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 SOURCE 4 FMOC SOLID-PHASE SYNTHESIS METHODS ON AN APPLIED SOURCE 5 BIOSYSTEMS 433A PEPTIDE 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 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 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER 6.0 REMARK 3 AUTHORS : KOLLMAN 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 RCSB ID CODE IS RCSB015598. 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 : XWINNMR 2.6, FELIX 95, CNS REMARK 210 1.0, AMBER 6.0 REMARK 210 METHOD USED : SIMULATED ANNEALING FROM REMARK 210 RANDOM STRUCTURES FOLLOWED BY REMARK 210 STEEPEST 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 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 ATOM 1 N ASN 1 -8.901 4.127 -0.555 1.00 0.00 N 1 ATOM 2 CA ASN A 1 -8.608 3.135 -1.618 1.00 0.00 C ATOM 3 C ASN A 1 -7.117 2.964 -1.897 1.00 0.00 C ATOM 4 O ASN A 1 -6.634 1.849 -1.758 1.00 0.00 O ATOM 5 CB ASN A 1 -9.437 3.396 -2.889 1.00 0.00 C ATOM 6 CG ASN A 1 -10.915 3.130 -2.611 1.00 0.00 C ATOM 7 OD1 ASN A 1 -11.269 2.700 -1.524 1.00 0.00 O ATOM 8 ND2 ASN A 1 -11.806 3.406 -3.543 1.00 0.00 N ATOM 9 H1 ASN A 1 -8.330 3.957 0.261 1.00 0.00 H ATOM 10 H2 ASN A 1 -8.740 5.068 -0.889 1.00 0.00 H ATOM 11 H3 ASN A 1 -9.877 4.041 -0.293 1.00 0.00 H ATOM 12 HA ASN A 1 -8.930 2.162 -1.239 1.00 0.00 H ATOM 13 HB2 ASN A 1 -9.310 4.417 -3.193 1.00 0.00 H ATOM 14 HB3 ASN A 1 -9.108 2.719 -3.679 1.00 0.00 H ATOM 15 HD21 ASN A 1 -11.572 3.791 -4.444 1.00 0.00 H ATOM 16 HD22 ASN A 1 -12.757 3.183 -3.294 1.00 0.00 H ATOM 17 N LEU A 2 -6.379 4.031 -2.228 1.00 0.00 N ATOM 18 CA LEU A 2 -4.923 4.002 -2.452 1.00 0.00 C ATOM 19 C LEU A 2 -4.136 3.187 -1.404 1.00 0.00 C ATOM 20 O LEU A 2 -3.391 2.274 -1.760 1.00 0.00 O ATOM 21 CB LEU A 2 -4.411 5.450 -2.619 1.00 0.00 C ATOM 22 CG LEU A 2 -4.795 6.450 -1.495 1.00 0.00 C ATOM 23 CD1 LEU A 2 -3.612 6.803 -0.599 1.00 0.00 C ATOM 24 CD2 LEU A 2 -5.351 7.748 -2.084 1.00 0.00 C ATOM 25 H LEU A 2 -6.821 4.923 -2.394 1.00 0.00 H ATOM 26 HA LEU A 2 -4.750 3.494 -3.403 1.00 0.00 H ATOM 27 HB2 LEU A 2 -3.340 5.414 -2.672 1.00 0.00 H ATOM 28 HB3 LEU A 2 -4.813 5.817 -3.564 1.00 0.00 H ATOM 29 HG LEU A 2 -5.568 6.022 -0.858 1.00 0.00 H ATOM 30 HD11 LEU A 2 -3.207 5.905 -0.146 1.00 0.00 H ATOM 31 HD12 LEU A 2 -2.841 7.304 -1.183 1.00 0.00 H ATOM 32 HD13 LEU A 2 -3.929 7.477 0.197 1.00 0.00 H ATOM 33 HD21 LEU A 2 -4.607 8.209 -2.736 1.00 0.00 H ATOM 34 HD22 LEU A 2 -6.255 7.544 -2.657 1.00 0.00 H ATOM 35 HD23 LEU A 2 -5.592 8.445 -1.281 1.00 0.00 H ATOM 36 N TYR A 3 -4.354 3.455 -0.111 1.00 0.00 N TER 36 SER A 20 ENDMDL MODEL 2 ATOM 1 Hg ASN A 1 -6.919 6.901 0.917 1.00 0.00 N ATOM 2 CA ASN A 1 -7.682 6.025 -0.010 1.00 0.00 Hg ATOM 3 C ASN A 1 -6.840 4.889 -0.589 1.00 0.00 C ATOM 4 O ASN A 1 -7.106 3.741 -0.253 1.00 0.00 O ATOM 5 CB ASN A 1 -8.428 6.847 -1.072 1.00 0.00 C ATOM 6 CG ASN A 1 -9.504 7.659 -0.362 1.00 0.00 C ATOM 7 OD1 ASN A 1 -9.180 8.568 0.382 1.00 0.00 O ATOM 8 ND2 ASN A 1 -10.768 7.290 -0.468 1.00 0.00 N ATOM 9 H1 ASN A 1 -6.513 6.358 1.667 1.00 0.00 H ATOM 10 H2 ASN A 1 -6.191 7.398 0.422 1.00 0.00 H ATOM 11 H3 ASN A 1 -7.553 7.592 1.308 1.00 0.00 H ATOM 12 HA ASN A 1 -8.451 5.523 0.581 1.00 0.00 H ATOM 13 HB2 ASN A 1 -7.743 7.506 -1.571 1.00 0.00 H ATOM 14 HB3 ASN A 1 -8.886 6.189 -1.811 1.00 0.00 H ATOM 15 HD21 ASN A 1 -11.078 6.519 -1.037 1.00 0.00 H ATOM 16 HD22 ASN A 1 -11.417 7.848 0.064 1.00 0.00 H ATOM 17 N LEU A 2 -5.819 5.175 -1.412 1.00 0.00 N ATOM 18 CA LEU A 2 -5.020 4.162 -2.130 1.00 0.00 C ATOM 19 C LEU A 2 -4.244 3.179 -1.224 1.00 0.00 C ATOM 20 O LEU A 2 -3.761 2.148 -1.693 1.00 0.00 O ATOM 21 CB LEU A 2 -4.073 4.863 -3.128 1.00 0.00 C ATOM 22 CG LEU A 2 -4.831 5.608 -4.250 1.00 0.00 C ATOM 23 CD1 LEU A 2 -5.010 7.109 -3.963 1.00 0.00 C ATOM 24 CD2 LEU A 2 -4.110 5.465 -5.592 1.00 0.00 C ATOM 25 H LEU A 2 -5.631 6.133 -1.665 1.00 0.00 H ATOM 26 HA LEU A 2 -5.709 3.545 -2.710 1.00 0.00 H ATOM 27 HB2 LEU A 2 -3.472 5.572 -2.591 1.00 0.00 H ATOM 28 HB3 LEU A 2 -3.451 4.089 -3.583 1.00 0.00 H ATOM 29 HG LEU A 2 -5.820 5.160 -4.359 1.00 0.00 H ATOM 30 HD11 LEU A 2 -5.173 7.303 -2.907 1.00 0.00 H ATOM 31 HD12 LEU A 2 -4.124 7.663 -4.273 1.00 0.00 H ATOM 32 HD13 LEU A 2 -5.867 7.480 -4.526 1.00 0.00 H ATOM 33 HD21 LEU A 2 -3.114 5.904 -5.535 1.00 0.00 H ATOM 34 HD22 LEU A 2 -4.023 4.410 -5.855 1.00 0.00 H ATOM 35 HD23 LEU A 2 -4.683 5.969 -6.371 1.00 0.00 H ATOM 36 N TYR A 3 -4.181 3.456 0.082 1.00 0.00 N TER 36 SER A 20 ENDMDL