HEADER TRANSCRIPTION 09-SEP-97 1PCF TITLE HUMAN TRANSCRIPTIONAL COACTIVATOR PC4 C-TERMINAL DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRANSCRIPTIONAL COACTIVATOR PC4; COMPND 3 CHAIN: A, B, C, D, E, F, G, H; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN; COMPND 5 SYNONYM: P15; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 CELL_LINE: BL21; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET-11A; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21 KEYWDS TRANSCRIPTION, TRANSCRIPTIONAL COFACTOR, TRANSCRIPTIONAL CO- KEYWDS 2 ACTIVATOR, SSDNA BINDING, NUCLEAR PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.BRANDSEN,P.GROS REVDAT 2 01-APR-03 1PCF 1 JRNL REVDAT 1 18-MAR-98 1PCF 0 JRNL AUTH J.BRANDSEN,S.WERTEN,P.C.VAN DER VLIET, JRNL AUTH 2 M.MEISTERERNST,J.KROON,P.GROS JRNL TITL C-TERMINAL DOMAIN OF TRANSCRIPTION COFACTOR PC4 JRNL TITL 2 REVEALS DIMERIC SSDNA BINDING SITE. JRNL REF NAT.STRUCT.BIOL. V. 4 900 1997 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.74 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CCP4 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 3 NUMBER OF REFLECTIONS : 69529 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : SHELL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3495 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1970 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3495 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 69529 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4360 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 434 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : 0.08 REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.013 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.028 ; 0.040 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; 0.050 REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.031 ; 0.040 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.141 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.176 ; 0.300 REMARK 3 MULTIPLE TORSION (A) : 0.248 ; 0.300 REMARK 3 H-BOND (X...Y) (A) : 0.167 ; 0.300 REMARK 3 H-BOND (X-H...Y) (A) : NULL ; 0.300 REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; 15.000 REMARK 3 PLANAR (DEGREES) : 5.100 ; 7.000 REMARK 3 STAGGERED (DEGREES) : 16.400; 15.000 REMARK 3 TRANSVERSE (DEGREES) : 18.900; 20.000 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 2.035 ; 3.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.773 ; 5.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 4.752 ; 6.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.820 ; 8.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PCF COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : SEP-1996 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X11 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9117 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE AREA DETECTOR 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 : 69529 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 200 DATA REDUNDANCY : 2.600 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : 0.06000 REMARK 200 FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4 REMARK 200 DATA REDUNDANCY IN SHELL : 1.50 REMARK 200 R MERGE FOR SHELL (I) : 0.22900 REMARK 200 R SYM FOR SHELL (I) : 0.22900 REMARK 200 FOR SHELL : 2.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 25% REMARK 280 MPD, 200 MM NACL AND 100 MM NAAC BUFFER (PH 4.6) 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, 2, 3, 4 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 8 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 BIOMOLECULE: 3 REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 BIOMOLECULE: 4 REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 DBREF 1PCF A 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF B 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF C 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF D 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF E 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF F 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF G 63 127 UNP P53999 TCP4_HUMAN 62 126 DBREF 1PCF H 63 127 UNP P53999 TCP4_HUMAN 62 126 SEQRES 1 A 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 A 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 A 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 A 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 A 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 A 66 LEU SEQRES 1 B 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 B 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 B 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 B 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 B 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 B 66 LEU SEQRES 1 C 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 C 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 C 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 C 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 C 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 C 66 LEU SEQRES 1 D 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 D 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 D 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 D 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 D 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 D 66 LEU SEQRES 1 E 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 E 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 E 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 E 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 E 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 E 66 LEU SEQRES 1 F 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 F 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 F 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 F 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 F 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 F 66 LEU SEQRES 1 G 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 G 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 G 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 G 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 G 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 G 66 LEU SEQRES 1 H 66 ALA MET PHE GLN ILE GLY LYS MET ARG TYR VAL SER VAL SEQRES 2 H 66 ARG ASP PHE LYS GLY LYS VAL LEU ILE ASP ILE ARG GLU SEQRES 3 H 66 TYR TRP MET ASP PRO GLU GLY GLU MET LYS PRO GLY ARG SEQRES 4 H 66 LYS GLY ILE SER LEU ASN PRO GLU GLN TRP SER GLN LEU SEQRES 5 H 66 LYS GLU GLN ILE SER ASP ILE ASP ASP ALA VAL ARG LYS SEQRES 6 H 66 LEU FORMUL 9 HOH *434(H2 O) HELIX 1 1 PRO A 107 ARG A 125 1 19 HELIX 2 2 PRO B 107 ARG B 125 1 19 HELIX 3 3 PRO C 107 ARG C 125 1 19 HELIX 4 4 PRO D 107 ARG D 125 1 19 HELIX 5 5 PRO E 107 ARG E 125 1 19 HELIX 6 6 PRO F 107 ARG F 125 1 19 HELIX 7 7 PRO G 107 ARG G 125 1 19 HELIX 8 8 PRO H 107 ARG H 125 1 19 SHEET 1 A 4 LYS A 101 LEU A 105 0 SHEET 2 A 4 LYS A 80 GLU A 87 -1 N ILE A 85 O ILE A 103 SHEET 3 A 4 ARG A 70 PHE A 77 -1 N PHE A 77 O LYS A 80 SHEET 4 A 4 MET A 63 GLY A 67 -1 N GLY A 67 O ARG A 70 SHEET 1 B 2 TYR A 88 MET A 90 0 SHEET 2 B 2 MET A 96 PRO A 98 -1 N LYS A 97 O TRP A 89 SHEET 1 C 4 LYS B 101 LEU B 105 0 SHEET 2 C 4 LYS B 80 GLU B 87 -1 N ILE B 85 O ILE B 103 SHEET 3 C 4 ARG B 70 PHE B 77 -1 N PHE B 77 O LYS B 80 SHEET 4 C 4 MET B 63 GLY B 67 -1 N GLY B 67 O ARG B 70 SHEET 1 D 2 TYR B 88 MET B 90 0 SHEET 2 D 2 MET B 96 PRO B 98 -1 N LYS B 97 O TRP B 89 SHEET 1 E 4 LYS C 101 LEU C 105 0 SHEET 2 E 4 LYS C 80 GLU C 87 -1 N ILE C 85 O ILE C 103 SHEET 3 E 4 ARG C 70 PHE C 77 -1 N PHE C 77 O LYS C 80 SHEET 4 E 4 MET C 63 GLY C 67 -1 N GLY C 67 O ARG C 70 SHEET 1 F 2 TYR C 88 MET C 90 0 SHEET 2 F 2 MET C 96 PRO C 98 -1 N LYS C 97 O TRP C 89 SHEET 1 G 4 LYS D 101 LEU D 105 0 SHEET 2 G 4 LYS D 80 GLU D 87 -1 N ILE D 85 O ILE D 103 SHEET 3 G 4 ARG D 70 PHE D 77 -1 N PHE D 77 O LYS D 80 SHEET 4 G 4 MET D 63 GLY D 67 -1 N GLY D 67 O ARG D 70 SHEET 1 H 2 TYR D 88 MET D 90 0 SHEET 2 H 2 MET D 96 PRO D 98 -1 N LYS D 97 O TRP D 89 SHEET 1 I 4 LYS E 101 LEU E 105 0 SHEET 2 I 4 LYS E 80 GLU E 87 -1 N ILE E 85 O ILE E 103 SHEET 3 I 4 ARG E 70 PHE E 77 -1 N PHE E 77 O LYS E 80 SHEET 4 I 4 MET E 63 GLY E 67 -1 N GLY E 67 O ARG E 70 SHEET 1 J 2 TYR E 88 MET E 90 0 SHEET 2 J 2 MET E 96 PRO E 98 -1 N LYS E 97 O TRP E 89 SHEET 1 K 4 LYS F 101 LEU F 105 0 SHEET 2 K 4 LYS F 80 GLU F 87 -1 N ILE F 85 O ILE F 103 SHEET 3 K 4 ARG F 70 PHE F 77 -1 N PHE F 77 O LYS F 80 SHEET 4 K 4 MET F 63 GLY F 67 -1 N GLY F 67 O ARG F 70 SHEET 1 L 2 TYR F 88 MET F 90 0 SHEET 2 L 2 MET F 96 PRO F 98 -1 N LYS F 97 O TRP F 89 SHEET 1 M 4 LYS G 101 LEU G 105 0 SHEET 2 M 4 LYS G 80 GLU G 87 -1 N ILE G 85 O ILE G 103 SHEET 3 M 4 ARG G 70 PHE G 77 -1 N PHE G 77 O LYS G 80 SHEET 4 M 4 MET G 63 GLY G 67 -1 N GLY G 67 O ARG G 70 SHEET 1 N 2 TYR G 88 MET G 90 0 SHEET 2 N 2 MET G 96 PRO G 98 -1 N LYS G 97 O TRP G 89 SHEET 1 O 4 LYS H 101 LEU H 105 0 SHEET 2 O 4 LYS H 80 GLU H 87 -1 N ILE H 85 O ILE H 103 SHEET 3 O 4 ARG H 70 PHE H 77 -1 N PHE H 77 O LYS H 80 SHEET 4 O 4 MET H 63 GLY H 67 -1 N GLY H 67 O ARG H 70 SHEET 1 P 2 TYR H 88 MET H 90 0 SHEET 2 P 2 MET H 96 PRO H 98 -1 N LYS H 97 O TRP H 89 CRYST1 41.283 67.814 67.170 87.69 84.37 85.79 P 1 8 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 0.024223 -0.001783 -0.002330 0.00000 SCALE2 0.000000 0.014786 -0.000493 0.00000 SCALE3 0.000000 0.000000 0.014968 0.00000 MTRIX1 1 -0.957210 -0.148412 0.248442 70.75560 1 MTRIX2 1 -0.166878 -0.418310 -0.892843 148.73750 1 MTRIX3 1 0.236434 -0.896097 0.375644 84.38610 1 MTRIX1 2 0.967650 -0.200512 -0.153130 15.03080 1 MTRIX2 2 0.140180 -0.077347 0.987100 -46.03310 1 MTRIX3 2 -0.209770 -0.976633 -0.046737 136.97400 1 MTRIX1 3 -0.998872 -0.035171 -0.031883 99.20800 1 MTRIX2 3 -0.022192 0.939681 -0.341331 42.41450 1 MTRIX3 3 0.041965 -0.340239 -0.939402 179.37010 1 MTRIX1 4 0.981550 -0.013781 -0.190706 0.33040 1 MTRIX2 4 -0.021136 -0.999107 -0.036585 81.47150 1 MTRIX3 4 -0.190031 0.039941 -0.980965 173.18330 1 MTRIX1 5 -0.980983 0.186876 -0.052431 100.70740 1 MTRIX2 5 0.017002 0.351836 0.935907 -40.33760 1 MTRIX3 5 0.193346 0.917218 -0.348323 72.34110 1 MTRIX1 6 0.995407 0.075178 -0.059274 -23.79220 1 MTRIX2 6 -0.059633 0.002541 -0.998217 123.06930 1 MTRIX3 6 -0.074894 0.997167 0.007012 50.12130 1 MTRIX1 7 -0.961603 0.173417 0.212712 87.35570 1 MTRIX2 7 -0.076437 -0.913627 0.399303 58.45530 1 MTRIX3 7 0.263585 0.367712 0.891802 -12.85080 1