REMARK File generated by Swiss-PdbViewer 4.00b0 REMARK http://www.expasy.org/spdbv/ HEADER NUCLEAR RECEPTOR 05-AUG-99 1QKU TITLE WILD TYPE ESTROGEN NUCLEAR RECEPTOR LIGAND BINDING DOMAIN TITLE 2 COMPLEXED WITH ESTRADIOL COMPND MOL_ID: 1; COMPND 2 MOLECULE: ESTRADIOL RECEPTOR; COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 CELLULAR_LOCATION: NUCLEUS; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: BL21; SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15 KEYWDS AGONISM, ANTAGONISM, CRYSTAL STRUCTURE, ESTRADIOL RECEPTOR, KEYWDS 2 STEROID EXPDTA X-RAY DIFFRACTION AUTHOR M.RUFF,M.GANGLOFF,S.EILER,S.DUCLAUD,J.M.WURTZ,D.MORAS REVDAT 1 18-AUG-00 1QKU 0 REMARK 2 REMARK 2 RESOLUTION. 3.2 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.4 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 2087323.51 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.9 REMARK 3 NUMBER OF REFLECTIONS : 13994 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.275 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.7 REMARK 3 FREE R VALUE TEST SET COUNT : 1357 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.8 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1949 REMARK 3 BIN R VALUE (WORKING SET) : 0.303 REMARK 3 BIN FREE R VALUE : 0.372 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.1 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 195 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5940 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 60 REMARK 3 SOLVENT ATOMS : 607 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 60. REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.7 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 20.84 REMARK 3 B22 (A**2) : 20.84 REMARK 3 B33 (A**2) : -41.68 REMARK 3 B12 (A**2) : 0.66 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36 REMARK 3 ESD FROM SIGMAA (A) : 0.51 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.64 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.3 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.8 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.67 ; 1.50 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.88 ; 2.00 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.23 ; 2.00 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.57 ; 2.50 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.228664 REMARK 3 BSOL : 12.9798 REMARK 3 REMARK 3 NCS MODEL : NONE REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : ESTRADIOL.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ESTRADIOL.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1QKU COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 5-AUG-1999. REMARK 100 THE EBI ID CODE IS EBI-3008. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19255 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.9 REMARK 200 RESOLUTION RANGE LOW (A) : 15.0 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96 REMARK 200 DATA REDUNDANCY : 1.8 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 Y-X,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,1/3-Z REMARK 290 6555 -X,Y-X,2/3-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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.72000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.36000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.36000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 90.72000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 300 REMARK 300 THE ASYMMETRIC UNIT CONTAINS 2 INDEPENDENT MOLECULES. REMARK 300 CHAINS B AND C MAKE ONE HOMO-DIMER WITH CHAIN A REMARK 300 CONSISTING OF ONE HALF OF A SECOND DIMER REMARK 300 REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350 REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR REMARK 300 THE CHAIN IN THE COMPLEX IS 1983.2 ANGSTROM**2 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, Z 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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 45.35955 REMARK 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, Y, X 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER B 301 REMARK 465 LYS B 302 REMARK 465 LYS B 303 REMARK 465 SER C 301 REMARK 465 LYS C 302 REMARK 465 LYS C 303 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 301 OG REMARK 470 LYS A 302 CG CD CE NZ REMARK 470 LYS A 303 CG CD CE NZ 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 SER A 464 N - CA - C ANGL. DEV. = -11.7 DEGREES REMARK 500 LEU B 306 CA - CB - CG ANGL. DEV. = 10.9 DEGREES REMARK 500 THR B 465 CB - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 SER C 464 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY REMARK 525 ASSOCIATED WITH: REMARK 525 PROTEIN CHAIN SOLVENT CHAIN REMARK 525 A Z REMARK 525 B Y REMARK 525 C X REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: EST BINDING SITE FOR CHAIN A REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 SITE_DESCRIPTION: EST BINDING SITE FOR CHAIN B REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 SITE_DESCRIPTION: EST BINDING SITE FOR CHAIN C REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1QKU RELATED DB: PDB REMARK 900 MUTANT ESTROGEN NUCLEAR RECEPTOR LIGAND BINDING DOMAIN REMARK 900 COMPLEXED WITH ESTRADIOL REMARK 900 RELATED ID: 1HCP RELATED DB: PDB REMARK 900 HUMAN/CHICKEN ESTROGEN RECEPTOR REMARK 900 RELATED ID: 1HCQ RELATED DB: PDB REMARK 900 HUMAN/CHICKEN ESTROGEN RECEPTOR REMARK 900 RELATED ID: 1AKF RELATED DB: PDB REMARK 900 HOMOLOGOUS-EXTENSION-BASED MODEL OF HUMAN ESTROGEN RECEPTOR REMARK 900 WITH BOUND ESTRADIOL, THEORETICAL MODEL REMARK 900 RELATED ID: 1A52 RELATED DB: PDB REMARK 900 ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN COMPLEXED TO REMARK 900 ESTRADIOL REMARK 900 RELATED ID: 1ERE RELATED DB: PDB REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX REMARK 900 WITH 17BETA-ESTRADIOL REMARK 900 RELATED ID: 1ERR RELATED DB: PDB REMARK 900 HUMAN ESTROGEN RECEPTOR LIGAND-BINDING DOMAIN IN COMPLEX REMARK 900 WITH RALOXIFENE REMARK 900 RELATED ID: 3ERD RELATED DB: PDB REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN REMARK 900 COMPLEX WITH DIETHYLSTILBESTROL AND A GLUCOCORTICOID REMARK 900 RECEPTOR INTERACTING PROTEIN 1 NR BOX II PEPTIDE REMARK 900 RELATED ID: 3ERT RELATED DB: PDB REMARK 900 HUMAN ESTROGEN RECEPTOR ALPHA LIGAND-BINDING DOMAIN IN REMARK 900 COMPLEX WITH 4-HYDROXYTAMOXIFEN REMARK 900 RELATED ID: 1QKM RELATED DB: PDB REMARK 900 HUMAN ESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN REMARK 900 COMPLEX WITH PARTIAL AGONIST GENISTEIN REMARK 900 RELATED ID: 1QKN RELATED DB: PDB REMARK 900 RAT ESTROGEN RECEPTOR BETA LIGAND-BINDING DOMAIN IN REMARK 900 COMPLEX WITH ANTAGONIST RALOXIFENE REMARK 900 DBREF 1QKU A 301 550 SWS P03372 ESR1_HUMAN 301 550 DBREF 1QKU B 301 550 SWS P03372 ESR1_HUMAN 301 550 DBREF 1QKU C 301 550 SWS P03372 ESR1_HUMAN 301 550 CRYST1 105.500 105.500 136.080 90.00 90.00 120.00 P 32 2 1 18 ATOM 1 N LEU B 511 47.490 45.177 50.283 1.00 43.93 ATOM 2 CA LEU B 511 47.695 44.363 49.093 1.00 44.36 ATOM 3 C LEU B 511 48.803 43.332 49.289 1.00 43.26 ATOM 4 O LEU B 511 48.883 42.344 48.559 1.00 43.05 ATOM 5 CB LEU B 511 48.023 45.255 47.895 1.00 44.45 ATOM 6 CG LEU B 511 46.997 46.355 47.664 1.00 44.29 ATOM 7 CD1 LEU B 511 47.260 46.987 46.319 1.00 45.13 ATOM 8 CD2 LEU B 511 45.591 45.780 47.717 1.00 43.55 ATOM 9 N SER B 512 49.661 43.578 50.269 1.00 41.36 ATOM 10 CA SER B 512 50.742 42.663 50.576 1.00 40.36 ATOM 11 C SER B 512 50.090 41.433 51.208 1.00 39.92 ATOM 12 O SER B 512 50.306 40.299 50.776 1.00 38.52 ATOM 13 CB SER B 512 51.702 43.339 51.558 1.00 39.87 ATOM 14 OG SER B 512 52.638 42.429 52.090 1.00 41.50 ATOM 15 N HIS B 513 49.271 41.683 52.224 1.00 39.95 ATOM 16 CA HIS B 513 48.559 40.635 52.946 1.00 40.44 ATOM 17 C HIS B 513 47.653 39.861 52.004 1.00 36.55 ATOM 18 O HIS B 513 47.588 38.650 52.045 1.00 35.58 ATOM 19 CB HIS B 513 47.705 41.253 54.061 1.00 46.83 ATOM 20 CG HIS B 513 47.114 40.248 55.009 1.00 53.31 ATOM 21 ND1 HIS B 513 46.054 40.544 55.842 1.00 54.08 ATOM 22 CD2 HIS B 513 47.464 38.968 55.289 1.00 54.73 ATOM 23 CE1 HIS B 513 45.779 39.491 56.593 1.00 54.24 ATOM 24 NE2 HIS B 513 46.620 38.521 56.278 1.00 53.80 ATOM 25 N ILE B 514 46.946 40.573 51.152 1.00 35.23 ATOM 26 CA ILE B 514 46.047 39.921 50.229 1.00 34.48 ATOM 27 C ILE B 514 46.834 38.943 49.395 1.00 36.40 ATOM 28 O ILE B 514 46.485 37.767 49.290 1.00 37.82 ATOM 29 CB ILE B 514 45.358 40.951 49.338 1.00 33.05 ATOM 30 CG1 ILE B 514 44.607 41.944 50.231 1.00 32.38 ATOM 31 CG2 ILE B 514 44.403 40.264 48.378 1.00 29.99 ATOM 32 CD1 ILE B 514 43.853 43.011 49.494 1.00 35.07 ATOM 33 N ARG B 515 47.911 39.434 48.804 1.00 38.13 ATOM 34 CA ARG B 515 48.783 38.593 47.983 1.00 38.15 ATOM 35 C ARG B 515 49.067 37.322 48.776 1.00 35.41 ATOM 36 O ARG B 515 48.988 36.209 48.259 1.00 30.75 ATOM 37 CB ARG B 515 50.101 39.333 47.714 1.00 39.74 ATOM 38 CG ARG B 515 50.526 39.344 46.270 1.00 39.54 ATOM 39 CD ARG B 515 51.149 38.031 45.861 1.00 41.62 ATOM 40 NE ARG B 515 51.283 37.947 44.411 1.00 44.19 ATOM 41 CZ ARG B 515 51.703 38.947 43.640 1.00 46.29 ATOM 42 NH1 ARG B 515 52.032 40.121 44.179 1.00 43.89 ATOM 43 NH2 ARG B 515 51.794 38.774 42.323 1.00 49.98 ATOM 44 N HIS B 516 49.385 37.523 50.051 1.00 34.40 ATOM 45 CA HIS B 516 49.698 36.438 50.944 1.00 34.87 ATOM 46 C HIS B 516 48.528 35.476 51.094 1.00 36.81 ATOM 47 O HIS B 516 48.688 34.275 50.909 1.00 38.18 ATOM 48 CB HIS B 516 50.092 36.999 52.297 1.00 35.74 ATOM 49 CG HIS B 516 50.485 35.950 53.287 1.00 39.33 ATOM 50 ND1 HIS B 516 51.549 35.100 53.085 1.00 40.14 ATOM 51 CD2 HIS B 516 49.963 35.619 54.491 1.00 42.07 ATOM 52 CE1 HIS B 516 51.670 34.294 54.124 1.00 41.92 ATOM 53 NE2 HIS B 516 50.720 34.589 54.992 1.00 44.06 ATOM 54 N MET B 517 47.347 35.992 51.425 1.00 38.11 ATOM 55 CA MET B 517 46.177 35.131 51.596 1.00 38.29 ATOM 56 C MET B 517 45.897 34.370 50.305 1.00 37.53 ATOM 57 O MET B 517 45.352 33.265 50.311 1.00 37.15 ATOM 58 CB MET B 517 44.937 35.954 51.970 1.00 38.64 ATOM 59 CG MET B 517 44.989 36.649 53.324 1.00 40.43 ATOM 60 SD MET B 517 43.399 37.455 53.730 1.00 40.11 ATOM 61 CE MET B 517 43.154 38.421 52.254 1.00 37.60 ATOM 62 N SER B 518 46.274 34.972 49.189 1.00 37.15 ATOM 63 CA SER B 518 46.029 34.347 47.914 1.00 37.42 ATOM 64 C SER B 518 46.922 33.128 47.752 1.00 37.41 ATOM 65 O SER B 518 46.478 32.082 47.278 1.00 37.13 ATOM 66 CB SER B 518 46.280 35.351 46.797 1.00 38.01 ATOM 67 OG SER B 518 45.869 34.820 45.552 1.00 39.84 ATOM 68 N ASN B 519 48.180 33.260 48.156 1.00 37.23 ATOM 69 CA ASN B 519 49.113 32.153 48.036 1.00 39.36 ATOM 70 C ASN B 519 48.679 30.993 48.913 1.00 41.14 ATOM 71 O ASN B 519 48.508 29.868 48.437 1.00 41.44 ATOM 72 CB ASN B 519 50.519 32.595 48.433 1.00 39.46 ATOM 73 CG ASN B 519 51.114 33.577 47.451 1.00 40.52 ATOM 74 OD1 ASN B 519 51.118 33.332 46.242 1.00 42.91 ATOM 75 ND2 ASN B 519 51.625 34.691 47.957 1.00 37.55 ATOM 76 N LYS B 520 48.503 31.279 50.198 1.00 40.98 ATOM 77 CA LYS B 520 48.088 30.269 51.155 1.00 40.86 ATOM 78 C LYS B 520 46.759 29.639 50.733 1.00 40.34 ATOM 79 O LYS B 520 46.608 28.419 50.712 1.00 39.63 ATOM 80 CB LYS B 520 47.982 30.904 52.546 1.00 41.06 ATOM 81 CG LYS B 520 49.334 31.242 53.168 1.00 43.96 ATOM 82 CD LYS B 520 49.902 30.030 53.913 1.00 49.19 ATOM 83 CE LYS B 520 51.439 29.996 53.937 1.00 49.42 ATOM 84 NZ LYS B 520 52.028 29.521 52.640 1.00 50.74 ATOM 85 N GLY B 521 45.804 30.480 50.367 1.00 40.85 ATOM 86 CA GLY B 521 44.507 29.978 49.967 1.00 40.60 ATOM 87 C GLY B 521 44.561 29.145 48.709 1.00 40.06 ATOM 88 O GLY B 521 43.704 28.286 48.481 1.00 41.27 ATOM 89 N MET B 522 45.561 29.398 47.877 1.00 39.04 ATOM 90 CA MET B 522 45.686 28.646 46.640 1.00 39.23 ATOM 91 C MET B 522 46.222 27.257 46.947 1.00 41.35 ATOM 92 O MET B 522 45.757 26.265 46.381 1.00 42.11 ATOM 93 CB MET B 522 46.625 29.362 45.687 1.00 37.25 ATOM 94 CG MET B 522 46.659 28.781 44.299 1.00 34.44 ATOM 95 SD MET B 522 45.584 29.654 43.174 1.00 36.47 ATOM 96 CE MET B 522 46.221 31.329 43.320 1.00 35.65 ATOM 97 N GLU B 523 47.207 27.191 47.843 1.00 41.24 ATOM 98 CA GLU B 523 47.786 25.912 48.237 1.00 42.86 ATOM 99 C GLU B 523 46.675 25.063 48.822 1.00 42.80 ATOM 100 O GLU B 523 46.613 23.852 48.610 1.00 43.78 ATOM 101 CB GLU B 523 48.868 26.100 49.297 1.00 44.40 ATOM 102 CG GLU B 523 50.241 26.502 48.771 1.00 48.26 ATOM 103 CD GLU B 523 50.900 25.422 47.928 1.00 50.26 ATOM 104 OE1 GLU B 523 50.733 24.226 48.249 1.00 50.17 ATOM 105 OE2 GLU B 523 51.602 25.767 46.951 1.00 52.49 ATOM 106 N HIS B 524 45.798 25.722 49.566 1.00 41.27 ATOM 107 CA HIS B 524 44.675 25.056 50.191 1.00 39.47 ATOM 108 C HIS B 524 43.808 24.403 49.141 1.00 38.47 ATOM 109 O HIS B 524 43.637 23.190 49.159 1.00 40.05 ATOM 110 CB HIS B 524 43.845 26.061 50.998 1.00 40.05 ATOM 111 CG HIS B 524 42.637 25.463 51.654 1.00 41.73 ATOM 112 ND1 HIS B 524 41.538 25.036 50.943 1.00 41.59 ATOM 113 CD2 HIS B 524 42.356 25.216 52.958 1.00 44.07 ATOM 114 CE1 HIS B 524 40.632 24.554 51.777 1.00 42.25 ATOM 115 NE2 HIS B 524 41.103 24.651 53.007 1.00 41.74 ATOM 116 N LEU B 525 43.273 25.204 48.223 1.00 37.18 ATOM 117 CA LEU B 525 42.399 24.668 47.191 1.00 37.76 ATOM 118 C LEU B 525 43.044 23.494 46.486 1.00 38.51 ATOM 119 O LEU B 525 42.383 22.492 46.200 1.00 38.88 ATOM 120 CB LEU B 525 42.026 25.727 46.152 1.00 36.97 ATOM 121 CG LEU B 525 40.943 25.213 45.178 1.00 36.52 ATOM 122 CD1 LEU B 525 39.629 25.142 45.941 1.00 34.14 ATOM 123 CD2 LEU B 525 40.796 26.103 43.940 1.00 34.32 ATOM 124 N TYR B 526 44.332 23.612 46.197 1.00 39.31 ATOM 125 CA TYR B 526 45.016 22.520 45.534 1.00 42.67 ATOM 126 C TYR B 526 44.881 21.242 46.372 1.00 45.28 ATOM 127 O TYR B 526 44.627 20.155 45.847 1.00 46.15 ATOM 128 CB TYR B 526 46.483 22.868 45.331 1.00 40.40 ATOM 129 CG TYR B 526 47.267 21.788 44.620 1.00 42.74 ATOM 130 CD1 TYR B 526 47.787 20.699 45.318 1.00 43.28 ATOM 131 CD2 TYR B 526 47.515 21.866 43.251 1.00 44.03 ATOM 132 CE1 TYR B 526 48.541 19.721 44.677 1.00 43.33 ATOM 133 CE2 TYR B 526 48.268 20.890 42.603 1.00 46.72 ATOM 134 CZ TYR B 526 48.778 19.823 43.327 1.00 45.45 ATOM 135 OH TYR B 526 49.531 18.864 42.694 1.00 50.38 ATOM 136 N SER B 527 45.037 21.384 47.683 1.00 47.19 ATOM 137 CA SER B 527 44.924 20.258 48.588 1.00 47.37 ATOM 138 C SER B 527 43.558 19.608 48.522 1.00 47.41 ATOM 139 O SER B 527 43.453 18.403 48.394 1.00 48.95 ATOM 140 CB SER B 527 45.181 20.709 50.011 1.00 49.17 ATOM 141 OG SER B 527 44.858 19.662 50.906 1.00 54.44 ATOM 142 N MET B 528 42.512 20.413 48.633 1.00 48.55 ATOM 143 CA MET B 528 41.149 19.907 48.583 1.00 51.14 ATOM 144 C MET B 528 40.940 19.136 47.293 1.00 51.98 ATOM 145 O MET B 528 40.188 18.168 47.258 1.00 52.47 ATOM 146 CB MET B 528 40.157 21.065 48.654 1.00 52.10 ATOM 147 CG MET B 528 40.279 21.931 49.901 1.00 52.61 ATOM 148 SD MET B 528 39.706 21.168 51.440 1.00 54.65 ATOM 149 CE MET B 528 41.241 20.531 52.121 1.00 55.14 ATOM 150 N LYS B 529 41.599 19.572 46.229 1.00 52.49 ATOM 151 CA LYS B 529 41.483 18.887 44.953 1.00 55.90 ATOM 152 C LYS B 529 42.238 17.571 44.994 1.00 58.07 ATOM 153 O LYS B 529 41.896 16.632 44.282 1.00 58.92 ATOM 154 CB LYS B 529 42.030 19.753 43.819 1.00 57.66 ATOM 155 CG LYS B 529 42.256 19.001 42.509 1.00 57.95 ATOM 156 CD LYS B 529 42.697 19.941 41.401 1.00 59.45 ATOM 157 CE LYS B 529 43.474 19.211 40.312 1.00 60.14 ATOM 158 NZ LYS B 529 44.809 18.748 40.793 1.00 59.78 ATOM 159 N CYS B 530 43.276 17.501 45.819 1.00 60.01 ATOM 160 CA CYS B 530 44.040 16.267 45.932 1.00 61.14 ATOM 161 C CYS B 530 43.298 15.280 46.815 1.00 62.39 ATOM 162 O CYS B 530 43.625 14.103 46.849 1.00 63.70 ATOM 163 CB CYS B 530 45.439 16.534 46.492 1.00 61.10 ATOM 164 SG CYS B 530 46.703 16.700 45.193 1.00 61.58 ATOM 165 N LYS B 531 42.292 15.766 47.531 1.00 64.80 ATOM 166 CA LYS B 531 41.492 14.913 48.401 1.00 66.25 ATOM 167 C LYS B 531 40.166 14.607 47.731 1.00 66.32 ATOM 168 O LYS B 531 39.297 13.982 48.318 1.00 65.77 ATOM 169 CB LYS B 531 41.248 15.590 49.756 1.00 69.76 ATOM 170 CG LYS B 531 42.402 15.429 50.746 1.00 74.47 ATOM 171 CD LYS B 531 42.012 15.850 52.178 1.00 77.60 ATOM 172 CE LYS B 531 43.090 15.451 53.203 1.00 76.54 ATOM 173 NZ LYS B 531 42.743 15.804 54.613 1.00 73.28 SPDBVT 1.0000000000 0.0000000000 0.0000000000 SPDBVT 0.0000000000 1.0000000000 0.0000000000 SPDBVT 0.0000000000 0.0000000000 1.0000000000 SPDBVT 0.0000000000 0.0000000000 0.0000000000 SPDBVT 0.0000000000 0.0000000000 0.0000000000 SPDBVV default; SPDBVV 50.327543725854 3726.032155488835 20.000000000000 SPDBVV 0.1196072202 0.2495495400 0.9609470016 SPDBVV 0.9917187727 -0.0756319326 -0.1037963711 SPDBVV 0.0467759422 0.9654039765 -0.2565290888 SPDBVV 45.9674987793 30.4845008850 48.4524993896 SPDBVV 0.0000000000 0.0000000000 0.0000000000 SPDBVf 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 19 SPDBVf 19 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 SPDBVl 1.00 1.00 1.00 SPDBVb 0.10 0.10 0.10 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 64 64 SPDBVg 64 64 64 64 64 64 64 64 SPDBVi 1 1 1 0 1 0 1 1 0 1 0 0 1 0 0 SPDBVp 9606 END