Header list of 1iiy.pdb file
Complete list - 29 20 Bytes
HEADER ANTIVIRAL PROTEIN 24-APR-01 1IIY
TITLE SOLUTION NMR STRUCTURE OF COMPLEX OF 1:2 CYANOVIRIN-N:MAN-ALPHA1,2-
TITLE 2 MAN-ALPHA RESTRAINED REGULARIZED MEAN COORDINATES
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, MAN-ALPHA1, 2-MAN-ALPHA, ANTIVIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR C.A.BEWLEY
REVDAT 3 29-JUL-20 1IIY 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 24-FEB-09 1IIY 1 VERSN
REVDAT 1 24-OCT-01 1IIY 0
JRNL AUTH C.A.BEWLEY
JRNL TITL SOLUTION STRUCTURE OF A CYANOVIRIN-N:MAN ALPHA 1-2MAN ALPHA
JRNL TITL 2 COMPLEX. STRUCTURAL BASIS FOR HIGH AFFINITY
JRNL TITL 3 CARBOHYDRATE-MEDIATED BINDING TO GP120
JRNL REF STRUCTURE V. 9 931 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11591348
JRNL DOI 10.1016/S0969-2126(01)00653-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE OF THE 1:1 COMPLEX IN
REMARK 3 WHICH DISACCHARIDE IS BOUND EXCLUSIVELY THROUGH THE HIGH
REMARK 3 AFFINITY SITE WAS CALCULATED USING CONJOINED RIGID BODY/TORSION
REMARK 3 ANGLE DYNAMICS (BEWLEY AND CLORE (2000) J.AM.CHEM.SOC. 122, 6009-
REMARK 3 6016; WANG ET AL. (2001) EMBO. J., 19, 5635-5649 & REFS THEREIN)
REMARK 3 IN WHICH THE PROTEIN BACKBONE AND NON-INTERFACIAL SIDE CHAINS
REMARK 3 ARE HELD FIXED AND THE DISACCHARIDE AND INTERFACIAL SIDE CHAINS
REMARK 3 ARE FREE TO TRANSLATE AND ROTATE SUBJECT TO EXPERIMENTAL
REMARK 3 DISTANCE AND TORSION ANGLE RESTRAINTS. THE STRUCTURE OF THE
REMARK 3 DISACCHARIDE BOUND THROUGH THE LOW AFFINITY SITE IS A MODEL
REMARK 3 CALCULATED FROM A COMBINATION OF EXPERIMENTAL DISTANCE AND
REMARK 3 TORSION ANGLE RESTRAINTS, AND ADDITIONAL RESTRAINTS INTRODUCED
REMARK 3 ON THE BASIS OF SYMMETRY PRESENT BETWEEN THE TWO DOMAINS (HIGH
REMARK 3 AND LOW AFFINITY). THE NMR COORDINATES FOR MONOMERIC CVN (PDB
REMARK 3 ACC. 2EZM) WERE USED FOR THE STARTING COORDINATES WITH 2 EQ. OF
REMARK 3 MAN-ALPHA-1,2-MAN-ALPHA POSITIONED WITHIN 10 A OF THE PREVIOUSLY
REMARK 3 MAPPED CARBOHYDRATE BINDING SITES (BEWLEY & OTERO-QUINTERO (2001)
REMARK 3 J.AM.CHEM.SOC. IN PRESS).
REMARK 4
REMARK 4 1IIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013314.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.4
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 HCCH-COSY; HCCH-TOCSY; 15N-
REMARK 210 SEPARATED HOHAHA; QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING
REMARK 210 CONSTANTS; DIPOLAR COUPLINGS
REMARK 210 OBTAINED BY TAKING THE
REMARK 210 DIFFERENCE IN THE J SPLITTINGS
REMARK 210 IN ISOTROPIC MEDIUM AND IN A
REMARK 210 LIQUID CRYSTALLINE MEDIUM (5%
REMARK 210 C12E5, R=0.96) (RUCKERT & OTTING
REMARK 210 (2000) J.AM.CHEM.SOC. 122, 7793-
REMARK 210 7797) MEASURED IN 2D IPAP (15N,
REMARK 210 1H)-HSQC EXPERIMENTS (OTTIGER ET
REMARK 210 AL (1998) J.AM.CHEM.SOC. 131,
REMARK 210 373-378); INTERMOLECULAR
REMARK 210 DISTANCE RESTRAINTS OBTAINED
REMARK 210 FROM 12C-FILTERED/13C-SEPARATED
REMARK 210 AND 15N-SEPARATED NOE
REMARK 210 EXPERIMENTS ON COMPLEXES
REMARK 210 COMPRISING 1:1 AND 1:2 CVN:MAN-
REMARK 210 ALPHA-(1,2)-MAN-ALPHA; INTRA-
REMARK 210 DISACCHARIDE AND INTER-
REMARK 210 MANNOPYRANOSE DISTANCE
REMARK 210 RESTRAINTS OBTAINED FROM 12C-
REMARK 210 FILTERED NOE AND HOHAHA
REMARK 210 EXPERIMENTS ON COMPLEXES
REMARK 210 COMPRISING 1:1 AND 1:2 CVN:MAN-
REMARK 210 ALPHA-(1,2)-MAN-ALPHA.
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CONJOINED RIGID BODY/TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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:
REMARK 210 THIS STRUCTURE IS THE RESTRAINED REGULARIZED MEAN STRUCTURE.
REMARK 210
REMARK 210
REMARK 210 IN THIS ENTRY THE ELEVENTH COLUMN OF THE COORDINATES (WITH "ATOM"
REMARK 210 AS THE FIRST COLUMN) REPRESENTS THE AVERAGE RMS
REMARK 210 DIFFERENCE BETWEEN THE 50 INDIVIDUAL SIMULATED ANNEALING
REMARK 210 STRUCTURES HAVING ZERO DISTANCE VIOLATIONS GREATER THAN
REMARK 210 0.2 A AND ZERO DIHEDRAL ANGLE VIOLATIONS GREATER THAN 5 DEG.
REMARK 210 THE AVERAGE STRUCTURE WAS GENERATED BY BEST FITTING TO
REMARK 210 THE BACKBONE OF RESIDUES 1-101. NOTE THE OCCUPANCY FIELD IN THE
REMARK 210 TENTH COLUMN HAS NO MEANING.
REMARK 210 AVE.RMS DIFF. TO MEAN FOR INTERFACIAL SIDE CHAINS AND
REMARK 210 DISACCHARIDE OF THE HIGH AFFINITY SITE=0.36.
REMARK 210 AVE.RMS DIFF. TO MEAN FOR INTERFACIAL SIDE CHAINS AND
REMARK 210 DISACCHARIDE OF THE LOW AFFINITY SITE=0.58.
REMARK 210 RMS DEVIATIONS FOR BONDS, ANGLES, IMPROPERS, NOE, CDIH
REMARK 210 6.389414E-03 0.717363 0.693234 8.897236E-03 9.181435E-02.
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, B, C
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: 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 SER A 52 12.36 174.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 RESIDUE NUMBERING:
REMARK 600 CVN:1-101
REMARK 600 MAN:201/202 (CHAIN B) CORRESPONDS TO
REMARK 600 MAN-ALPHA-1,2-MAN-ALPHA BOUND THROUGH THE
REMARK 600 HIGH AFFINITY SITE WITH C1-C6 OF MAN 201 CORRESPONDING
REMARK 600 TO THE REDUCING MANNOPYRANOSE RING AND C1-C6 OF MAN 202
REMARK 600 CORRESPONDING TO C1-C6 OF THE NONREDUCING PYRANOSE.
REMARK 600 MAN:203/204 (CHAIN C) CORRESPONDS TO
REMARK 600 MAN-ALPHA-1,2-MAN-ALPHA BOUND THROUGH THE LOW AFFINITY
REMARK 600 SITE WITH C1-C6 OF MAN 203 CORRESPONDING TO THE REDUCING
REMARK 600 MANNOPYRANOSE RING AND C1-C6 OF MAN 204 CORRESPONDING
REMARK 600 TO C1-C6 OF THE NONREDUCING PYRANOSE.
DBREF 1IIY 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
HET MAN B 1 23
HET MAN B 2 22
HET MAN C 1 23
HET MAN C 2 22
HETNAM MAN ALPHA-D-MANNOPYRANOSE
FORMUL 2 MAN 4(C6 H12 O6)
HELIX 1 1 LYS A 3 GLN A 6 5 4
HELIX 2 2 ASN A 53 GLU A 56 5 4
SHEET 1 A 3 CYS A 8 GLN A 14 0
SHEET 2 A 3 VAL A 17 GLU A 23 -1 N VAL A 17 O GLN A 14
SHEET 3 A 3 TYR A 29 ASP A 35 -1 N ASN A 30 O 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 SER A 46 N VAL A 43
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 N VAL A 81 O CYS A 73
SHEET 1 D 2 ILE A 91 ILE A 94 0
SHEET 2 D 2 THR A 97 TYR A 100 -1 O THR A 97 N ILE A 94
SSBOND 1 CYS A 8 CYS A 22 1555 1555 2.02
SSBOND 2 CYS A 58 CYS A 73 1555 1555 2.02
LINK O2 MAN B 1 C1 MAN B 2 1555 1555 1.44
LINK O2 MAN C 1 C1 MAN C 2 1555 1555 1.44
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 - 29 20 Bytes