PDB Full entry for 1M24 HEADER ANTIBIOTIC 21-JUN-02 1M24 TITLE TRICHOTOXIN_A50E, AN ION CHANNEL-FORMING POLYPEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRICHOTOXIN_A50E; COMPND 3 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRICHODERMA VIRIDE; SOURCE 3 ORGANISM_COMMON: FUNGI; SOURCE 4 STRAIN: NRRL 5242 KEYWDS HELICAL BUNDLE, ION CHANNEL, PEPTAIBOL, ANTIBIOTIC EXPDTA X-RAY DIFFRACTION AUTHOR J.K.CHUGH,H.BRUECKNER,B.A.WALLACE JRNL AUTH J.K.CHUGH,H.BRUECKNER,B.A.WALLACE JRNL TITL MODEL FOR A HELICAL BUNDLE CHANNEL BASED ON THE JRNL TITL 2 HIGH RESOLUTION CRYSTAL STRUCTURE OF JRNL TITL 3 TRICHOTOXIN_A50E JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 0.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-97 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.076 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.075 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.092 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 688 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 13427 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.057 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.056 REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.072 REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 508 REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 10153 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 510 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 17 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 249.00 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 278.00 REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 2244 REMARK 3 NUMBER OF RESTRAINTS : 2814 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.026 REMARK 3 ANGLE DISTANCES (A) : 0.026 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.026 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.101 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 1.186 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.000 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.006 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.030 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.091 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER REMARK 3 SPECIAL CASE: NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST REMARK 3 SQUARES PROCEDURE, NO RESTRAINTS USED REMARK 4 REMARK 4 1M24 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-2002. REMARK 100 THE RCSB ID CODE IS RCSB016502. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-APR-2001 REMARK 200 TEMPERATURE (KELVIN) : 150.0 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : 9.8 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6883 REMARK 200 MONOCHROMATOR : SILICON 111 REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BRUKER SMART VERSION 5.054 REMARK 200 DATA SCALING SOFTWARE : BRUKER SAINT VERSION 6.02A REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13427 REMARK 200 RESOLUTION RANGE HIGH (A) : 0.900 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 2.790 REMARK 200 R MERGE (I) : 0.05140 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.0300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.18 REMARK 200 R MERGE FOR SHELL (I) : 0.26140 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.360 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP, ARP/WARP REMARK 200 STARTING MODEL: MODEL OF HELICAL PEPTIDE, RESIDUES 1-13. REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 8.3 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: METHANOL:ACETONITRILE 1:10 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, B 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 999 REMARK 999 SEQUENCE REMARK 999 THE SEQUENCE FOR CHAIN A AND B ARE FROM REMARK 999 THE PEPTAIBOL DATABASE, TRICHOTOXIN_A-50_E SEQRES 1 A 19 ACE AIB GLY AIB LEU AIB GLN AIB AIB AIB ALA ALA AIB SEQRES 2 A 19 PRO LEU AIB AIB GLN VOL SEQRES 1 B 19 ACE AIB GLY AIB LEU AIB GLN AIB AIB AIB ALA ALA AIB SEQRES 2 B 19 PRO LEU AIB AIB GLN VOL MODRES 1M24 AIB A 1 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 3 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 5 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 7 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 8 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 9 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 12 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 15 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB A 16 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 VOL A 18 L-VALINOL MODRES 1M24 AIB B 1 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 3 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 5 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 7 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 8 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 9 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 12 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 15 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 AIB B 16 ALA ALPHA-AMINOISOBUTYRIC ACID MODRES 1M24 VOL B 18 L-VALINOL HET ACE A 0 6 HET AIB A 1 13 HET AIB A 3 13 HET AIB A 5 13 HET AIB A 7 13 HET AIB A 8 13 HET AIB A 9 13 HET AIB A 12 13 HET AIB A 15 13 HET AIB A 16 13 HET VOL A 18 19 HET ACE B 0 6 HET AIB B 1 13 HET AIB B 3 13 HET AIB B 5 13 HET AIB B 7 13 HET AIB B 8 13 HET AIB B 9 13 HET AIB B 12 13 HET AIB B 15 13 HET AIB B 16 13 HET VOL B 18 19 HET CCN 11 6 HET CCN 12 6 HETNAM ACE ACETYL GROUP HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID HETNAM VOL L-VALINOL HETNAM CCN ACETONITRILE FORMUL 1 ACE 2(C2 H3 O1) FORMUL 1 AIB 18(C4 H9 N1 O2) FORMUL 1 VOL 2(C5 H13 N1 O1) FORMUL 3 CCN 2(C2 H3 N1) FORMUL 5 HOH *5(H2 O1) CRYST1 9.490 16.850 31.680 95.77 98.07 99.45 P 1 2 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 0.105374 0.017539 0.017299 0.00000 SCALE2 0.000000 0.060164 0.007675 0.00000 SCALE3 0.000000 0.000000 0.032140 0.00000 HETATM 1 C ACE A 0 3.466 5.475 29.446 1.00 4.46 C HETATM 2 O ACE A 0 3.268 5.775 28.243 1.00 4.96 O HETATM 3 CH3 ACE A 0 2.332 5.601 30.465 1.00 6.06 C HETATM 4 1H ACE A 0 2.650 5.338 31.332 1.00 9.09 H HETATM 5 2H ACE A 0 1.604 5.031 30.206 1.00 9.09 H HETATM 6 3H ACE A 0 2.029 6.511 30.498 1.00 9.09 H HETATM 7 N AIB A 1 4.656 5.074 29.882 1.00 4.47 N HETATM 8 CA AIB A 1 5.822 5.023 29.012 1.00 4.39 C HETATM 9 C AIB A 1 5.510 4.135 27.812 1.00 3.57 C HETATM 10 O1 AIB A 1 5.843 4.454 26.664 1.00 4.42 O HETATM 11 CB1 AIB A 1 6.960 4.359 29.800 1.00 5.74 C HETATM 12 CB2 AIB A 1 6.267 6.403 28.580 1.00 6.42 C HETATM 13 1HN AIB A 1 4.739 4.836 30.704 1.00 5.36 H HETATM 14 1HB1 AIB A 1 7.171 4.894 30.569 1.00 8.61 H HETATM 15 2HB1 AIB A 1 7.736 4.284 29.239 1.00 8.61 H HETATM 16 3HB1 AIB A 1 6.685 3.485 30.084 1.00 8.61 H HETATM 17 1HB2 AIB A 1 5.559 6.829 28.090 1.00 9.63 H HETATM 18 2HB2 AIB A 1 7.043 6.328 28.020 1.00 9.63 H HETATM 19 3HB2 AIB A 1 6.480 6.928 29.355 1.00 9.63 H ATOM 20 N GLY A 2 4.933 2.965 28.039 1.00 3.74 N ATOM 21 CA GLY A 2 4.701 2.016 26.976 1.00 3.54 C ATOM 22 C GLY A 2 3.609 2.486 26.018 1.00 3.25 C ATOM 23 O GLY A 2 3.752 2.319 24.788 1.00 3.60 O ATOM 24 H GLY A 2 4.690 2.765 28.840 1.00 4.49 H ATOM 25 1HA GLY A 2 5.524 1.884 26.481 1.00 4.24 H ATOM 26 2HA GLY A 2 4.443 1.163 27.360 1.00 4.24 H HETATM 27 N AIB A 3 2.551 3.073 26.536 1.00 3.38 N HETATM 28 CA AIB A 3 1.477 3.658 25.710 1.00 3.54 C HETATM 29 C AIB A 3 2.094 4.632 24.736 1.00 3.18 C HETATM 30 O1 AIB A 3 1.789 4.663 23.531 1.00 3.74 O HETATM 31 CB1 AIB A 3 0.517 4.407 26.620 1.00 4.18 C HETATM 32 CB2 AIB A 3 0.719 2.542 24.984 1.00 4.10 C HETATM 33 1HN AIB A 3 2.483 3.118 27.392 1.00 4.05 H HETATM 34 1HB1 AIB A 3 0.120 3.793 27.241 1.00 6.27 H HETATM 35 2HB1 AIB A 3 -0.171 4.817 26.091 1.00 6.27 H HETATM 36 3HB1 AIB A 3 0.996 5.085 27.102 1.00 6.27 H HETATM 37 1HB2 AIB A 3 0.336 1.943 25.629 1.00 6.15 H HETATM 38 2HB2 AIB A 3 1.325 2.059 24.418 1.00 6.15 H HETATM 39 3HB2 AIB A 3 0.019 2.926 24.449 1.00 6.15 H ATOM 40 N LEU A 4 2.983 5.513 25.250 1.00 3.24 N ATOM 41 CA LEU A 4 3.605 6.536 24.416 1.00 3.51 C ATOM 42 C LEU A 4 4.519 5.899 23.391 1.00 2.96 C ATOM 43 O LEU A 4 4.486 6.261 22.196 1.00 3.51 O ATOM 44 CB LEU A 4 4.312 7.535 25.319 1.00 3.82 C ATOM 45 CG LEU A 4 4.594 8.899 24.682 1.00 4.76 C ATOM 46 CD1 LEU A 4 4.924 9.913 25.777 1.00 6.10 C ATOM 47 CD2 LEU A 4 5.706 8.891 23.662 1.00 6.25 C ATOM 48 H LEU A 4 3.186 5.469 26.084 1.00 3.89 H ATOM 49 HA LEU A 4 2.894 7.010 23.937 1.00 4.21 H ATOM 50 1HB LEU A 4 3.770 7.671 26.111 1.00 4.58 H ATOM 51 2HB LEU A 4 5.155 7.148 25.605 1.00 4.58 H ATOM 52 HG LEU A 4 3.776 9.196 24.233 1.00 5.71 H ATOM 53 1HD1 LEU A 4 4.217 9.923 26.427 1.00 9.15 H ATOM 54 2HD1 LEU A 4 5.013 10.786 25.388 1.00 9.15 H ATOM 55 3HD1 LEU A 4 5.748 9.666 26.203 1.00 9.15 H ATOM 56 1HD2 LEU A 4 5.499 8.261 22.968 1.00 9.38 H ATOM 57 2HD2 LEU A 4 6.529 8.640 24.088 1.00 9.38 H ATOM 58 3HD2 LEU A 4 5.797 9.768 23.281 1.00 9.38 H HETATM 59 N AIB A 5 5.349 4.937 23.815 1.00 3.06 N HETATM 60 CA AIB A 5 6.243 4.214 22.904 1.00 3.45 C HETATM 61 C AIB A 5 5.425 3.730 21.700 1.00 3.14 C HETATM 62 O1 AIB A 5 5.860 3.802 20.542 1.00 3.81 O HETATM 63 CB1 AIB A 5 6.770 2.977 23.637 1.00 3.93 C HETATM 64 CB2 AIB A 5 7.393 5.119 22.470 1.00 4.83 C HETATM 65 1HN AIB A 5 5.357 4.736 24.651 1.00 3.67 H HETATM 66 1HB1 AIB A 5 7.286 3.251 24.398 1.00 5.90 H HETATM 67 2HB1 AIB A 5 7.324 2.464 23.043 1.00 5.90 H HETATM 68 3HB1 AIB A 5 6.031 2.438 23.929 1.00 5.90 H HETATM 69 1HB2 AIB A 5 7.884 5.405 23.244 1.00 7.25 H HETATM 70 2HB2 AIB A 5 7.041 5.886 22.012 1.00 7.25 H HETATM 71 3HB2 AIB A 5 7.977 4.634 21.882 1.00 7.25 H ATOM 72 N GLN A 6 4.273 3.142 21.981 1.00 2.97 N ATOM 73 CA GLN A 6 3.444 2.504 20.950 1.00 3.11 C ATOM 74 C GLN A 6 2.785 3.522 20.029 1.00 2.69 C ATOM 75 O GLN A 6 2.741 3.298 18.811 1.00 2.79 O ATOM 76 CB GLN A 6 2.465 1.586 21.610 1.00 3.88 C ATOM 77 CG GLN A 6 1.710 0.733 20.597 1.00 5.41 C ATOM 78 CD GLN A 6 1.097 -0.491 21.213 1.00 6.93 C ATOM 79 OE1 GLN A 6 1.657 -1.201 22.018 1.00 8.65 O ATOM 80 NE2 GLN A 6 -0.082 -0.791 20.710 1.00 19.71 N ATOM 81 H GLN A 6 4.000 3.134 22.796 1.00 3.56 H ATOM 82 HA GLN A 6 4.037 1.952 20.399 1.00 3.73 H ATOM 83 1HB GLN A 6 2.938 1.005 22.227 1.00 4.66 H ATOM 84 2HB GLN A 6 1.830 2.111 22.122 1.00 4.66 H ATOM 85 1HG GLN A 6 1.010 1.268 20.192 1.00 6.49 H ATOM 86 2HG GLN A 6 2.321 0.462 19.894 1.00 6.49 H ATOM 87 1HE2 GLN A 6 -0.482 -1.513 20.952 1.00 23.65 H ATOM 88 2HE2 GLN A 6 -0.453 -0.264 20.140 1.00 23.65 H HETATM 89 N AIB A 7 2.248 4.597 20.603 1.00 2.80 N HETATM 90 CA AIB A 7 1.642 5.684 19.805 1.00 3.06 C HETATM 91 C AIB A 7 2.689 6.163 18.780 1.00 2.93 C HETATM 92 O1 AIB A 7 2.408 6.283 17.590 1.00 3.53 O HETATM 93 CB1 AIB A 7 1.319 6.835 20.776 1.00 4.38 C HETATM 94 CB2 AIB A 7 0.383 5.201 19.117 1.00 3.85 C HETATM 95 1HN AIB A 7 2.253 4.661 21.460 1.00 3.35 H HETATM 96 1HB1 AIB A 7 2.128 7.137 21.194 1.00 6.57 H HETATM 97 2HB1 AIB A 7 0.708 6.524 21.448 1.00 6.57 H HETATM 98 3HB1 AIB A 7 0.919 7.560 20.290 1.00 6.57 H HETATM 99 1HB2 AIB A 7 -0.251 4.912 19.778 1.00 5.78 H HETATM 100 2HB2 AIB A 7 0.597 4.467 18.536 1.00 5.78 H HETATM 101 3HB2 AIB A 7 0.004 5.917 18.602 1.00 5.78 H HETATM 102 N AIB A 8 3.889 6.488 19.271 1.00 3.00 N HETATM 103 CA AIB A 8 4.990 6.981 18.418 1.00 3.19 C HETATM 104 C AIB A 8 5.268 5.930 17.327 1.00 2.64 C HETATM 105 O1 AIB A 8 5.406 6.244 16.147 1.00 3.17 O HETATM 106 CB1 AIB A 8 6.237 7.099 19.292 1.00 4.47 C HETATM 107 CB2 AIB A 8 4.653 8.319 17.785 1.00 4.67 C HETATM 108 1HN AIB A 8 4.025 6.408 20.116 1.00 3.60 H HETATM 109 1HB1 AIB A 8 6.084 7.749 19.982 1.00 6.71 H HETATM 110 2HB1 AIB A 8 6.982 7.375 18.752 1.00 6.71 H HETATM 111 3HB1 AIB A 8 6.430 6.248 19.692 1.00 6.71 H HETATM 112 1HB2 AIB A 8 4.475 8.963 18.474 1.00 7.00 H HETATM 113 2HB2 AIB A 8 3.877 8.222 17.228 1.00 7.00 H HETATM 114 3HB2 AIB A 8 5.394 8.617 17.252 1.00 7.00 H HETATM 115 N AIB A 9 5.413 4.676 17.745 1.00 2.59 N HETATM 116 CA AIB A 9 5.781 3.592 16.841 1.00 2.61 C HETATM 117 C AIB A 9 4.821 3.595 15.642 1.00 2.31 C HETATM 118 O1 AIB A 9 5.232 3.442 14.479 1.00 2.62 O HETATM 119 CB1 AIB A 9 5.614 2.270 17.552 1.00 3.26 C HETATM 120 CB2 AIB A 9 7.238 3.752 16.396 1.00 3.67 C HETATM 121 1HN AIB A 9 5.286 4.498 18.577 1.00 3.10 H HETATM 122 1HB1 AIB A 9 6.205 2.236 18.308 1.00 4.89 H HETATM 123 2HB1 AIB A 9 5.823 1.553 16.949 1.00 4.89 H HETATM 124 3HB1 AIB A 9 4.706 2.180 17.852 1.00 4.89 H HETATM 125 1HB2 AIB A 9 7.343 4.590 15.940 1.00 5.50 H HETATM 126 2HB2 AIB A 9 7.472 3.034 15.803 1.00 5.50 H HETATM 127 3HB2 AIB A 9 7.811 3.731 17.165 1.00 5.50 H ATOM 128 N ALA A 10 3.531 3.733 15.931 1.00 2.25 N ATOM 129 CA ALA A 10 2.505 3.600 14.917 1.00 2.40 C ATOM 130 C ALA A 10 2.646 4.596 13.773 1.00 2.26 C ATOM 131 O ALA A 10 2.183 4.311 12.663 1.00 3.35 O ATOM 132 CB ALA A 10 1.137 3.749 15.548 1.00 2.59 C ATOM 133 H ALA A 10 3.300 3.905 16.741 1.00 2.70 H ATOM 134 HA ALA A 10 2.567 2.698 14.541 1.00 2.88 H ATOM 135 1HB ALA A 10 1.047 3.120 16.268 1.00 3.89 H ATOM 136 2HB ALA A 10 0.460 3.580 14.889 1.00 3.89 H ATOM 137 3HB ALA A 10 1.037 4.641 15.888 1.00 3.89 H ATOM 138 N ALA A 11 3.212 5.766 14.062 1.00 2.35 N ATOM 139 CA ALA A 11 3.403 6.807 13.077 1.00 2.76 C ATOM 140 C ALA A 11 4.696 6.680 12.283 1.00 2.40 C ATOM 141 O ALA A 11 4.809 7.265 11.199 1.00 2.65 O ATOM 142 CB ALA A 11 3.367 8.173 13.770 1.00 4.43 C ATOM 143 H ALA A 11 3.475 5.908 14.868 1.00 2.82 H ATOM 144 HA ALA A 11 2.655 6.768 12.446 1.00 3.31 H ATOM 145 1HB ALA A 11 2.548 8.260 14.263 1.00 6.65 H ATOM 146 2HB ALA A 11 3.419 8.868 13.110 1.00 6.65 H ATOM 147 3HB ALA A 11 4.112 8.246 14.372 1.00 6.65 H HETATM 148 N AIB A 12 5.686 5.983 12.827 1.00 2.46 N HETATM 149 CA AIB A 12 7.012 5.903 12.210 1.00 2.65 C HETATM 150 C AIB A 12 6.946 5.524 10.722 1.00 2.13 C HETATM 151 O1 AIB A 12 7.783 6.007 9.957 1.00 2.72 O HETATM 152 CB1 AIB A 12 7.837 4.827 12.930 1.00 3.56 C HETATM 153 CB2 AIB A 12 7.740 7.248 12.382 1.00 3.54 C HETATM 154 1HN AIB A 12 5.545 5.565 13.566 1.00 2.95 H HETATM 155 1HB1 AIB A 12 7.897 5.042 13.864 1.00 5.33 H HETATM 156 2HB1 AIB A 12 8.719 4.794 12.553 1.00 5.33 H HETATM 157 3HB1 AIB A 12 7.411 3.974 12.825 1.00 5.33 H HETATM 158 1HB2 AIB A 12 7.776 7.476 13.314 1.00 5.31 H HETATM 159 2HB2 AIB A 12 7.267 7.932 11.903 1.00 5.31 H HETATM 160 3HB2 AIB A 12 8.633 7.175 12.036 1.00 5.31 H ATOM 161 N PRO A 13 6.028 4.641 10.284 1.00 2.16 N ATOM 162 CA PRO A 13 6.019 4.313 8.862 1.00 2.29 C ATOM 163 C PRO A 13 5.829 5.479 7.910 1.00 1.95 C ATOM 164 O PRO A 13 6.184 5.350 6.746 1.00 2.66 O ATOM 165 CB PRO A 13 4.898 3.301 8.724 1.00 3.13 C ATOM 166 CG PRO A 13 4.835 2.643 10.089 1.00 3.36 C ATOM 167 CD PRO A 13 5.056 3.819 11.034 1.00 2.88 C ATOM 168 HA PRO A 13 6.865 3.869 8.642 1.00 2.75 H ATOM 169 1HB PRO A 13 4.059 3.739 8.510 1.00 3.75 H ATOM 170 2HB PRO A 13 5.100 2.650 8.033 1.00 3.75 H ATOM 171 1HG PRO A 13 3.971 2.228 10.239 1.00 4.03 H ATOM 172 2HG PRO A 13 5.531 1.975 10.190 1.00 4.03 H ATOM 173 1HD PRO A 13 4.231 4.304 11.193 1.00 3.46 H ATOM 174 2HD PRO A 13 5.423 3.526 11.883 1.00 3.46 H ATOM 175 N LEU A 14 5.234 6.586 8.374 1.00 2.15 N ATOM 176 CA LEU A 14 5.143 7.750 7.481 1.00 2.06 C ATOM 177 C LEU A 14 6.538 8.278 7.162 1.00 2.15 C ATOM 178 O LEU A 14 6.909 8.458 6.001 1.00 2.82 O ATOM 179 CB LEU A 14 4.260 8.820 8.099 1.00 2.47 C ATOM 180 CG LEU A 14 4.275 10.145 7.357 1.00 2.69 C ATOM 181 CD1 LEU A 14 3.887 9.997 5.908 1.00 3.46 C ATOM 182 CD2 LEU A 14 3.352 11.125 8.070 1.00 4.01 C ATOM 183 H LEU A 14 4.915 6.614 9.172 1.00 2.58 H ATOM 184 HA LEU A 14 4.729 7.459 6.642 1.00 2.48 H ATOM 185 1HB LEU A 14 3.348 8.491 8.129 1.00 2.97 H ATOM 186 2HB LEU A 14 4.548 8.972 9.012 1.00 2.97 H ATOM 187 HG LEU A 14 5.186 10.504 7.392 1.00 3.23 H ATOM 188 1HD1 LEU A 14 3.911 10.857 5.481 1.00 5.19 H ATOM 189 2HD1 LEU A 14 2.999 9.636 5.850 1.00 5.19 H ATOM 190 3HD1 LEU A 14 4.502 9.405 5.471 1.00 5.19 H ATOM 191 1HD2 LEU A 14 3.357 11.965 7.605 1.00 6.01 H ATOM 192 2HD2 LEU A 14 3.658 11.256 8.970 1.00 6.01 H ATOM 193 3HD2 LEU A 14 2.459 10.772 8.083 1.00 6.01 H HETATM 194 N AIB A 15 7.312 8.570 8.218 1.00 2.41 N HETATM 195 CA AIB A 15 8.675 9.099 8.040 1.00 2.50 C HETATM 196 C AIB A 15 9.473 8.161 7.153 1.00 2.21 C HETATM 197 O1 AIB A 15 10.257 8.581 6.291 1.00 2.97 O HETATM 198 CB1 AIB A 15 9.341 9.108 9.441 1.00 3.61 C HETATM 199 CB2 AIB A 15 8.625 10.514 7.472 1.00 3.74 C HETATM 200 1HN AIB A 15 7.008 8.446 9.012 1.00 2.89 H HETATM 201 1HB1 AIB A 15 8.848 9.689 10.026 1.00 5.41 H HETATM 202 2HB1 AIB A 15 10.244 9.423 9.364 1.00 5.41 H HETATM 203 3HB1 AIB A 15 9.341 8.218 9.801 1.00 5.41 H HETATM 204 1HB2 AIB A 15 8.116 11.077 8.060 1.00 5.61 H HETATM 205 2HB2 AIB A 15 8.210 10.497 6.606 1.00 5.61 H HETATM 206 3HB2 AIB A 15 9.517 10.859 7.392 1.00 5.61 H HETATM 207 N AIB A 16 9.307 6.856 7.376 1.00 1.94 N HETATM 208 CA AIB A 16 10.083 5.799 6.708 1.00 2.35 C HETATM 209 C AIB A 16 9.939 5.907 5.183 1.00 2.33 C HETATM 210 O1 AIB A 16 10.836 5.553 4.440 1.00 3.18 O HETATM 211 CB1 AIB A 16 9.492 4.457 7.106 1.00 2.87 C HETATM 212 CB2 AIB A 16 11.551 5.890 7.113 1.00 3.11 C HETATM 213 1HN AIB A 16 8.708 6.618 7.946 1.00 2.33 H HETATM 214 1HB1 AIB A 16 8.568 4.425 6.848 1.00 4.31 H HETATM 215 2HB1 AIB A 16 9.563 4.346 8.057 1.00 4.31 H HETATM 216 3HB1 AIB A 16 9.972 3.753 6.665 1.00 4.31 H HETATM 217 1HB2 AIB A 16 11.903 6.745 6.853 1.00 4.67 H HETATM 218 2HB2 AIB A 16 12.047 5.194 6.677 1.00 4.67 H HETATM 219 3HB2 AIB A 16 11.628 5.789 8.065 1.00 4.67 H ATOM 220 N GLN A 17 8.775 6.360 4.719 1.00 2.58 N ATOM 221 CA GLN A 17 8.456 6.403 3.298 1.00 3.03 C ATOM 222 C GLN A 17 9.072 7.597 2.576 1.00 3.73 C ATOM 223 O GLN A 17 8.858 7.704 1.353 1.00 5.50 O ATOM 224 CB GLN A 17 6.937 6.336 3.119 1.00 3.15 C ATOM 225 CG GLN A 17 6.400 4.963 3.448 1.00 3.23 C ATOM 226 CD GLN A 17 4.911 4.959 3.385 1.00 3.97 C ATOM 227 OE1 GLN A 17 4.223 5.059 4.501 1.00 5.41 O ATOM 228 NE2 GLN A 17 4.325 4.898 2.266 1.00 5.05 N ATOM 229 H GLN A 17 8.187 6.638 5.281 1.00 3.10 H ATOM 230 HA GLN A 17 8.831 5.594 2.892 1.00 3.64 H ATOM 231 1HB GLN A 17 6.516 6.992 3.697 1.00 3.78 H ATOM 232 2HB GLN A 17 6.711 6.558 2.202 1.00 3.78 H ATOM 233 1HG GLN A 17 6.754 4.316 2.817 1.00 3.87 H ATOM 234 2HG GLN A 17 6.689 4.705 4.337 1.00 3.87 H ATOM 235 1HE2 GLN A 17 3.466 4.921 2.228 1.00 6.06 H ATOM 236 2HE2 GLN A 17 4.786 4.833 1.542 1.00 6.06 H HETATM 237 N VOL A 18 9.817 8.445 3.235 1.00 4.24 N HETATM 238 CA VOL A 18 10.698 9.460 2.757 1.00 5.22 C HETATM 239 CB VOL A 18 10.418 10.769 3.317 1.00 7.10 C HETATM 240 CG1 VOL A 18 11.211 11.932 2.739 1.00 13.45 C HETATM 241 CG2 VOL A 18 8.947 11.146 3.384 1.00 9.44 C HETATM 242 CH2 VOL A 18 12.073 9.008 2.495 1.00 7.68 C HETATM 243 OH VOL A 18 12.288 7.848 1.824 1.00 11.35 O HETATM 244 1HN VOL A 18 9.767 8.382 4.091 1.00 5.09 H HETATM 245 HA VOL A 18 10.366 9.576 1.842 1.00 6.27 H HETATM 246 HB VOL A 18 10.705 10.708 4.253 1.00 8.51 H HETATM 247 HG1 VOL A 18 11.026 12.727 3.243 1.00 20.18 H HETATM 248 HG2 VOL A 18 10.958 12.067 1.823 1.00 20.18 H HETATM 249 HG3 VOL A 18 12.149 11.734 2.786 1.00 20.18 H HETATM 250 HH1 VOL A 18 12.521 9.714 2.003 1.00 9.22 H HETATM 251 HH2 VOL A 18 12.521 8.934 3.352 1.00 9.22 H HETATM 252 HH VOL A 18 11.847 7.248 2.168 1.00 17.02 H HETATM 253 H21 VOL A 18 8.852 11.982 3.847 1.00 14.16 H HETATM 254 H22 VOL A 18 8.462 10.464 3.854 1.00 14.16 H HETATM 255 H23 VOL A 18 8.597 11.232 2.494 1.00 14.16 H TER 256 VOL A 18 HETATM 257 C ACE B 0 -2.121 -0.306 -9.164 1.00 6.88 C HETATM 258 O ACE B 0 -2.236 -0.570 -7.947 1.00 7.69 O HETATM 259 CH3 ACE B 0 -3.377 -0.348 -10.058 1.00 8.81 C HETATM 260 1H ACE B 0 -3.137 -0.116 -10.958 1.00 13.22 H HETATM 261 2H ACE B 0 -4.026 0.279 -9.729 1.00 13.22 H HETATM 262 3H ACE B 0 -3.751 -1.232 -10.045 1.00 13.22 H HETATM 263 N AIB B 1 -1.019 -0.007 -9.716 1.00 6.40 N HETATM 264 CA AIB B 1 0.239 -0.001 -8.996 1.00 5.87 C HETATM 265 C AIB B 1 0.076 0.904 -7.759 1.00 4.95 C HETATM 266 O1 AIB B 1 0.403 0.503 -6.628 1.00 6.60 O HETATM 267 CB1 AIB B 1 1.305 0.614 -9.931 1.00 9.17 C HETATM 268 CB2 AIB B 1 0.670 -1.404 -8.604 1.00 7.52 C HETATM 269 1HN AIB B 1 -1.018 0.200 -10.550 1.00 7.68 H HETATM 270 1HB1 AIB B 1 1.401 0.065 -10.713 1.00 13.75 H HETATM 271 2HB1 AIB B 1 2.146 0.663 -9.470 1.00 13.75 H HETATM 272 3HB1 AIB B 1 1.032 1.497 -10.192 1.00 13.75 H HETATM 273 1HB2 AIB B 1 0.752 -1.946 -9.392 1.00 11.27 H HETATM 274 2HB2 AIB B 1 0.015 -1.788 -8.017 1.00 11.27 H HETATM 275 3HB2 AIB B 1 1.518 -1.364 -8.154 1.00 11.27 H ATOM 276 N GLY B 2 -0.379 2.131 -7.952 1.00 4.39 N ATOM 277 CA GLY B 2 -0.515 3.063 -6.852 1.00 4.35 C ATOM 278 C GLY B 2 -1.602 2.663 -5.853 1.00 3.76 C ATOM 279 O GLY B 2 -1.395 2.795 -4.641 1.00 4.09 O ATOM 280 H GLY B 2 -0.598 2.380 -8.745 1.00 5.26 H ATOM 281 1HA GLY B 2 0.333 3.126 -6.385 1.00 5.22 H ATOM 282 2HA GLY B 2 -0.722 3.942 -7.207 1.00 5.22 H HETATM 283 N AIB B 3 -2.717 2.165 -6.349 1.00 3.90 N HETATM 284 CA AIB B 3 -3.815 1.705 -5.508 1.00 3.71 C HETATM 285 C AIB B 3 -3.263 0.667 -4.518 1.00 3.47 C HETATM 286 O1 AIB B 3 -3.566 0.685 -3.324 1.00 3.93 O HETATM 287 CB1 AIB B 3 -4.844 0.998 -6.386 1.00 4.70 C HETATM 288 CB2 AIB B 3 -4.447 2.869 -4.759 1.00 4.76 C HETATM 289 1HN AIB B 3 -2.800 2.109 -7.203 1.00 4.68 H HETATM 290 1HB1 AIB B 3 -4.424 0.269 -6.848 1.00 7.05 H HETATM 291 2HB1 AIB B 3 -5.199 1.620 -7.026 1.00 7.05 H HETATM 292 3HB1 AIB B 3 -5.556 0.662 -5.837 1.00 7.05 H HETATM 293 1HB2 AIB B 3 -4.793 3.504 -5.389 1.00 7.14 H HETATM 294 2HB2 AIB B 3 -3.784 3.293 -4.209 1.00 7.14 H HETATM 295 3HB2 AIB B 3 -5.161 2.544 -4.206 1.00 7.14 H ATOM 296 N LEU B 4 -2.494 -0.297 -5.037 1.00 3.50 N ATOM 297 CA LEU B 4 -1.970 -1.382 -4.201 1.00 3.67 C ATOM 298 C LEU B 4 -0.890 -0.857 -3.256 1.00 3.59 C ATOM 299 O LEU B 4 -0.855 -1.295 -2.084 1.00 4.31 O ATOM 300 CB LEU B 4 -1.444 -2.514 -5.055 1.00 3.98 C ATOM 301 CG LEU B 4 -2.536 -3.382 -5.644 1.00 4.37 C ATOM 302 CD1 LEU B 4 -1.946 -4.287 -6.752 1.00 7.48 C ATOM 303 CD2 LEU B 4 -3.204 -4.256 -4.619 1.00 6.31 C ATOM 304 H LEU B 4 -2.305 -0.281 -5.876 1.00 4.21 H ATOM 305 HA LEU B 4 -2.707 -1.729 -3.657 1.00 4.40 H ATOM 306 1HB LEU B 4 -0.915 -2.142 -5.778 1.00 4.78 H ATOM 307 2HB LEU B 4 -0.859 -3.069 -4.515 1.00 4.78 H ATOM 308 HG LEU B 4 -3.214 -2.799 -6.046 1.00 5.24 H ATOM 309 1HD1 LEU B 4 -2.645 -4.825 -7.131 1.00 11.21 H ATOM 310 2HD1 LEU B 4 -1.272 -4.857 -6.374 1.00 11.21 H ATOM 311 3HD1 LEU B 4 -1.555 -3.740 -7.437 1.00 11.21 H ATOM 312 1HD2 LEU B 4 -3.891 -4.777 -5.042 1.00 9.47 H ATOM 313 2HD2 LEU B 4 -3.595 -3.706 -3.936 1.00 9.47 H ATOM 314 3HD2 LEU B 4 -2.554 -4.842 -4.225 1.00 9.47 H HETATM 315 N AIB B 5 -0.022 0.013 -3.695 1.00 3.77 N HETATM 316 CA AIB B 5 0.989 0.648 -2.835 1.00 3.87 C HETATM 317 C AIB B 5 0.265 1.220 -1.611 1.00 3.38 C HETATM 318 O1 AIB B 5 0.719 1.077 -0.461 1.00 4.01 O HETATM 319 CB1 AIB B 5 1.611 1.824 -3.592 1.00 5.11 C HETATM 320 CB2 AIB B 5 2.057 -0.342 -2.417 1.00 5.70 C HETATM 321 1HN AIB B 5 -0.042 0.226 -4.528 1.00 4.52 H HETATM 322 1HB1 AIB B 5 0.921 2.438 -3.851 1.00 7.66 H HETATM 323 2HB1 AIB B 5 2.061 1.498 -4.375 1.00 7.66 H HETATM 324 3HB1 AIB B 5 2.242 2.272 -3.024 1.00 7.66 H HETATM 325 1HB2 AIB B 5 2.495 -0.689 -3.198 1.00 8.54 H HETATM 326 2HB2 AIB B 5 1.652 -1.063 -1.930 1.00 8.54 H HETATM 327 3HB2 AIB B 5 2.701 0.099 -1.859 1.00 8.54 H ATOM 328 N GLN B 6 -0.829 1.924 -1.855 1.00 3.50 N ATOM 329 CA GLN B 6 -1.517 2.627 -0.777 1.00 3.19 C ATOM 330 C GLN B 6 -2.271 1.684 0.151 1.00 2.97 C ATOM 331 O GLN B 6 -2.260 1.878 1.368 1.00 3.09 O ATOM 332 CB GLN B 6 -2.394 3.720 -1.347 1.00 3.57 C ATOM 333 CG GLN B 6 -2.888 4.674 -0.288 1.00 4.67 C ATOM 334 CD GLN B 6 -3.536 5.910 -0.813 1.00 4.65 C ATOM 335 OE1 GLN B 6 -3.096 6.476 -1.821 1.00 6.45 O ATOM 336 NE2 GLN B 6 -4.546 6.384 -0.138 1.00 5.02 N ATOM 337 H GLN B 6 -1.138 1.968 -2.656 1.00 4.21 H ATOM 338 HA GLN B 6 -0.828 3.067 -0.238 1.00 3.83 H ATOM 339 1HB GLN B 6 -1.891 4.216 -2.012 1.00 4.28 H ATOM 340 2HB GLN B 6 -3.156 3.316 -1.792 1.00 4.28 H ATOM 341 1HG GLN B 6 -3.524 4.207 0.276 1.00 5.61 H ATOM 342 2HG GLN B 6 -2.137 4.932 0.270 1.00 5.61 H ATOM 343 1HE2 GLN B 6 -4.928 7.112 -0.389 1.00 6.02 H ATOM 344 2HE2 GLN B 6 -4.830 5.968 0.559 1.00 6.02 H HETATM 345 N AIB B 7 -2.897 0.654 -0.412 1.00 3.06 N HETATM 346 CA AIB B 7 -3.560 -0.395 0.378 1.00 3.09 C HETATM 347 C AIB B 7 -2.527 -0.949 1.389 1.00 3.22 C HETATM 348 O1 AIB B 7 -2.772 -1.015 2.589 1.00 3.82 O HETATM 349 CB1 AIB B 7 -3.988 -1.514 -0.585 1.00 4.13 C HETATM 350 CB2 AIB B 7 -4.765 0.153 1.094 1.00 4.13 C HETATM 351 1HN AIB B 7 -2.914 0.600 -1.270 1.00 3.68 H HETATM 352 1HB1 AIB B 7 -3.215 -1.866 -1.031 1.00 6.20 H HETATM 353 2HB1 AIB B 7 -4.599 -1.160 -1.235 1.00 6.20 H HETATM 354 3HB1 AIB B 7 -4.419 -2.215 -0.090 1.00 6.20 H HETATM 355 1HB2 AIB B 7 -5.393 0.491 0.451 1.00 6.19 H HETATM 356 2HB2 AIB B 7 -4.494 0.864 1.680 1.00 6.19 H HETATM 357 3HB2 AIB B 7 -5.178 -0.545 1.607 1.00 6.19 H HETATM 358 N AIB B 8 -1.367 -1.347 0.864 1.00 3.32 N HETATM 359 CA AIB B 8 -0.305 -1.957 1.687 1.00 3.85 C HETATM 360 C AIB B 8 0.116 -0.960 2.775 1.00 3.31 C HETATM 361 O1 AIB B 8 0.270 -1.330 3.953 1.00 3.87 O HETATM 362 CB1 AIB B 8 0.896 -2.223 0.789 1.00 4.72 C HETATM 363 CB2 AIB B 8 -0.812 -3.273 2.298 1.00 5.05 C HETATM 364 1HN AIB B 8 -1.234 -1.244 0.020 1.00 3.98 H HETATM 365 1HB1 AIB B 8 1.208 -1.394 0.417 1.00 7.07 H HETATM 366 2HB1 AIB B 8 0.640 -2.815 0.078 1.00 7.07 H HETATM 367 3HB1 AIB B 8 1.598 -2.627 1.305 1.00 7.07 H HETATM 368 1HB2 AIB B 8 -1.569 -3.094 2.860 1.00 7.58 H HETATM 369 2HB2 AIB B 8 -0.113 -3.673 2.821 1.00 7.58 H HETATM 370 3HB2 AIB B 8 -1.070 -3.874 1.595 1.00 7.58 H HETATM 371 N AIB B 9 0.331 0.276 2.400 1.00 3.02 N HETATM 372 CA AIB B 9 0.832 1.327 3.298 1.00 2.90 C HETATM 373 C AIB B 9 -0.096 1.391 4.525 1.00 2.42 C HETATM 374 O1 AIB B 9 0.373 1.569 5.656 1.00 2.67 O HETATM 375 CB1 AIB B 9 0.768 2.664 2.596 1.00 3.84 C HETATM 376 CB2 AIB B 9 2.267 1.042 3.731 1.00 4.36 C HETATM 377 1HN AIB B 9 0.170 0.486 1.582 1.00 3.62 H HETATM 378 1HB1 AIB B 9 1.341 2.649 1.825 1.00 5.77 H HETATM 379 2HB1 AIB B 9 1.058 3.355 3.196 1.00 5.77 H HETATM 380 3HB1 AIB B 9 -0.135 2.838 2.319 1.00 5.77 H HETATM 381 1HB2 AIB B 9 2.832 0.999 2.956 1.00 6.55 H HETATM 382 2HB2 AIB B 9 2.300 0.203 4.197 1.00 6.55 H HETATM 383 3HB2 AIB B 9 2.572 1.743 4.311 1.00 6.55 H ATOM 384 N ALA B 10 -1.394 1.296 4.301 1.00 2.63 N ATOM 385 CA ALA B 10 -2.358 1.441 5.373 1.00 2.72 C ATOM 386 C ALA B 10 -2.181 0.403 6.487 1.00 2.70 C ATOM 387 O ALA B 10 -2.645 0.629 7.598 1.00 3.78 O ATOM 388 CB ALA B 10 -3.763 1.360 4.806 1.00 3.40 C ATOM 389 H ALA B 10 -1.673 1.145 3.502 1.00 3.16 H ATOM 390 HA ALA B 10 -2.241 2.331 5.767 1.00 3.27 H ATOM 391 1HB ALA B 10 -3.865 2.013 4.110 1.00 5.10 H ATOM 392 2HB ALA B 10 -4.400 1.533 5.503 1.00 5.10 H ATOM 393 3HB ALA B 10 -3.912 0.483 4.445 1.00 5.10 H ATOM 394 N ALA B 11 -1.563 -0.747 6.155 1.00 2.64 N ATOM 395 CA ALA B 11 -1.283 -1.787 7.123 1.00 3.24 C ATOM 396 C ALA B 11 -0.046 -1.550 7.973 1.00 2.63 C ATOM 397 O ALA B 11 0.118 -2.195 9.004 1.00 3.25 O ATOM 398 CB ALA B 11 -1.100 -3.117 6.385 1.00 4.44 C ATOM 399 H ALA B 11 -1.326 -0.868 5.337 1.00 3.16 H ATOM 400 HA ALA B 11 -2.056 -1.869 7.720 1.00 3.88 H ATOM 401 1HB ALA B 11 -1.873 -3.292 5.844 1.00 6.66 H ATOM 402 2HB ALA B 11 -0.989 -3.825 7.023 1.00 6.66 H ATOM 403 3HB ALA B 11 -0.322 -3.068 5.824 1.00 6.66 H HETATM 404 N AIB B 12 0.840 -0.679 7.509 1.00 2.72 N HETATM 405 CA AIB B 12 2.180 -0.557 8.099 1.00 2.88 C HETATM 406 C AIB B 12 2.079 -0.285 9.629 1.00 2.28 C HETATM 407 O1 AIB B 12 2.944 -0.777 10.373 1.00 2.80 O HETATM 408 CB1 AIB B 12 2.895 0.642 7.485 1.00 4.02 C HETATM 409 CB2 AIB B 12 2.970 -1.840 7.863 1.00 4.32 C HETATM 410 1HN AIB B 12 0.626 -0.174 6.847 1.00 3.26 H HETATM 411 1HB1 AIB B 12 2.379 1.437 7.640 1.00 6.04 H HETATM 412 2HB1 AIB B 12 2.995 0.506 6.540 1.00 6.04 H HETATM 413 3HB1 AIB B 12 3.761 0.739 7.887 1.00 6.04 H HETATM 414 1HB2 AIB B 12 2.499 -2.582 8.249 1.00 6.47 H HETATM 415 2HB2 AIB B 12 3.835 -1.763 8.273 1.00 6.47 H HETATM 416 3HB2 AIB B 12 3.075 -1.983 6.920 1.00 6.47 H ATOM 417 N PRO B 13 1.130 0.507 10.123 1.00 2.31 N ATOM 418 CA PRO B 13 1.127 0.778 11.586 1.00 2.41 C ATOM 419 C PRO B 13 0.937 -0.450 12.433 1.00 2.01 C ATOM 420 O PRO B 13 1.296 -0.416 13.629 1.00 2.59 O ATOM 421 CB PRO B 13 -0.038 1.752 11.763 1.00 3.20 C ATOM 422 CG PRO B 13 -0.114 2.459 10.429 1.00 3.50 C ATOM 423 CD PRO B 13 0.112 1.328 9.442 1.00 3.11 C ATOM 424 HA PRO B 13 1.965 1.222 11.837 1.00 2.90 H ATOM 425 1HB PRO B 13 -0.862 1.279 11.955 1.00 3.84 H ATOM 426 2HB PRO B 13 0.140 2.381 12.481 1.00 3.84 H ATOM 427 1HG PRO B 13 -0.983 2.870 10.298 1.00 4.20 H ATOM 428 2HG PRO B 13 0.574 3.137 10.350 1.00 4.20 H ATOM 429 1HD PRO B 13 -0.703 0.824 9.292 1.00 3.73 H ATOM 430 2HD PRO B 13 0.441 1.662 8.593 1.00 3.73 H ATOM 431 N LEU B 14 0.368 -1.531 11.901 1.00 2.03 N ATOM 432 CA LEU B 14 0.270 -2.780 12.642 1.00 2.33 C ATOM 433 C LEU B 14 1.670 -3.312 12.977 1.00 2.38 C ATOM 434 O LEU B 14 2.008 -3.580 14.122 1.00 3.06 O ATOM 435 CB LEU B 14 -0.539 -3.798 11.847 1.00 2.77 C ATOM 436 CG LEU B 14 -0.493 -5.217 12.349 1.00 3.50 C ATOM 437 CD1 LEU B 14 -1.052 -5.373 13.758 1.00 4.94 C ATOM 438 CD2 LEU B 14 -1.247 -6.101 11.363 1.00 4.61 C ATOM 439 H LEU B 14 0.051 -1.489 11.102 1.00 2.44 H ATOM 440 HA LEU B 14 -0.201 -2.603 13.483 1.00 2.79 H ATOM 441 1HB LEU B 14 -1.465 -3.510 11.836 1.00 3.33 H ATOM 442 2HB LEU B 14 -0.222 -3.790 10.930 1.00 3.33 H ATOM 443 HG LEU B 14 0.444 -5.505 12.361 1.00 4.20 H ATOM 444 1HD1 LEU B 14 -0.997 -6.294 14.024 1.00 7.42 H ATOM 445 2HD1 LEU B 14 -1.970 -5.092 13.771 1.00 7.42 H ATOM 446 3HD1 LEU B 14 -0.543 -4.833 14.366 1.00 7.42 H ATOM 447 1HD2 LEU B 14 -0.880 -5.984 10.484 1.00 6.91 H ATOM 448 2HD2 LEU B 14 -2.175 -5.855 11.358 1.00 6.91 H ATOM 449 3HD2 LEU B 14 -1.161 -7.020 11.627 1.00 6.91 H HETATM 450 N AIB B 15 2.470 -3.500 11.922 1.00 2.90 N HETATM 451 CA AIB B 15 3.823 -4.002 12.073 1.00 2.89 C HETATM 452 C AIB B 15 4.596 -3.095 13.060 1.00 2.49 C HETATM 453 O1 AIB B 15 5.337 -3.550 13.927 1.00 3.28 O HETATM 454 CB1 AIB B 15 4.522 -3.883 10.718 1.00 4.21 C HETATM 455 CB2 AIB B 15 3.829 -5.443 12.566 1.00 4.18 C HETATM 456 1HN AIB B 15 2.176 -3.319 11.134 1.00 3.48 H HETATM 457 1HB1 AIB B 15 4.505 -2.968 10.429 1.00 6.31 H HETATM 458 2HB1 AIB B 15 4.066 -4.431 10.074 1.00 6.31 H HETATM 459 3HB1 AIB B 15 5.432 -4.177 10.800 1.00 6.31 H HETATM 460 1HB2 AIB B 15 3.386 -5.492 13.416 1.00 6.27 H HETATM 461 2HB2 AIB B 15 4.736 -5.745 12.660 1.00 6.27 H HETATM 462 3HB2 AIB B 15 3.371 -6.000 11.933 1.00 6.27 H HETATM 463 N AIB B 16 4.442 -1.799 12.871 1.00 2.28 N HETATM 464 CA AIB B 16 5.218 -0.788 13.603 1.00 2.37 C HETATM 465 C AIB B 16 5.000 -0.971 15.111 1.00 2.19 C HETATM 466 O1 AIB B 16 5.919 -0.795 15.906 1.00 2.97 O HETATM 467 CB1 AIB B 16 4.688 0.593 13.211 1.00 3.17 C HETATM 468 CB2 AIB B 16 6.691 -0.890 13.250 1.00 3.43 C HETATM 469 1HN AIB B 16 3.862 -1.534 12.295 1.00 2.73 H HETATM 470 1HB1 AIB B 16 4.812 0.727 12.269 1.00 4.75 H HETATM 471 2HB1 AIB B 16 5.167 1.269 13.696 1.00 4.75 H HETATM 472 3HB1 AIB B 16 3.753 0.649 13.422 1.00 4.75 H HETATM 473 1HB2 AIB B 16 6.803 -0.776 12.304 1.00 5.15 H HETATM 474 2HB2 AIB B 16 7.023 -1.753 13.510 1.00 5.15 H HETATM 475 3HB2 AIB B 16 7.180 -0.207 13.715 1.00 5.15 H ATOM 476 N GLN B 17 3.753 -1.238 15.502 1.00 2.23 N ATOM 477 CA GLN B 17 3.411 -1.336 16.916 1.00 2.55 C ATOM 478 C GLN B 17 3.745 -2.694 17.524 1.00 3.25 C ATOM 479 O GLN B 17 4.036 -2.739 18.728 1.00 5.24 O ATOM 480 CB GLN B 17 1.922 -1.105 17.119 1.00 2.45 C ATOM 481 CG GLN B 17 1.468 0.309 16.826 1.00 2.65 C ATOM 482 CD GLN B 17 -0.026 0.379 16.964 1.00 3.08 C ATOM 483 OE1 GLN B 17 -0.727 0.097 15.857 1.00 5.26 O ATOM 484 NE2 GLN B 17 -0.563 0.634 18.027 1.00 3.74 N ATOM 485 H GLN B 17 3.140 -1.355 14.910 1.00 2.68 H ATOM 486 HA GLN B 17 3.904 -0.645 17.405 1.00 3.06 H ATOM 487 1HB GLN B 17 1.432 -1.714 16.545 1.00 2.94 H ATOM 488 2HB GLN B 17 1.696 -1.320 18.037 1.00 2.94 H ATOM 489 1HG GLN B 17 1.886 0.926 17.447 1.00 3.18 H ATOM 490 2HG GLN B 17 1.728 0.560 15.926 1.00 3.18 H ATOM 491 1HE2 GLN B 17 -1.421 0.639 18.085 1.00 4.49 H ATOM 492 2HE2 GLN B 17 -0.084 0.811 18.719 1.00 4.49 H HETATM 493 N VOL B 18 3.607 -3.766 16.772 1.00 4.39 N HETATM 494 CA VOL B 18 3.812 -5.142 17.125 1.00 6.04 C HETATM 495 CB VOL B 18 2.642 -6.010 16.840 1.00 11.39 C HETATM 496 CG1 VOL B 18 2.862 -7.497 17.187 1.00 16.46 C HETATM 497 CG2 VOL B 18 1.264 -5.561 17.109 1.00 12.65 C HETATM 498 CH2 VOL B 18 5.125 -5.587 17.040 1.00 10.00 C HETATM 499 OH VOL B 18 5.441 -5.819 15.698 1.00 9.46 O HETATM 500 1HN VOL B 18 3.362 -3.622 15.960 1.00 5.27 H HETATM 501 HA VOL B 18 3.728 -5.073 18.099 1.00 7.25 H HETATM 502 HB VOL B 18 2.651 -6.035 15.861 1.00 13.67 H HETATM 503 HG1 VOL B 18 3.758 -7.750 16.953 1.00 24.68 H HETATM 504 HG2 VOL B 18 2.238 -8.036 16.696 1.00 24.68 H HETATM 505 HG3 VOL B 18 2.728 -7.629 18.128 1.00 24.68 H HETATM 506 HH1 VOL B 18 5.230 -6.406 17.550 1.00 12.00 H HETATM 507 HH2 VOL B 18 5.725 -4.920 17.409 1.00 12.00 H HETATM 508 HH VOL B 18 5.421 -5.111 15.286 1.00 14.19 H HETATM 509 H21 VOL B 18 1.150 -4.665 16.783 1.00 18.97 H HETATM 510 H22 VOL B 18 1.100 -5.581 18.055 1.00 18.97 H HETATM 511 H23 VOL B 18 0.644 -6.144 16.665 1.00 18.97 H TER 512 VOL B 18 HETATM 513 N CCN 11 2.307 3.949 -0.604 1.00 31.89 N HETATM 514 C1 CCN 11 1.403 4.712 -1.201 1.00 46.02 C HETATM 515 C2 CCN 11 0.357 5.444 -0.468 1.00 28.84 C HETATM 516 1H2 CCN 11 -0.364 5.656 -1.065 1.00 43.26 H HETATM 517 2H2 CCN 11 0.725 6.254 -0.109 1.00 43.26 H HETATM 518 3H2 CCN 11 0.027 4.897 0.250 1.00 43.26 H HETATM 519 N CCN 12 -1.123 -3.517 18.798 1.00 61.54 N HETATM 520 C1 CCN 12 -1.697 -2.879 17.827 1.00 66.55 C HETATM 521 C2 CCN 12 -2.053 -3.611 16.639 1.00 62.07 C HETATM 522 1H2 CCN 12 -2.369 -3.000 15.969 1.00 93.11 H HETATM 523 2H2 CCN 12 -2.745 -4.242 16.848 1.00 93.11 H HETATM 524 3H2 CCN 12 -1.282 -4.078 16.309 1.00 93.11 H HETATM 525 O HOH 1 11.425 5.816 1.769 1.00 26.98 O HETATM 526 O HOH 2 -0.290 3.415 -10.639 1.00 11.24 O HETATM 527 O HOH 3 -3.527 -0.705 9.881 1.00 12.64 O HETATM 528 O HOH 4 -2.267 1.105 20.292 1.00 31.59 O HETATM 529 O HOH 5 10.721 5.742 10.425 1.00 15.87 O CONECT 1 2 3 CONECT 2 1 CONECT 3 1 4 5 6 CONECT 4 3 CONECT 5 3 CONECT 6 3 CONECT 7 8 13 CONECT 8 7 9 11 12 CONECT 9 8 10 CONECT 10 9 CONECT 11 8 14 15 16 CONECT 12 8 17 18 19 CONECT 13 7 CONECT 14 11 CONECT 15 11 CONECT 16 11 CONECT 17 12 CONECT 18 12 CONECT 19 12 CONECT 27 28 33 CONECT 28 27 29 31 32 CONECT 29 28 30 CONECT 30 29 CONECT 31 28 34 35 36 CONECT 32 28 37 38 39 CONECT 33 27 CONECT 34 31 CONECT 35 31 CONECT 36 31 CONECT 37 32 CONECT 38 32 CONECT 39 32 CONECT 59 60 65 CONECT 60 59 61 63 64 CONECT 61 60 62 CONECT 62 61 CONECT 63 60 66 67 68 CONECT 64 60 69 70 71 CONECT 65 59 CONECT 66 63 CONECT 67 63 CONECT 68 63 CONECT 69 64 CONECT 70 64 CONECT 71 64 CONECT 89 90 95 CONECT 90 89 91 93 94 CONECT 91 90 92 CONECT 92 91 CONECT 93 90 96 97 98 CONECT 94 90 99 100 101 CONECT 95 89 CONECT 96 93 CONECT 97 93 CONECT 98 93 CONECT 99 94 CONECT 100 94 CONECT 101 94 CONECT 102 103 108 CONECT 103 102 104 106 107 CONECT 104 103 105 CONECT 105 104 CONECT 106 103 109 110 111 CONECT 107 103 112 113 114 CONECT 108 102 CONECT 109 106 CONECT 110 106 CONECT 111 106 CONECT 112 107 CONECT 113 107 CONECT 114 107 CONECT 115 116 121 CONECT 116 115 117 119 120 CONECT 117 116 118 CONECT 118 117 CONECT 119 116 122 123 124 CONECT 120 116 125 126 127 CONECT 121 115 CONECT 122 119 CONECT 123 119 CONECT 124 119 CONECT 125 120 CONECT 126 120 CONECT 127 120 CONECT 148 149 154 CONECT 149 148 150 152 153 CONECT 150 149 151 CONECT 151 150 CONECT 152 149 155 156 157 CONECT 153 149 158 159 160 CONECT 154 148 CONECT 155 152 CONECT 156 152 CONECT 157 152 CONECT 158 153 CONECT 159 153 CONECT 160 153 CONECT 194 195 200 CONECT 195 194 196 198 199 CONECT 196 195 197 CONECT 197 196 CONECT 198 195 201 202 203 CONECT 199 195 204 205 206 CONECT 200 194 CONECT 201 198 CONECT 202 198 CONECT 203 198 CONECT 204 199 CONECT 205 199 CONECT 206 199 CONECT 207 208 213 CONECT 208 207 209 211 212 CONECT 209 208 210 CONECT 210 209 CONECT 211 208 214 215 216 CONECT 212 208 217 218 219 CONECT 213 207 CONECT 214 211 CONECT 215 211 CONECT 216 211 CONECT 217 212 CONECT 218 212 CONECT 219 212 CONECT 237 238 244 CONECT 238 237 239 242 245 CONECT 239 238 240 241 246 CONECT 240 239 247 248 249 CONECT 241 239 253 254 255 CONECT 242 238 243 250 251 CONECT 243 242 252 CONECT 244 237 CONECT 245 238 CONECT 246 239 CONECT 247 240 CONECT 248 240 CONECT 249 240 CONECT 250 242 CONECT 251 242 CONECT 252 243 CONECT 253 241 CONECT 254 241 CONECT 255 241 CONECT 257 258 259 CONECT 258 257 CONECT 259 257 260 261 262 CONECT 260 259 CONECT 261 259 CONECT 262 259 CONECT 263 264 269 CONECT 264 263 265 267 268 CONECT 265 264 266 CONECT 266 265 CONECT 267 264 270 271 272 CONECT 268 264 273 274 275 CONECT 269 263 CONECT 270 267 CONECT 271 267 CONECT 272 267 CONECT 273 268 CONECT 274 268 CONECT 275 268 CONECT 283 284 289 CONECT 284 283 285 287 288 CONECT 285 284 286 CONECT 286 285 CONECT 287 284 290 291 292 CONECT 288 284 293 294 295 CONECT 289 283 CONECT 290 287 CONECT 291 287 CONECT 292 287 CONECT 293 288 CONECT 294 288 CONECT 295 288 CONECT 315 316 321 CONECT 316 315 317 319 320 CONECT 317 316 318 CONECT 318 317 CONECT 319 316 322 323 324 CONECT 320 316 325 326 327 CONECT 321 315 CONECT 322 319 CONECT 323 319 CONECT 324 319 CONECT 325 320 CONECT 326 320 CONECT 327 320 CONECT 345 346 351 CONECT 346 345 347 349 350 CONECT 347 346 348 CONECT 348 347 CONECT 349 346 352 353 354 CONECT 350 346 355 356 357 CONECT 351 345 CONECT 352 349 CONECT 353 349 CONECT 354 349 CONECT 355 350 CONECT 356 350 CONECT 357 350 CONECT 358 359 364 CONECT 359 358 360 362 363 CONECT 360 359 361 CONECT 361 360 CONECT 362 359 365 366 367 CONECT 363 359 368 369 370 CONECT 364 358 CONECT 365 362 CONECT 366 362 CONECT 367 362 CONECT 368 363 CONECT 369 363 CONECT 370 363 CONECT 371 372 377 CONECT 372 371 373 375 376 CONECT 373 372 374 CONECT 374 373 CONECT 375 372 378 379 380 CONECT 376 372 381 382 383 CONECT 377 371 CONECT 378 375 CONECT 379 375 CONECT 380 375 CONECT 381 376 CONECT 382 376 CONECT 383 376 CONECT 404 405 410 CONECT 405 404 406 408 409 CONECT 406 405 407 CONECT 407 406 CONECT 408 405 411 412 413 CONECT 409 405 414 415 416 CONECT 410 404 CONECT 411 408 CONECT 412 408 CONECT 413 408 CONECT 414 409 CONECT 415 409 CONECT 416 409 CONECT 450 451 456 CONECT 451 450 452 454 455 CONECT 452 451 453 CONECT 453 452 CONECT 454 451 457 458 459 CONECT 455 451 460 461 462 CONECT 456 450 CONECT 457 454 CONECT 458 454 CONECT 459 454 CONECT 460 455 CONECT 461 455 CONECT 462 455 CONECT 463 464 469 CONECT 464 463 465 467 468 CONECT 465 464 466 CONECT 466 465 CONECT 467 464 470 471 472 CONECT 468 464 473 474 475 CONECT 469 463 CONECT 470 467 CONECT 471 467 CONECT 472 467 CONECT 473 468 CONECT 474 468 CONECT 475 468 CONECT 493 494 500 CONECT 494 493 495 498 501 CONECT 495 494 496 497 502 CONECT 496 495 503 504 505 CONECT 497 495 509 510 511 CONECT 498 494 499 506 507 CONECT 499 498 508 CONECT 500 493 CONECT 501 494 CONECT 502 495 CONECT 503 496 CONECT 504 496 CONECT 505 496 CONECT 506 498 CONECT 507 498 CONECT 508 499 CONECT 509 497 CONECT 510 497 CONECT 511 497 CONECT 513 514 CONECT 514 513 515 CONECT 515 514 516 517 518 CONECT 516 515 CONECT 517 515 CONECT 518 515 CONECT 519 520 CONECT 520 519 521 CONECT 521 520 522 523 524 CONECT 522 521 CONECT 523 521 CONECT 524 521 MASTER 166 0 24 0 0 0 0 6 527 2 296 4 END