HEADER BLOOD CLOTTING 15-JAN-10 SMS20118 TITLE A 15-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINAL DOMAIN OF THE GQ TITLE 2 PROTEIN ALPHA SUBUNIT (GAQ-CT PEPTIDE) WAS SYNTHESIZED AND TITLE 3 CHARACTERIZED USING NMR SPECTROSCOPIC STUDIES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 345-359; COMPND 5 SYNONYM: GQ PROTEIN ALPHA SUBUNIT, GUANINE NUCLEOTIDE-BINDING PROTEIN COMPND 6 ALPHA-Q; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: GAQ-CT PEPTIDE SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606; SOURCE 6 OTHER_DETAILS: CHEMICAL SYNTHESIS KEYWDS CALCIUM BINDING PROTEINS, CALCIUM INTRACELLULAR RELEASE, KEYWDS 2 CYCLOOXYGENASE (COX) PATHWAY, G PROTEIN COUPLED RECEPTORS (GPCR), KEYWDS 3 MEMBRANE LIPIDS, PROSTAGLANDINS, PROTEIN-PROTEIN INTERACTIONS, KEYWDS 4 RECEPTOR MODIFICATION, RECEPTOR STRUCTURE-FUNCTION, BLOOD CLOTTING EXPDTA SOLUTION NMR AUTHOR A.CHILLAR,J.WU,V.CERVANTES,K.-H.RUAN JRNL AUTH A.CHILLAR,J.WU,V.CERVANTES,K.-H.RUAN JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE C-TERMINUS OF JRNL TITL 2 GALPHAQ IN COMPLEX WITH THE HUMAN THROMBOXANE A2 RECEPTOR JRNL TITL 3 PROVIDES EVIDENCE OF CONSTITUTIVE ACTIVITY JRNL REF BIOCHEMISTRY V. 49 6365 2010 JRNL REFN ISSN 0006-2960 JRNL PMID 20590159 JRNL DOI 10.1021/BI100047N REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 2000 REMARK 3 AUTHORS : ACCELRYS SOFTWARE INC. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 NULL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-10. REMARK 100 THE BMRB ID CODE IS SMS20118. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1.1MM C-TERMINAL DOMAIN OF THE REMARK 210 GQ PROTEIN ALPHA SUBUNIT; 95% REMARK 210 H2O/5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D DQF-COSY; 2D 1H-1H TOCSY; 2D REMARK 210 1H-1H NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 2000 REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 6 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NULL 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 LEU A 9 H GLU A 11 2.16 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU A 11 CD GLU A 11 OE2 0.109 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 ASP A 2 CB - CG - OD2 ANGL. DEV. = -5.5 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 ASP A 2 87.05 65.63 REMARK 500 GLN A 6 -44.85 152.27 REMARK 500 LYS A 10 68.66 -69.72 REMARK 500 GLU A 11 -26.26 164.65 REMARK 500 TYR A 12 -57.43 -123.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 20118 RELATED DB: BMRB REMARK 900 RELATED ID: 20109 RELATED DB: BMRB REMARK 900 THE SAME PEPTIDE WITH DIFFERENT CRITERIA REMARK 900 RELATED ID: 20112 RELATED DB: BMRB REMARK 900 THE SAME PEPTIDE WITH DIFFERENT CRITERIA DBREF A 1 15 UNP P50148 GNAQ_HUMAN 345 359 SEQADV NH2 A 16 UNP P50148 AMIDATION SEQRES 1 A 16 LYS ASP THR ILE LEU GLN LEU ASN LEU LYS GLU TYR ASN SEQRES 2 A 16 LEU VAL NH2 HET NH2 A 16 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N 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 ATOM 1 N LYS A 1 9.822 0.742 -6.123 1.00 0.00 N ATOM 2 CA LYS A 1 10.017 1.730 -5.030 1.00 0.00 C ATOM 3 C LYS A 1 8.971 1.486 -3.900 1.00 0.00 C ATOM 4 O LYS A 1 7.783 1.750 -4.085 1.00 0.00 O ATOM 5 CB LYS A 1 9.957 3.180 -5.592 1.00 0.00 C ATOM 6 CG LYS A 1 11.243 3.714 -6.274 1.00 0.00 C ATOM 7 CD LYS A 1 11.464 3.157 -7.697 1.00 0.00 C ATOM 8 CE LYS A 1 12.207 4.134 -8.621 1.00 0.00 C ATOM 9 NZ LYS A 1 11.984 3.736 -10.024 1.00 0.00 N ATOM 10 H1 LYS A 1 10.194 -0.177 -5.862 1.00 0.00 H ATOM 11 H2 LYS A 1 8.816 0.602 -6.276 1.00 0.00 H ATOM 12 HA LYS A 1 11.032 1.582 -4.616 1.00 0.00 H ATOM 13 HB2 LYS A 1 9.088 3.292 -6.273 1.00 0.00 H ATOM 14 HB3 LYS A 1 9.719 3.877 -4.765 1.00 0.00 H ATOM 15 HG2 LYS A 1 11.164 4.818 -6.312 1.00 0.00 H ATOM 16 HG3 LYS A 1 12.134 3.522 -5.644 1.00 0.00 H ATOM 17 HD2 LYS A 1 12.010 2.194 -7.643 1.00 0.00 H ATOM 18 HD3 LYS A 1 10.480 2.891 -8.135 1.00 0.00 H ATOM 19 HE2 LYS A 1 11.843 5.171 -8.472 1.00 0.00 H ATOM 20 HE3 LYS A 1 13.292 4.153 -8.393 1.00 0.00 H ATOM 21 HZ1 LYS A 1 11.043 3.331 -10.121 1.00 0.00 H ATOM 22 HZ3 LYS A 1 11.976 4.558 -10.640 1.00 0.00 H ATOM 23 N ASP A 2 9.407 0.999 -2.719 1.00 0.00 N ATOM 24 CA ASP A 2 8.526 0.821 -1.518 1.00 0.00 C ATOM 25 C ASP A 2 7.381 -0.251 -1.660 1.00 0.00 C ATOM 26 O ASP A 2 6.230 0.081 -1.936 1.00 0.00 O ATOM 27 CB ASP A 2 8.013 2.197 -0.981 1.00 0.00 C ATOM 28 CG ASP A 2 9.027 2.989 -0.169 1.00 0.00 C ATOM 29 OD1 ASP A 2 9.166 2.865 1.042 1.00 0.00 O ATOM 30 OD2 ASP A 2 9.766 3.837 -0.932 1.00 0.00 O ATOM 31 H ASP A 2 10.423 0.881 -2.680 1.00 0.00 H ATOM 32 HA ASP A 2 9.181 0.415 -0.722 1.00 0.00 H ATOM 33 HB2 ASP A 2 7.632 2.830 -1.804 1.00 0.00 H ATOM 34 HB3 ASP A 2 7.129 2.056 -0.335 1.00 0.00 H ATOM 35 HD2 ASP A 2 10.358 4.322 -0.355 1.00 0.00 H ATOM 36 N THR A 3 7.651 -1.535 -1.366 1.00 0.00 N ATOM 37 CA THR A 3 6.588 -2.607 -1.301 1.00 0.00 C ATOM 38 C THR A 3 5.747 -2.718 0.037 1.00 0.00 C ATOM 39 O THR A 3 5.063 -3.721 0.261 1.00 0.00 O ATOM 40 CB THR A 3 7.203 -3.981 -1.736 1.00 0.00 C ATOM 41 OG1 THR A 3 8.421 -4.257 -1.049 1.00 0.00 O ATOM 42 CG2 THR A 3 7.476 -4.113 -3.243 1.00 0.00 C ATOM 43 H THR A 3 8.640 -1.771 -1.240 1.00 0.00 H ATOM 44 HA THR A 3 5.810 -2.378 -2.056 1.00 0.00 H ATOM 45 HB THR A 3 6.483 -4.788 -1.486 1.00 0.00 H ATOM 46 HG1 THR A 3 8.682 -5.146 -1.305 1.00 0.00 H ATOM 47 HG21 THR A 3 8.164 -3.331 -3.614 1.00 0.00 H ATOM 48 HG22 THR A 3 7.924 -5.092 -3.499 1.00 0.00 H ATOM 49 HG23 THR A 3 6.543 -4.030 -3.832 1.00 0.00 H ATOM 50 N ILE A 4 5.706 -1.669 0.879 1.00 0.00 N ATOM 51 CA ILE A 4 4.755 -1.541 2.035 1.00 0.00 C ATOM 52 C ILE A 4 3.723 -0.377 1.787 1.00 0.00 C ATOM 53 O ILE A 4 2.514 -0.613 1.710 1.00 0.00 O ATOM 54 CB ILE A 4 5.531 -1.477 3.409 1.00 0.00 C ATOM 55 CG1 ILE A 4 4.648 -1.989 4.599 1.00 0.00 C ATOM 56 CG2 ILE A 4 6.246 -0.121 3.687 1.00 0.00 C ATOM 57 CD1 ILE A 4 4.777 -1.310 5.977 1.00 0.00 C ATOM 58 H ILE A 4 6.234 -0.874 0.507 1.00 0.00 H ATOM 59 HA ILE A 4 4.133 -2.459 2.077 1.00 0.00 H ATOM 60 HB ILE A 4 6.354 -2.217 3.334 1.00 0.00 H ATOM 61 HG12 ILE A 4 3.576 -1.950 4.333 1.00 0.00 H ATOM 62 HG13 ILE A 4 4.842 -3.072 4.733 1.00 0.00 H ATOM 63 HG21 ILE A 4 6.917 -0.177 4.562 1.00 0.00 H ATOM 64 HG22 ILE A 4 6.862 0.219 2.835 1.00 0.00 H ATOM 65 HG23 ILE A 4 5.517 0.680 3.917 1.00 0.00 H ATOM 66 HD11 ILE A 4 4.420 -0.263 5.939 1.00 0.00 H ATOM 67 HD12 ILE A 4 4.175 -1.825 6.750 1.00 0.00 H ATOM 68 HD13 ILE A 4 5.822 -1.290 6.335 1.00 0.00 H ATOM 69 N LEU A 5 4.204 0.872 1.617 1.00 0.00 N ATOM 70 CA LEU A 5 3.375 2.060 1.280 1.00 0.00 C ATOM 71 C LEU A 5 3.075 2.136 -0.239 1.00 0.00 C ATOM 72 O LEU A 5 3.683 2.932 -0.954 1.00 0.00 O ATOM 73 CB LEU A 5 4.063 3.327 1.908 1.00 0.00 C ATOM 74 CG LEU A 5 3.648 4.763 1.434 1.00 0.00 C ATOM 75 CD1 LEU A 5 2.155 4.894 1.144 1.00 0.00 C ATOM 76 CD2 LEU A 5 3.966 5.843 2.490 1.00 0.00 C ATOM 77 H LEU A 5 5.215 0.936 1.763 1.00 0.00 H ATOM 78 HA LEU A 5 2.391 1.946 1.759 1.00 0.00 H ATOM 79 HB2 LEU A 5 3.921 3.249 3.003 1.00 0.00 H ATOM 80 HB3 LEU A 5 5.160 3.261 1.773 1.00 0.00 H ATOM 81 HG LEU A 5 4.192 5.005 0.496 1.00 0.00 H ATOM 82 HD11 LEU A 5 1.833 5.923 0.901 1.00 0.00 H ATOM 83 HD12 LEU A 5 1.790 4.275 0.308 1.00 0.00 H ATOM 84 HD13 LEU A 5 1.649 4.565 2.052 1.00 0.00 H ATOM 85 HD21 LEU A 5 3.787 5.489 3.522 1.00 0.00 H ATOM 86 HD22 LEU A 5 5.011 6.192 2.425 1.00 0.00 H ATOM 87 HD23 LEU A 5 3.340 6.752 2.376 1.00 0.00 H ATOM 88 N GLN A 6 2.114 1.314 -0.703 1.00 0.00 N ATOM 89 CA GLN A 6 1.908 0.964 -2.147 1.00 0.00 C ATOM 90 C GLN A 6 1.251 -0.447 -2.294 1.00 0.00 C ATOM 91 O GLN A 6 0.350 -0.561 -3.111 1.00 0.00 O ATOM 92 CB GLN A 6 3.178 1.147 -3.033 1.00 0.00 C ATOM 93 CG GLN A 6 3.307 0.462 -4.404 1.00 0.00 C ATOM 94 CD GLN A 6 4.663 0.764 -5.044 1.00 0.00 C ATOM 95 OE1 GLN A 6 4.969 1.887 -5.422 1.00 0.00 O ATOM 96 NE2 GLN A 6 5.530 -0.207 -5.150 1.00 0.00 N ATOM 97 H GLN A 6 1.741 0.712 0.040 1.00 0.00 H ATOM 98 HA GLN A 6 1.148 1.672 -2.534 1.00 0.00 H ATOM 99 HB2 GLN A 6 3.305 2.236 -3.194 1.00 0.00 H ATOM 100 HB3 GLN A 6 4.052 0.858 -2.426 1.00 0.00 H ATOM 101 HG2 GLN A 6 3.162 -0.626 -4.290 1.00 0.00 H ATOM 102 HG3 GLN A 6 2.508 0.812 -5.080 1.00 0.00 H ATOM 103 HE21 GLN A 6 5.301 -1.029 -4.590 1.00 0.00 H ATOM 104 HE22 GLN A 6 6.462 0.179 -5.326 1.00 0.00 H ATOM 105 N LEU A 7 1.683 -1.498 -1.569 1.00 0.00 N ATOM 106 CA LEU A 7 0.976 -2.821 -1.518 1.00 0.00 C ATOM 107 C LEU A 7 0.114 -3.014 -0.227 1.00 0.00 C ATOM 108 O LEU A 7 -1.077 -3.285 -0.338 1.00 0.00 O ATOM 109 CB LEU A 7 1.991 -3.971 -1.809 1.00 0.00 C ATOM 110 CG LEU A 7 2.056 -4.573 -3.249 1.00 0.00 C ATOM 111 CD1 LEU A 7 1.177 -5.829 -3.372 1.00 0.00 C ATOM 112 CD2 LEU A 7 1.710 -3.619 -4.409 1.00 0.00 C ATOM 113 H LEU A 7 2.525 -1.294 -1.024 1.00 0.00 H ATOM 114 HA LEU A 7 0.216 -2.874 -2.317 1.00 0.00 H ATOM 115 HB2 LEU A 7 3.010 -3.657 -1.513 1.00 0.00 H ATOM 116 HB3 LEU A 7 1.802 -4.802 -1.100 1.00 0.00 H ATOM 117 HG LEU A 7 3.102 -4.903 -3.409 1.00 0.00 H ATOM 118 HD11 LEU A 7 1.287 -6.311 -4.362 1.00 0.00 H ATOM 119 HD12 LEU A 7 1.452 -6.595 -2.623 1.00 0.00 H ATOM 120 HD13 LEU A 7 0.102 -5.607 -3.232 1.00 0.00 H ATOM 121 HD21 LEU A 7 2.329 -2.707 -4.393 1.00 0.00 H ATOM 122 HD22 LEU A 7 1.849 -4.090 -5.399 1.00 0.00 H ATOM 123 HD23 LEU A 7 0.656 -3.287 -4.379 1.00 0.00 H ATOM 124 N ASN A 8 0.673 -2.853 0.985 1.00 0.00 N ATOM 125 CA ASN A 8 -0.115 -2.823 2.257 1.00 0.00 C ATOM 126 C ASN A 8 -1.016 -1.550 2.501 1.00 0.00 C ATOM 127 O ASN A 8 -2.037 -1.684 3.175 1.00 0.00 O ATOM 128 CB ASN A 8 0.873 -3.216 3.399 1.00 0.00 C ATOM 129 CG ASN A 8 0.581 -2.773 4.836 1.00 0.00 C ATOM 130 OD1 ASN A 8 0.218 -3.552 5.705 1.00 0.00 O ATOM 131 ND2 ASN A 8 0.734 -1.508 5.136 1.00 0.00 N ATOM 132 H ASN A 8 1.657 -2.572 0.944 1.00 0.00 H ATOM 133 HA ASN A 8 -0.851 -3.652 2.214 1.00 0.00 H ATOM 134 HB2 ASN A 8 0.926 -4.321 3.419 1.00 0.00 H ATOM 135 HB3 ASN A 8 1.909 -2.913 3.169 1.00 0.00 H ATOM 136 HD21 ASN A 8 0.772 -0.898 4.315 1.00 0.00 H ATOM 137 HD22 ASN A 8 0.307 -1.287 6.039 1.00 0.00 H ATOM 138 N LEU A 9 -0.690 -0.336 2.021 1.00 0.00 N ATOM 139 CA LEU A 9 -1.683 0.789 2.002 1.00 0.00 C ATOM 140 C LEU A 9 -2.881 0.598 1.001 1.00 0.00 C ATOM 141 O LEU A 9 -4.035 0.818 1.389 1.00 0.00 O ATOM 142 CB LEU A 9 -0.971 2.163 1.846 1.00 0.00 C ATOM 143 CG LEU A 9 -0.706 2.924 3.177 1.00 0.00 C ATOM 144 CD1 LEU A 9 0.565 2.442 3.903 1.00 0.00 C ATOM 145 CD2 LEU A 9 -0.703 4.444 2.924 1.00 0.00 C ATOM 146 H LEU A 9 0.174 -0.347 1.470 1.00 0.00 H ATOM 147 HA LEU A 9 -2.183 0.803 2.993 1.00 0.00 H ATOM 148 HB2 LEU A 9 -0.047 2.079 1.242 1.00 0.00 H ATOM 149 HB3 LEU A 9 -1.614 2.807 1.213 1.00 0.00 H ATOM 150 HG LEU A 9 -1.545 2.745 3.877 1.00 0.00 H ATOM 151 HD11 LEU A 9 0.669 2.895 4.905 1.00 0.00 H ATOM 152 HD12 LEU A 9 0.572 1.346 4.049 1.00 0.00 H ATOM 153 HD13 LEU A 9 1.489 2.711 3.379 1.00 0.00 H ATOM 154 HD21 LEU A 9 -1.719 4.868 2.965 1.00 0.00 H ATOM 155 HD22 LEU A 9 -0.079 5.007 3.644 1.00 0.00 H ATOM 156 HD23 LEU A 9 -0.359 4.704 1.907 1.00 0.00 H ATOM 157 N LYS A 10 -2.627 0.143 -0.245 1.00 0.00 N ATOM 158 CA LYS A 10 -3.681 -0.423 -1.147 1.00 0.00 C ATOM 159 C LYS A 10 -4.230 -1.836 -0.655 1.00 0.00 C ATOM 160 O LYS A 10 -3.970 -2.898 -1.212 1.00 0.00 O ATOM 161 CB LYS A 10 -3.133 -0.296 -2.614 1.00 0.00 C ATOM 162 CG LYS A 10 -2.465 -1.533 -3.257 1.00 0.00 C ATOM 163 CD LYS A 10 -1.996 -1.366 -4.720 1.00 0.00 C ATOM 164 CE LYS A 10 -2.960 -1.925 -5.779 1.00 0.00 C ATOM 165 NZ LYS A 10 -3.124 -3.389 -5.630 1.00 0.00 N ATOM 166 H LYS A 10 -1.631 0.034 -0.457 1.00 0.00 H ATOM 167 HA LYS A 10 -4.551 0.261 -1.114 1.00 0.00 H ATOM 168 HB2 LYS A 10 -3.964 0.013 -3.273 1.00 0.00 H ATOM 169 HB3 LYS A 10 -2.415 0.547 -2.698 1.00 0.00 H ATOM 170 HG2 LYS A 10 -1.632 -1.856 -2.613 1.00 0.00 H ATOM 171 HG3 LYS A 10 -3.150 -2.391 -3.232 1.00 0.00 H ATOM 172 HD2 LYS A 10 -1.779 -0.301 -4.930 1.00 0.00 H ATOM 173 HD3 LYS A 10 -1.011 -1.855 -4.845 1.00 0.00 H ATOM 174 HE2 LYS A 10 -3.943 -1.418 -5.716 1.00 0.00 H ATOM 175 HE3 LYS A 10 -2.567 -1.702 -6.790 1.00 0.00 H ATOM 176 HZ1 LYS A 10 -2.284 -3.772 -5.178 1.00 0.00 H ATOM 177 HZ3 LYS A 10 -3.858 -3.583 -4.936 1.00 0.00 H ATOM 178 N GLU A 11 -4.957 -1.853 0.469 1.00 0.00 N ATOM 179 CA GLU A 11 -5.068 -3.036 1.402 1.00 0.00 C ATOM 180 C GLU A 11 -5.662 -2.666 2.816 1.00 0.00 C ATOM 181 O GLU A 11 -6.198 -3.549 3.486 1.00 0.00 O ATOM 182 CB GLU A 11 -3.734 -3.852 1.617 1.00 0.00 C ATOM 183 CG GLU A 11 -3.449 -5.142 0.793 1.00 0.00 C ATOM 184 CD GLU A 11 -4.622 -6.051 0.457 1.00 0.00 C ATOM 185 OE1 GLU A 11 -5.003 -6.978 1.162 1.00 0.00 O ATOM 186 OE2 GLU A 11 -5.203 -5.717 -0.727 1.00 0.00 O ATOM 187 H GLU A 11 -5.186 -0.904 0.775 1.00 0.00 H ATOM 188 HA GLU A 11 -5.823 -3.714 0.966 1.00 0.00 H ATOM 189 HB2 GLU A 11 -2.896 -3.169 1.411 1.00 0.00 H ATOM 190 HB3 GLU A 11 -3.583 -4.106 2.685 1.00 0.00 H ATOM 191 HG2 GLU A 11 -2.956 -4.881 -0.160 1.00 0.00 H ATOM 192 HG3 GLU A 11 -2.689 -5.749 1.318 1.00 0.00 H ATOM 193 HE2 GLU A 11 -5.940 -6.306 -0.879 1.00 0.00 H ATOM 194 N TYR A 12 -5.526 -1.413 3.298 1.00 0.00 N ATOM 195 CA TYR A 12 -5.798 -1.029 4.718 1.00 0.00 C ATOM 196 C TYR A 12 -6.867 0.114 4.839 1.00 0.00 C ATOM 197 O TYR A 12 -7.884 -0.061 5.511 1.00 0.00 O ATOM 198 CB TYR A 12 -4.414 -0.675 5.353 1.00 0.00 C ATOM 199 CG TYR A 12 -4.312 -0.789 6.878 1.00 0.00 C ATOM 200 CD1 TYR A 12 -4.840 0.210 7.709 1.00 0.00 C ATOM 201 CD2 TYR A 12 -3.654 -1.877 7.460 1.00 0.00 C ATOM 202 CE1 TYR A 12 -4.739 0.098 9.091 1.00 0.00 C ATOM 203 CE2 TYR A 12 -3.539 -1.980 8.841 1.00 0.00 C ATOM 204 CZ TYR A 12 -4.094 -0.995 9.660 1.00 0.00 C ATOM 205 OH TYR A 12 -4.031 -1.134 11.017 1.00 0.00 O ATOM 206 H TYR A 12 -5.038 -0.793 2.646 1.00 0.00 H ATOM 207 HA TYR A 12 -6.217 -1.893 5.274 1.00 0.00 H ATOM 208 HB2 TYR A 12 -3.631 -1.330 4.928 1.00 0.00 H ATOM 209 HB3 TYR A 12 -4.095 0.336 5.037 1.00 0.00 H ATOM 210 HD1 TYR A 12 -5.339 1.062 7.277 1.00 0.00 H ATOM 211 HD2 TYR A 12 -3.226 -2.654 6.836 1.00 0.00 H ATOM 212 HE1 TYR A 12 -5.166 0.869 9.721 1.00 0.00 H ATOM 213 HE2 TYR A 12 -3.036 -2.824 9.287 1.00 0.00 H ATOM 214 HH TYR A 12 -4.761 -0.645 11.403 1.00 0.00 H ATOM 215 N ASN A 13 -6.625 1.278 4.204 1.00 0.00 N ATOM 216 CA ASN A 13 -7.546 2.459 4.244 1.00 0.00 C ATOM 217 C ASN A 13 -8.070 2.939 2.842 1.00 0.00 C ATOM 218 O ASN A 13 -9.180 3.470 2.781 1.00 0.00 O ATOM 219 CB ASN A 13 -6.846 3.617 5.017 1.00 0.00 C ATOM 220 CG ASN A 13 -6.808 3.498 6.547 1.00 0.00 C ATOM 221 OD1 ASN A 13 -7.314 2.582 7.178 1.00 0.00 O ATOM 222 ND2 ASN A 13 -6.210 4.443 7.221 1.00 0.00 N ATOM 223 H ASN A 13 -5.785 1.237 3.623 1.00 0.00 H ATOM 224 HA ASN A 13 -8.474 2.202 4.798 1.00 0.00 H ATOM 225 HB2 ASN A 13 -5.816 3.758 4.639 1.00 0.00 H ATOM 226 HB3 ASN A 13 -7.367 4.567 4.794 1.00 0.00 H ATOM 227 HD21 ASN A 13 -5.864 5.252 6.702 1.00 0.00 H ATOM 228 HD22 ASN A 13 -6.255 4.298 8.233 1.00 0.00 H ATOM 229 N LEU A 14 -7.311 2.797 1.733 1.00 0.00 N ATOM 230 CA LEU A 14 -7.754 3.248 0.369 1.00 0.00 C ATOM 231 C LEU A 14 -8.388 2.149 -0.564 1.00 0.00 C ATOM 232 O LEU A 14 -8.400 2.302 -1.786 1.00 0.00 O ATOM 233 CB LEU A 14 -6.515 3.962 -0.275 1.00 0.00 C ATOM 234 CG LEU A 14 -6.735 5.160 -1.246 1.00 0.00 C ATOM 235 CD1 LEU A 14 -7.042 4.750 -2.698 1.00 0.00 C ATOM 236 CD2 LEU A 14 -7.785 6.174 -0.751 1.00 0.00 C ATOM 237 H LEU A 14 -6.425 2.310 1.886 1.00 0.00 H ATOM 238 HA LEU A 14 -8.558 3.999 0.486 1.00 0.00 H ATOM 239 HB2 LEU A 14 -5.843 4.355 0.513 1.00 0.00 H ATOM 240 HB3 LEU A 14 -5.886 3.199 -0.776 1.00 0.00 H ATOM 241 HG LEU A 14 -5.763 5.692 -1.282 1.00 0.00 H ATOM 242 HD11 LEU A 14 -6.532 3.812 -2.988 1.00 0.00 H ATOM 243 HD12 LEU A 14 -8.122 4.576 -2.870 1.00 0.00 H ATOM 244 HD13 LEU A 14 -6.724 5.523 -3.421 1.00 0.00 H ATOM 245 HD21 LEU A 14 -7.758 6.302 0.347 1.00 0.00 H ATOM 246 HD22 LEU A 14 -7.642 7.174 -1.198 1.00 0.00 H ATOM 247 HD23 LEU A 14 -8.816 5.855 -1.002 1.00 0.00 H ATOM 248 N VAL A 15 -8.944 1.043 -0.036 1.00 0.00 N ATOM 249 CA VAL A 15 -9.557 -0.042 -0.868 1.00 0.00 C ATOM 250 C VAL A 15 -10.748 0.431 -1.791 1.00 0.00 C ATOM 251 O VAL A 15 -11.554 1.298 -1.462 1.00 0.00 O ATOM 252 CB VAL A 15 -9.903 -1.251 0.073 1.00 0.00 C ATOM 253 CG1 VAL A 15 -11.231 -1.093 0.852 1.00 0.00 C ATOM 254 CG2 VAL A 15 -9.931 -2.601 -0.675 1.00 0.00 C ATOM 255 H VAL A 15 -8.958 1.037 0.989 1.00 0.00 H ATOM 256 HA VAL A 15 -8.749 -0.384 -1.546 1.00 0.00 H ATOM 257 HB VAL A 15 -9.094 -1.348 0.827 1.00 0.00 H ATOM 258 HG11 VAL A 15 -11.336 -0.078 1.280 1.00 0.00 H ATOM 259 HG12 VAL A 15 -12.113 -1.244 0.199 1.00 0.00 H ATOM 260 HG13 VAL A 15 -11.314 -1.809 1.689 1.00 0.00 H ATOM 261 HG21 VAL A 15 -10.158 -3.443 0.007 1.00 0.00 H ATOM 262 HG22 VAL A 15 -10.696 -2.622 -1.474 1.00 0.00 H ATOM 263 HG23 VAL A 15 -8.956 -2.832 -1.145 1.00 0.00 H HETATM 264 N NH2 A 16 -10.913 -0.105 -2.981 1.00 0.00 N HETATM 265 HN1 NH2 A 16 -10.262 -0.838 -3.267 1.00 0.00 H HETATM 266 HN2 NH2 A 16 -11.680 0.323 -3.506 1.00 0.00 H TER 267 NH2 A 16 CONECT 264 265 266 CONECT 265 264 CONECT 266 264 MASTER 143 0 1 0 0 0 0 6 127 1 3 2 END