Header list of 1l2y.pdb file
Complete list - 9 20 Bytes
HEADER DE NOVO PROTEIN 25-FEB-02 1L2Y
TITLE NMR STRUCTURE OF TRP-CAGE MINIPROTEIN CONSTRUCT TC5B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TC5B;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS SYNTHESIZED USING STANDARD FMOC
SOURCE 4 SOLID-PHASE SYNTHESIS METHODS ON AN APPLIED BIOSYSTEMS 433A PEPTIDE
SOURCE 5 SYNTHESIZER.
KEYWDS MINIPROTEIN, TWO-STATE FOLDING, TRP-CAGE, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 38
AUTHOR J.W.NEIDIGH,R.M.FESINMEYER,N.H.ANDERSEN
REVDAT 4 14-JUN-23 1L2Y 1 REMARK
REVDAT 3 05-FEB-20 1L2Y 1 REMARK
REVDAT 2 24-FEB-09 1L2Y 1 VERSN
REVDAT 1 29-MAY-02 1L2Y 0
JRNL AUTH J.W.NEIDIGH,R.M.FESINMEYER,N.H.ANDERSEN
JRNL TITL DESIGNING A 20-RESIDUE PROTEIN.
JRNL REF NAT.STRUCT.BIOL. V. 9 425 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 11979279
JRNL DOI 10.1038/NSB798
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 6.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 169 NOE DISTANCE CONSTRAINTS WERE
REMARK 3 EMPLOYED. CNS WAS EMPLOYED FOR S.A., FOLLOWED BY MINIMIZATION
REMARK 3 USING THE SANDER MODULE OF AMBER.
REMARK 4
REMARK 4 1L2Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015598.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 282
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0-1.8 MM TC5B
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, CNS 1.0, AMBER 6.0
REMARK 210 METHOD USED : SIMULATED ANNEALING FROM RANDOM
REMARK 210 STRUCTURES FOLLOWED BY STEEPEST
REMARK 210 DESCENT MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 38
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 O ASP A 9 HG SER A 14 1.55
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 2 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 13 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 4.7 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 5 LEU A 2 -34.83 72.95
REMARK 500 6 LEU A 2 -33.93 63.45
REMARK 500 9 LEU A 2 -18.34 57.13
REMARK 500 13 LEU A 2 -33.72 66.32
REMARK 500 18 LEU A 2 -3.11 60.50
REMARK 500 19 LEU A 2 -1.16 58.98
REMARK 500 20 LEU A 2 -32.96 68.39
REMARK 500 23 LEU A 2 -47.12 63.92
REMARK 500 28 LEU A 2 -2.46 61.26
REMARK 500 29 LEU A 2 -42.02 66.43
REMARK 500 34 PRO A 12 11.15 -66.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5292 RELATED DB: BMRB
REMARK 900 BMRB 5292 IS CHEMICAL SHIFTS FOR TC5B IN BUFFER AND BUFFER
REMARK 900 CONTAINING 30 VOL-% TFE.
REMARK 900 RELATED ID: 1JRJ RELATED DB: PDB
REMARK 900 1JRJ IS AN ANALAGOUS C-TERMINAL STRUCTURE.
DBREF 1L2Y A 1 20 PDB 1L2Y 1L2Y 1 20
SEQRES 1 A 20 ASN LEU TYR ILE GLN TRP LEU LYS ASP GLY GLY PRO SER
SEQRES 2 A 20 SER GLY ARG PRO PRO PRO SER
HELIX 1 1 ASN A 1 ASP A 9 1 9
HELIX 2 2 GLY A 10 GLY A 15 5 6
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 - 9 20 Bytes