REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.5 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 551538.890 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4 REMARK 3 NUMBER OF REFLECTIONS : 73464 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) : 0.253 REMARK 3 FREE R VALUE : 0.285 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 3726 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005 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) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10014 REMARK 3 BIN R VALUE (WORKING SET) : 0.3900 REMARK 3 BIN FREE R VALUE : 0.4190 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 519 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 18308 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 49.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 11.20000 REMARK 3 B22 (A**2) : -4.64000 REMARK 3 B33 (A**2) : -6.56000 REMARK 3 B12 (A**2) : 5.26000 REMARK 3 B13 (A**2) : 1.18000 REMARK 3 B23 (A**2) : -8.71000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.46 REMARK 3 ESD FROM SIGMAA (A) : 0.58 REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.54 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.66 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.60 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.20 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.94 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) : 2.750 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.660 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.770 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.800 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.31 REMARK 3 BSOL : 38.46 REMARK 3 REMARK 3 NCS MODEL : CONSTR 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.PA REMARK 3 PARAMETER FILE 2 : CIS_PEPT REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FSK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-00. REMARK 100 THE RCSB ID CODE IS RCSB011866. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-MAY-98 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 4.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MAX II REMARK 200 BEAMLINE : I711 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.950 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 : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.04700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.8500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.37000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL 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 (%): 65.49 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.1M SODIUM CITRATE, REMARK 280 PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K 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 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I 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 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L 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: 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 TYR K 94 N - CA - C ANGL. DEV. = -16.4 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 TYR A 5 71.85 -159.81 REMARK 500 GLU A 6 171.17 -55.92 REMARK 500 ALA A 16 -75.77 -30.42 REMARK 500 ALA A 21 -79.15 -51.72 REMARK 500 ILE A 23 -75.47 -100.68 REMARK 500 ASP A 27 8.26 -64.55 REMARK 500 PRO A 35 -28.55 -38.86 REMARK 500 ALA A 37 -60.28 -99.42 REMARK 500 LEU A 62 173.97 -55.86 REMARK 500 ASP A 93 -92.84 56.09 REMARK 500 GLU A 96 -63.54 -93.61 REMARK 500 ASN A 118 56.54 -163.59 REMARK 500 ASP A 125 23.92 -162.05 REMARK 500 ALA A 130 -16.91 -41.32 REMARK 500 TYR A 158 57.23 25.36 REMARK 500 GLU B 17 173.58 -55.87 REMARK 500 ASP B 30 -97.61 60.74 REMARK 500 TYR B 32 48.04 -82.03 REMARK 500 LEU B 47 -73.41 -91.00 REMARK 500 PRO B 51 156.02 -49.82 REMARK 500 VAL B 58 117.41 -12.67 REMARK 500 ASP B 60 2.21 -57.17 REMARK 500 SER B 67 172.38 176.51 REMARK 500 THR B 68 -87.30 70.51 REMARK 500 ASP B 82 4.57 -52.79 REMARK 500 ALA B 84 -177.96 -172.43 REMARK 500 PRO B 113 173.50 -54.62 REMARK 500 PRO B 120 135.70 -37.29 REMARK 500 PHE B 139 -159.87 -106.73 REMARK 500 TYR B 140 125.57 162.95 REMARK 500 PRO B 141 174.90 -58.18 REMARK 500 SER B 162 135.77 179.51 REMARK 500 THR B 164 -155.22 -92.67 REMARK 500 GLN B 166 118.73 -32.41 REMARK 500 ARG B 188 5.33 -68.15 REMARK 500 ASN B 190 -78.37 -98.58 REMARK 500 HIS B 198 -125.92 -89.63 REMARK 500 LYS B 199 8.78 -153.38 REMARK 500 GLU B 213 2.85 -67.95 REMARK 500 VAL C 2 102.20 176.04 REMARK 500 PRO C 41 117.93 -36.01 REMARK 500 PRO C 53 -157.83 -67.13 REMARK 500 SER C 54 -71.50 69.53 REMARK 500 LYS C 63 -28.07 -39.79 REMARK 500 LYS C 65 -64.73 -18.50 REMARK 500 SER C 77 63.21 35.72 REMARK 500 ALA C 92 -175.55 -177.22 REMARK 500 ARG C 101 95.88 -32.68 REMARK 500 ASP C 102 11.71 86.84 REMARK 500 ALA C 134 47.59 -71.15 REMARK 500 LEU C 143 -144.42 -115.68 REMARK 500 SER C 177 74.01 26.15 REMARK 500 TYR D 5 71.85 -159.85 REMARK 500 GLU D 6 171.18 -55.89 REMARK 500 ALA D 16 -75.83 -30.43 REMARK 500 ALA D 21 -79.20 -51.72 REMARK 500 ILE D 23 -75.56 -100.71 REMARK 500 ASP D 27 8.15 -64.57 REMARK 500 PRO D 35 -28.64 -38.82 REMARK 500 ALA D 37 -60.24 -99.63 REMARK 500 LEU D 62 173.88 -55.67 REMARK 500 ASP D 93 -92.55 56.03 REMARK 500 GLU D 96 -63.49 -93.57 REMARK 500 ASN D 118 56.33 -163.32 REMARK 500 ASP D 125 23.90 -162.09 REMARK 500 ALA D 130 -16.95 -41.38 REMARK 500 TYR D 158 57.30 25.40 REMARK 500 GLU E 17 173.64 -56.04 REMARK 500 ASP E 30 -97.74 60.88 REMARK 500 TYR E 32 48.08 -82.26 REMARK 500 LEU E 47 -73.29 -91.27 REMARK 500 PRO E 51 156.03 -49.87 REMARK 500 VAL E 58 117.50 -12.84 REMARK 500 ASP E 60 2.17 -57.03 REMARK 500 SER E 67 172.34 176.77 REMARK 500 THR E 68 -87.15 70.57 REMARK 500 ASP E 82 4.52 -52.94 REMARK 500 ALA E 84 -178.07 -172.43 REMARK 500 PRO E 113 173.53 -54.48 REMARK 500 PRO E 120 135.68 -37.35 REMARK 500 PHE E 139 -159.87 -106.65 REMARK 500 TYR E 140 125.55 163.05 REMARK 500 PRO E 141 174.86 -58.16 REMARK 500 SER E 162 135.69 179.57 REMARK 500 THR E 164 -155.27 -92.83 REMARK 500 GLN E 166 118.61 -32.16 REMARK 500 ARG E 188 5.25 -68.10 REMARK 500 ASN E 190 -78.34 -98.66 REMARK 500 HIS E 198 -125.89 -89.69 REMARK 500 LYS E 199 8.88 -153.41 REMARK 500 GLU E 213 2.87 -67.85 REMARK 500 VAL F 2 102.24 176.23 REMARK 500 PRO F 41 117.83 -35.99 REMARK 500 PRO F 53 -157.58 -67.07 REMARK 500 SER F 54 -71.33 69.29 REMARK 500 LYS F 63 -28.04 -39.84 REMARK 500 LYS F 65 -64.81 -18.45 REMARK 500 SER F 77 63.30 35.65 REMARK 500 ALA F 92 -175.60 -177.37 REMARK 500 ARG F 101 96.18 -32.66 REMARK 500 ASP F 102 11.67 86.45 REMARK 500 ALA F 134 47.50 -71.11 REMARK 500 LEU F 143 -144.58 -115.77 REMARK 500 SER F 177 74.04 26.07 REMARK 500 TYR G 5 71.67 -159.83 REMARK 500 GLU G 6 171.15 -55.67 REMARK 500 ALA G 16 -75.92 -30.48 REMARK 500 ALA G 21 -79.10 -51.88 REMARK 500 ILE G 23 -75.70 -100.57 REMARK 500 ASP G 27 8.11 -64.53 REMARK 500 PRO G 35 -28.52 -38.77 REMARK 500 ALA G 37 -60.45 -99.42 REMARK 500 LEU G 62 173.97 -55.63 REMARK 500 ASP G 93 -92.68 55.98 REMARK 500 GLU G 96 -63.47 -93.76 REMARK 500 ASN G 118 56.44 -163.62 REMARK 500 ASP G 125 23.92 -162.11 REMARK 500 ALA G 130 -16.85 -41.31 REMARK 500 TYR G 158 57.24 25.37 REMARK 500 GLU H 17 173.59 -55.77 REMARK 500 ASP H 30 -97.58 60.78 REMARK 500 TYR H 32 48.12 -82.17 REMARK 500 LEU H 47 -73.04 -91.15 REMARK 500 PRO H 51 156.00 -49.78 REMARK 500 VAL H 58 117.58 -12.67 REMARK 500 ASP H 60 2.13 -57.14 REMARK 500 SER H 67 172.48 176.72 REMARK 500 THR H 68 -87.16 70.59 REMARK 500 ASP H 82 4.48 -52.73 REMARK 500 ALA H 84 -177.86 -172.48 REMARK 500 PRO H 113 173.57 -54.40 REMARK 500 PRO H 120 135.62 -37.24 REMARK 500 PHE H 139 -159.86 -106.65 REMARK 500 TYR H 140 125.46 162.98 REMARK 500 PRO H 141 174.89 -58.19 REMARK 500 SER H 162 135.87 179.53 REMARK 500 THR H 164 -155.14 -92.68 REMARK 500 GLN H 166 118.60 -32.23 REMARK 500 ARG H 188 5.23 -67.98 REMARK 500 ASN H 190 -78.45 -98.63 REMARK 500 HIS H 198 -125.94 -89.63 REMARK 500 LYS H 199 8.85 -153.35 REMARK 500 GLU H 213 2.78 -67.90 REMARK 500 VAL I 2 102.24 176.22 REMARK 500 PRO I 41 118.01 -35.95 REMARK 500 PRO I 53 -157.67 -67.09 REMARK 500 SER I 54 -71.45 69.19 REMARK 500 LYS I 63 -28.10 -39.81 REMARK 500 LYS I 65 -64.85 -18.52 REMARK 500 SER I 77 63.35 35.70 REMARK 500 ALA I 92 -175.66 -177.36 REMARK 500 ARG I 101 95.97 -32.85 REMARK 500 ASP I 102 11.67 86.68 REMARK 500 ALA I 134 47.62 -71.17 REMARK 500 LEU I 143 -144.38 -115.50 REMARK 500 SER I 177 73.88 26.26 REMARK 500 TYR J 5 71.78 -159.84 REMARK 500 GLU J 6 171.18 -55.80 REMARK 500 ALA J 16 -75.81 -30.47 REMARK 500 ALA J 21 -79.15 -51.85 REMARK 500 ILE J 23 -75.77 -100.49 REMARK 500 ASP J 27 8.29 -64.53 REMARK 500 PRO J 35 -28.56 -38.85 REMARK 500 ALA J 37 -60.46 -99.37 REMARK 500 LEU J 62 173.91 -55.66 REMARK 500 ASP J 93 -92.82 56.10 REMARK 500 GLU J 96 -63.65 -93.54 REMARK 500 ASN J 118 56.40 -163.60 REMARK 500 ASP J 125 23.82 -162.08 REMARK 500 ALA J 130 -16.88 -41.31 REMARK 500 TYR J 158 57.17 25.39 REMARK 500 GLU K 17 173.59 -55.86 REMARK 500 ASP K 30 -97.63 60.78 REMARK 500 TYR K 32 48.27 -82.19 REMARK 500 LEU K 47 -73.04 -91.27 REMARK 500 PRO K 51 155.98 -49.82 REMARK 500 VAL K 58 117.49 -12.73 REMARK 500 ASP K 60 2.12 -57.20 REMARK 500 SER K 67 172.46 176.74 REMARK 500 THR K 68 -87.15 70.55 REMARK 500 ASP K 82 4.49 -52.86 REMARK 500 ALA K 84 -177.89 -172.21 REMARK 500 PRO K 113 173.60 -54.51 REMARK 500 PRO K 120 135.71 -37.18 REMARK 500 PHE K 139 -159.94 -106.75 REMARK 500 TYR K 140 125.50 163.07 REMARK 500 PRO K 141 174.86 -58.06 REMARK 500 SER K 162 135.72 179.57 REMARK 500 THR K 164 -155.23 -92.94 REMARK 500 GLN K 166 118.74 -32.33 REMARK 500 ARG K 188 5.31 -67.93 REMARK 500 ASN K 190 -78.46 -98.68 REMARK 500 HIS K 198 -125.87 -89.68 REMARK 500 LYS K 199 8.81 -153.36 REMARK 500 GLU K 213 2.85 -67.90 REMARK 500 VAL L 2 102.20 176.29 REMARK 500 PRO L 41 117.94 -36.04 REMARK 500 PRO L 53 -157.54 -67.19 REMARK 500 SER L 54 -71.54 69.18 REMARK 500 LYS L 63 -28.05 -39.86 REMARK 500 LYS L 65 -64.83 -18.38 REMARK 500 SER L 77 63.32 35.83 REMARK 500 ALA L 92 -175.77 -177.38 REMARK 500 ARG L 101 95.97 -32.82 REMARK 500 ASP L 102 11.50 86.80 REMARK 500 ALA L 134 47.56 -71.12 REMARK 500 LEU L 143 -144.35 -115.63 REMARK 500 SER L 177 73.98 26.16 REMARK 500 REMARK 500 REMARK: NULL