REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.DUTZLER,E.B.CAMBELL,R.MACKINNON REMARK 1 TITL GATING THE SELECTIVITY FILTER IN CLC CHLORIDE REMARK 1 TITL 2 CHANNELS REMARK 1 REF SCIENCE V. 300 108 2003 REMARK 1 REFN ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. 3.32 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.32 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.81 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 36343 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 + TEST SET) : 0.250 REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.287 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1928 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.32 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1377 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.3160 REMARK 3 BIN FREE R VALUE SET COUNT : 47 REMARK 3 BIN FREE R VALUE : 0.4730 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13223 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) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 94.83 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.59000 REMARK 3 B22 (A**2) : 0.06000 REMARK 3 B33 (A**2) : -0.34000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.66000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.583 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.475 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.980 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.870 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13551 ; 0.007 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18452 ; 1.082 ; 1.961 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1743 ; 5.153 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 479 ;35.222 ;22.985 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2145 ;18.305 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 67 ;13.521 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2121 ; 0.070 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10079 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6813 ; 0.206 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9351 ; 0.307 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 441 ; 0.140 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 23 ; 0.152 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 1 ; 0.047 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8841 ; 0.446 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13908 ; 0.809 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5427 ; 0.543 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4544 ; 0.917 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 A 18 A 458 3 REMARK 3 1 B 18 B 458 3 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 1764 ; 0.02 ; 0.05 REMARK 3 LOOSE POSITIONAL 1 A (A): 1540 ; 0.42 ; 5.00 REMARK 3 TIGHT THERMAL 1 A (A**2): 1764 ; 3.50 ; 0.50 REMARK 3 LOOSE THERMAL 1 A (A**2): 1540 ; 3.29 ; 10.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2FED COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-05. REMARK 100 THE RCSB ID CODE IS RCSB035776. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9198 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36343 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.317 REMARK 200 RESOLUTION RANGE LOW (A) : 49.810 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.3 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.09600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.32 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.47000 REMARK 200 R SYM FOR SHELL (I) : 0.47000 REMARK 200 FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1OTS REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.05 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 250 MM NACL, PEG 400 37%, 0.05 M REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 116.13700 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.11300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 116.13700 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.11300 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 MET A 1 REMARK 465 LYS A 2 REMARK 465 THR A 3 REMARK 465 ASP A 4 REMARK 465 THR A 5 REMARK 465 PRO A 6 REMARK 465 SER A 7 REMARK 465 LEU A 8 REMARK 465 GLU A 9 REMARK 465 THR A 10 REMARK 465 PRO A 11 REMARK 465 GLN A 12 REMARK 465 ALA A 13 REMARK 465 ALA A 14 REMARK 465 ARG A 15 REMARK 465 LEU A 16 REMARK 465 LEU A 461 REMARK 465 ALA A 462 REMARK 465 ARG A 463 REMARK 465 SER A 464 REMARK 465 LYS A 465 REMARK 465 MET B 1 REMARK 465 LYS B 2 REMARK 465 THR B 3 REMARK 465 ASP B 4 REMARK 465 THR B 5 REMARK 465 PRO B 6 REMARK 465 SER B 7 REMARK 465 LEU B 8 REMARK 465 GLU B 9 REMARK 465 THR B 10 REMARK 465 PRO B 11 REMARK 465 GLN B 12 REMARK 465 ALA B 13 REMARK 465 ALA B 14 REMARK 465 ARG B 15 REMARK 465 LEU B 16 REMARK 465 ARG B 17 REMARK 465 GLU B 459 REMARK 465 GLN B 460 REMARK 465 LEU B 461 REMARK 465 ALA B 462 REMARK 465 ARG B 463 REMARK 465 SER B 464 REMARK 465 LYS B 465 REMARK 465 GLU C 1 REMARK 465 GLU E 1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLN B 203 N ARG B 205 2.19 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 GLU A 27 40.64 -105.96 REMARK 500 ASP A 73 -74.68 -81.68 REMARK 500 ASN A 74 104.77 -54.50 REMARK 500 SER A 107 -79.80 -68.80 REMARK 500 PHE A 132 -73.19 -54.50 REMARK 500 LEU A 136 -39.27 -37.54 REMARK 500 ARG A 167 61.71 26.91 REMARK 500 ASN A 191 29.57 45.31 REMARK 500 GLU A 202 -51.19 -125.76 REMARK 500 GLN A 203 -132.85 -99.64 REMARK 500 MET A 204 -42.17 43.82 REMARK 500 PRO A 206 104.23 -44.48 REMARK 500 LEU A 212 39.82 -93.15 REMARK 500 GLU A 235 -7.98 65.07 REMARK 500 VAL A 241 -8.25 -143.02 REMARK 500 ASN A 250 5.69 -66.56 REMARK 500 PHE A 307 -52.50 -136.36 REMARK 500 ALA A 309 83.13 -169.79 REMARK 500 ASN A 418 60.47 -113.80 REMARK 500 PRO A 443 103.50 -55.02 REMARK 500 ASP B 73 -71.00 -84.15 REMARK 500 SER B 107 -78.10 -68.33 REMARK 500 VAL B 122 79.93 -117.05 REMARK 500 PHE B 132 -77.02 -51.43 REMARK 500 LEU B 136 -37.70 -37.42 REMARK 500 ASN B 191 27.67 48.12 REMARK 500 GLU B 202 -52.43 -123.89 REMARK 500 GLN B 203 -128.72 -99.90 REMARK 500 MET B 204 -43.73 42.44 REMARK 500 PRO B 206 102.40 -43.11 REMARK 500 LEU B 212 36.53 -92.63 REMARK 500 GLU B 235 -7.06 62.44 REMARK 500 VAL B 241 -10.38 -142.20 REMARK 500 ASN B 250 4.34 -64.44 REMARK 500 PHE B 307 -47.49 -138.19 REMARK 500 ALA B 309 79.88 -168.13 REMARK 500 ASN B 418 61.29 -115.56 REMARK 500 PRO B 443 103.53 -55.34 REMARK 500 SER C 7 -169.41 -122.94 REMARK 500 SER C 30 -169.55 -70.05 REMARK 500 ARG C 31 -28.77 66.57 REMARK 500 PRO C 62 92.06 -44.45 REMARK 500 LYS C 65 -126.71 22.65 REMARK 500 LYS C 85 75.77 16.33 REMARK 500 ALA C 141 -154.02 -97.34 REMARK 500 LEU C 146 -164.15 -114.44 REMARK 500 SER C 164 44.50 33.91 REMARK 500 ALA C 180 65.16 38.70 REMARK 500 SER D 7 -74.09 -71.14 REMARK 500 SER D 27 -167.18 -103.81 REMARK 500 TYR D 31 86.65 52.45 REMARK 500 THR D 50 -38.43 69.97 REMARK 500 SER D 51 -3.47 -152.64 REMARK 500 SER D 55 73.82 -63.02 REMARK 500 THR D 76 96.21 63.58 REMARK 500 GLU D 80 30.96 -63.29 REMARK 500 TRP D 90 14.66 -150.16 REMARK 500 ASP D 109 151.70 -48.93 REMARK 500 THR D 125 29.90 -70.27 REMARK 500 SER D 126 -3.59 -148.97 REMARK 500 ASN D 137 79.24 60.00 REMARK 500 ASP D 169 -4.77 -143.70 REMARK 500 ARG D 187 31.78 -96.93 REMARK 500 ASN D 189 -51.25 -124.25 REMARK 500 SER E 25 122.50 -175.64 REMARK 500 ARG E 31 -25.75 75.70 REMARK 500 LYS E 43 -159.72 -132.49 REMARK 500 ILE E 48 -62.34 -94.73 REMARK 500 SER E 55 15.05 56.44 REMARK 500 PRO E 62 87.80 -34.72 REMARK 500 LYS E 65 -15.54 -47.02 REMARK 500 LYS E 85 76.48 42.78 REMARK 500 ALA E 122 -179.15 -56.80 REMARK 500 SER E 136 -54.58 -26.96 REMARK 500 ALA E 139 49.41 -69.58 REMARK 500 ALA E 140 91.49 -49.40 REMARK 500 ALA E 141 -127.03 -81.03 REMARK 500 PRO E 155 -143.97 -97.75 REMARK 500 PRO E 157 -165.20 -107.80 REMARK 500 SER E 164 27.73 49.25 REMARK 500 SER E 194 49.68 -83.19 REMARK 500 SER E 195 9.45 -167.48 REMARK 500 SER E 198 -0.57 -56.29 REMARK 500 SER F 7 -104.22 -37.47 REMARK 500 SER F 27 -153.28 -113.93 REMARK 500 TYR F 31 73.62 58.31 REMARK 500 ARG F 45 108.61 -52.86 REMARK 500 TRP F 46 -61.75 -95.81 REMARK 500 THR F 50 -45.17 66.91 REMARK 500 SER F 51 -2.96 -144.15 REMARK 500 THR F 76 96.88 59.20 REMARK 500 ALA F 82 94.92 -65.63 REMARK 500 TRP F 90 28.55 -149.68 REMARK 500 ASN F 137 75.12 64.01 REMARK 500 GLN F 155 16.77 -147.10 REMARK 500 ASN F 156 44.14 -80.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OTS RELATED DB: PDB REMARK 900 RELATED ID: 2FEC RELATED DB: PDB REMARK 900 RELATED ID: 2FEE RELATED DB: PDB