL REF NAT.STRUCT.BIOL. V. 5 571 1998
JRNL REFN ISSN 1072-8368
JRNL PMID 9665171
JRNL DOI 10.1038/828
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 AVE.RMS DIFF. TO MEAN FOR ALL NON-H-ATOMS (RESIDUES
REMARK 3 1:101)= 0.433636
REMARK 3
REMARK 3 AVE.RMS DIFF. TO MEAN FOR BACKBONE ATOMS (N, CA, C', O)
REMARK 3 (RESIDUES 1:101)= 0.139826
REMARK 3
REMARK 3 RMS DEVIATIONS FOR BONDS, ANGLES, IMPROPERS, CDIH, NOE,
REMARK 3 COUP 5.067337E-03, 0.712983, 0.667194, 0.157308,
REMARK 3 1.428009E-02, 0.608909
REMARK 3 C13CA AND CB SHIFTS RMS : 0.852581, 1.15742
REMARK 3
REMARK 3 JCOUP STATS: NON-GLY RESIDUES GLY
REMARK 3 RMS-D: 0.608909 1.46813
REMARK 3
REMARK 3 BACKBONE DIPOLAR COUPLINGS NH CH CACO NCO HNCO
REMARK 3 RMS : 0.466712 1.15058 1.29414 0.572019 1.2653
REMARK 3
REMARK 3 SIDECHAIN DIPOLAR COUPLINGS CH CH3S CH3D ARO
REMARK 3 RMS DIPO_SIDE: 1.6875 0.796796 0.531907 0.160016
REMARK 3
REMARK 3 RMS FOR 1H SHIFTS: ALL ALPHA ALPHA_GLY METHYL(S)
REMARK 3 METHYL(D) OTHER(S) OTHER(D)
REMARK 3 RMS PROT: 0.263524 0.243015 0.23853 0.115892 0.148148
REMARK 3 0.267304 0.300122
REMARK 3
REMARK 3 IN THE RESTRAINED REGULARIZED MEAN COORDINATES (2EZM) THE
REMARK 3 LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN
REMARK 3 THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN
REMARK 3 COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA
REMARK 3 STRUCTURES (2EZN) HAS NO MEANING. BEST FITTING TO GENERATE
REMARK 3 THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 1-101.
REMARK 3 NOTE THE OCCUPANCY FIELD HAS NO MEANING.
REMARK 4
REMARK 4 2EZN 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_1000178064.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE FOR ASSIGNMENT
REMARK 210 OF PROTEIN: CBCA(CO)NH; CBCANH;
REMARK 210 HNCO; C(CO)NH; H(CCO)NH; HCCH-
REMARK 210 COSY; HCCH-TOCSY; HNHA; 15N-
REMARK 210 SEPARATED HOHAHA; QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING
REMARK 210 CONSTANTS; 3D 15N-SEPARATED NOE;
REMARK 210 3D 13C-SEPARATED NOE AND ROE; 4D
REMARK 210 15N/13C-SEPARATED NOE; 4D 13C/
REMARK 210 13C-SEPARATED NOE EXPERIMENTS;
REMARK 210 3D HCA(CO)N FOR THREE-BOND
REMARK 210 AMINIDE DEUTERIUM ISOTOPE SHIFTS;
REMARK 210 VARIOUS COUPLED 2D AND 3D
REMARK 210 SPECTRA TO MEASURE THE N-H; CA-H;
REMARK 210 C-H CA-C'; N-C'; HN-C' DIPOLAR
REMARK 210 COUPLINGS OBTAINED BY TAKING THE
REMARK 210 DIFFERENCE IN THE J SPLITTINGS
REMARK 210 IN ISOTROPIC MEDIUM; IN A LIQUID
REMARK 210 CRYSTALLINE MEDIUM (4% 3:1 DMPC:
REMARK 210 DHPC).
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS (SEE ABOVE) ABOVE)
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE 3D STRUCTURE OF CYANOVIRIN SOLVED BY MULTI-DIMENSIONAL
REMARK 210 HETERONUCLEAR NMR AND IS BASED ON 2597 EXPERIMENTAL NMR
REMARK 210 RESTRAINTS: 419 SEQUENTIAL (|I- J|=1), 170 MEDIUM RANGE (1 < |I-
REMARK 210 J| <=5) AND 554 LONG RANGE (|I-J| >5) INTERRESIDUES AND 19
REMARK 210 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 109
REMARK 210 DISTANCE RESTRAINTS FOR 55 H-BONDS; 339 TORSION ANGLE RESTRAINTS
REMARK 210 (100 PHI, 98 PSI, 76 CHI1, 48 CHI2, 15 CHI3, 2 CHI4); 82 THREE-
REMARK 210 BOND HN-HA COUPLING CONSTANT RESTRAINTS; 157 (82 CALPHA AND 75
REMARK 210 CBETA) 13C SHIFT RESTRAINTS; 362 1H SHIFT RESTRAINTS; AND 386
REMARK 210 DIPOLAR COUPLING RESTRAINTS (82 N-H, 76 C-H, 43 CA-C', 65 N-C'
REMARK 210 62 HNC', 58 SIDE-CHAIN C-H). THE STRUCTURES WERE CALCULATED
REMARK 210 USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988)
REMARK 210 FEBS LETT. 229, 129-136 USING THE PROGRAM CNS (BRUNGER ET AL.
REMARK 210 ACTA CRYST SERIES D IN PRESS) MODIFIED TO INCORPORATE COUPLING
REMARK 210 CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-
REMARK 210 103), CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN.
REMARK 210 RESON. SERIES B 106, 92-96), 1H CHEMICAL SHIFT (KUSZEWSKI ET AL.
REMARK 210 (1995) J. MAGN. RESON. SERIES B 107, 293-297; KUSZEWSKI ET AL.
REMARK 210 (1996) J. MAGN. RESON. SERIES B 112, 79-81), AND DIPOLAR
REMARK 210 COUPLING (CLORE ET AL. (1998) J. MAGN. RESON. 131, 159-162)
REMARK 210 RESTRAINTS, AND A CONFORMATIONAL DATABASE POTENTIAL (KUSZEWSKI
REMARK 210 ET AL. (1996) PROTEIN SCI. 5, 1067-1080; KUSZEWSKI ET AL. (1997)
REMARK 210 J. MAGN. RESON 125, 171-177).
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: 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 PHE A 4 -18.97 -47.30
REMARK 500 1 SER A 52 12.31 178.78
REMARK 500 1 ASN A 53 62.58 60.01
REMARK 500 2 PHE A 4 -19.96 -48.14
REMARK 500 2 SER A 52 15.59 -179.77
REMARK 500 3 SER A 52 8.46 169.97
REMARK 500 3 ILE A 55 -17.72 -46.24
REMARK 500 4 ASN A 26 31.65 -93.59
REMARK 500 4 SER A 52 15.79 168.04
REMARK 500 5 PHE A 4 -20.00 -48.46
REMARK 500 5 ASN A 26 31.00 -91.15
REMARK 500 5 SER A 52 15.17 161.95
REMARK 500 6 SER A 52 16.07 165.37
REMARK 500 7 SER A 52 12.02 166.18
REMARK 500 8 ASN A 26 30.76 -90.52
REMARK 500 8 SER A 52 13.06 165.15
REMARK 500 9 SER A 52 10.02 168.57
REMARK 500 9 ASN A 53 60.25 60.10
REMARK 500 10 PHE A 4 -19.86 -48.56
REMARK 500 10 SER A 52 15.42 178.43
REMARK 500 11 PHE A 4 -20.00 -49.69
REMARK 500 11 SER A 52 13.24 -179.31
REMARK 500 12 PHE A 4 -19.86 -47.62
REMARK 500 12 SER A 52 16.46 178.58
REMARK 500 13 SER A 52 13.56 179.33
REMARK 500 14 SER A 52 14.04 177.39
REMARK 500 15 SER A 52 12.53 168.55
REMARK 500 16 ASN A 26 30.42 -93.01
REMARK 500 16 SER A 52 13.03 179.27
REMARK 500 16 HIS A 90 -10.18 -140.12
REMARK 500 17 PHE A 4 -19.15 -47.75
REMARK 500 17 SER A 52 12.83 167.37
REMARK 500 18 SER A 52 14.95 165.84
REMARK 500 18 HIS A 90 -10.20 -140.01
REMARK 500 19 ASN A 26 30.70 -94.04
REMARK 500 19 SER A 52 11.71 -178.59
REMARK 500 19 ASN A 53 62.64 60.09
REMARK 500 20 SER A 52 12.55 166.50
REMARK 500 21 ASN A 26 30.10 -91.83
REMARK 500 21 SER A 52 16.10 166.74
REMARK 500 22 ASN A 26 30.38 -95.69
REMARK 500 22 SER A 52 14.25 179.67
REMARK 500 23 SER A 52 12.33 162.53
REMARK 500 24 SER A 52 13.15 166.63
REMARK 500 25 SER A 52 9.24 166.13
REMARK 500 25 ILE A 55 -18.26 -47.70
REMARK 500 26 SER A 52 12.43 173.48
REMARK 500 27 ASN A 26 30.98 -92.89
REMARK 500 27 SER A 52 10.51 166.40
REMARK 500 28 LYS A 3 18.18 80.37
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2EZN A 1 101 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
HELIX 1 1 PHE A 4 GLN A 6 5 3
HELIX 2 2 LEU A 36 SER A 38 5 3
HELIX 3 3 PHE A 54 GLU A 56 5 3
HELIX 4 4 LEU A 87 ASP A 89 5 3
SHEET 1 A 3 ALA A 12 GLN A 14 0
SHEET 2 A 3 VAL A 17 GLU A 23 -1 N THR A 19 O ALA A 12
SHEET 3 A 3 TYR A 29 ASP A 35 -1 N ILE A 34 O LEU A 18
SHEET 1 B 2 ILE A 40 VAL A 43 0
SHEET 2 B 2 SER A 46 TRP A 49 -1 N LYS A 48 O GLU A 41
SHEET 1 C 3 GLN A 62 ALA A 64 0
SHEET 2 C 3 GLU A 68 LYS A 74 -1 N ALA A 70 O GLN A 62
SHEET 3 C 3 PHE A 80 ASN A 86 -1 N ILE A 85 O LEU A 69
SSBOND 1 CYS A 8 CYS A 22 1555 1555 2.03
SSBOND 2 CYS A 58 CYS A 73 1555 1555 2.02
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 9 2 Bytes