REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.10 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) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 56530 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) : 0.278 REMARK 3 R VALUE (WORKING SET) : 0.278 REMARK 3 FREE R VALUE : 0.280 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2834 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) : 3.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3859 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.16 REMARK 3 BIN R VALUE (WORKING SET) : 0.4220 REMARK 3 BIN FREE R VALUE SET COUNT : 217 REMARK 3 BIN FREE R VALUE : 0.4010 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 : 8 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) : 76.51 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.65000 REMARK 3 B22 (A**2) : 7.97000 REMARK 3 B33 (A**2) : -10.97000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -6.99000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.856 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.439 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13553 ; 0.010 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18456 ; 1.494 ; 1.962 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1743 ; 1.414 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 479 ;38.232 ;22.985 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2145 ;15.870 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 67 ;21.085 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2121 ; 0.094 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10087 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7367 ; 0.332 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9547 ; 0.342 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 590 ; 0.219 ; 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): 25 ; 0.293 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.258 ; 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 454 3 REMARK 3 1 B 18 B 454 3 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 TIGHT POSITIONAL 1 A (A): 1748 ; 0.060 ; 0.050 REMARK 3 LOOSE POSITIONAL 1 A (A): 1524 ; 0.210 ; 5.000 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 : 1.20 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 2H2P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAY-06. REMARK 100 THE RCSB ID CODE IS RCSB037854. 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 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61583 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.08700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8 REMARK 200 DATA REDUNDANCY IN SHELL : 3.20 REMARK 200 R MERGE FOR SHELL (I) : 0.65200 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 70.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM KSCN, PEG 300 38%, PH 7.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K 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 110.29050 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.78900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 110.29050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 60.78900 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 300 REMARK: THE COMPLEX IS A HOMODIMER OF CHAINS A AND B ALONG WITH REMARK 300 NONEQUIVALENT FAB FRAGMENTS 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 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 OE2 GLU A 457 NH2 ARG B 18 1.46 REMARK 500 NH1 ARG A 18 OE1 GLN B 456 1.62 REMARK 500 CE1 TYR C 107 NH1 ARG D 45 1.70 REMARK 500 CD2 LEU A 274 NH1 ARG A 451 1.71 REMARK 500 CD GLU A 457 NH2 ARG B 18 1.81 REMARK 500 O ASP B 171 ND1 HIS B 175 1.82 REMARK 500 CG GLU A 457 NH2 ARG B 18 1.89 REMARK 500 O LYS F 38 CG2 THR F 41 1.97 REMARK 500 O ASP A 171 CD2 HIS A 175 2.02 REMARK 500 O TYR D 185 NH1 ARG D 210 2.08 REMARK 500 CD1 ILE F 2 OG SER F 27 2.11 REMARK 500 CA GLU D 186 NH2 ARG D 210 2.14 REMARK 500 NH2 ARG D 154 OE2 GLU D 184 2.16 REMARK 500 ND2 ASN E 163 CD1 LEU E 167 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 CYS C 22 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 GLY D 16 N - CA - C ANGL. DEV. = -17.0 DEGREES REMARK 500 CYS E 148 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 CYS F 193 CA - CB - SG ANGL. DEV. = 7.1 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 ARG A 18 1.40 -58.23 REMARK 500 ASP A 29 71.19 49.19 REMARK 500 LYS A 30 54.90 -142.14 REMARK 500 TRP A 59 -37.01 -37.62 REMARK 500 ALA A 72 -17.37 -42.54 REMARK 500 TYR A 75 -70.48 -59.74 REMARK 500 PHE A 95 -75.20 -56.46 REMARK 500 LEU A 96 -31.68 -36.96 REMARK 500 LYS A 99 -70.60 -70.05 REMARK 500 ALA A 101 92.51 -164.86 REMARK 500 SER A 107 -70.92 -56.23 REMARK 500 VAL A 122 72.69 -108.11 REMARK 500 ARG A 126 -70.44 -107.08 REMARK 500 LEU A 128 -70.84 -48.24 REMARK 500 PHE A 132 -80.16 -57.85 REMARK 500 ILE A 165 -74.24 -35.94 REMARK 500 ARG A 167 133.85 58.94 REMARK 500 GLU A 172 -70.72 -69.23 REMARK 500 THR A 176 -78.07 -61.58 REMARK 500 ILE A 200 -71.95 -55.92 REMARK 500 ILE A 201 30.38 -63.05 REMARK 500 GLU A 202 -24.63 -151.62 REMARK 500 GLU A 203 -60.73 -134.32 REMARK 500 PRO A 206 107.26 -45.38 REMARK 500 VAL A 236 118.49 -160.01 REMARK 500 LEU A 244 -173.27 -69.69 REMARK 500 SER A 245 -167.58 -75.19 REMARK 500 ASP A 278 -73.57 -70.34 REMARK 500 ARG A 282 -74.48 -51.94 REMARK 500 VAL A 283 -47.08 -20.19 REMARK 500 PHE A 307 -61.08 -126.40 REMARK 500 ALA A 309 67.37 -159.00 REMARK 500 PRO A 310 -34.12 -30.97 REMARK 500 SER A 313 -158.07 -86.71 REMARK 500 ASN A 318 -39.97 -25.87 REMARK 500 MET A 332 -30.69 -39.54 REMARK 500 PHE A 335 -72.03 -54.18 REMARK 500 PHE A 337 -73.08 -60.87 REMARK 500 SER A 350 39.59 -81.28 REMARK 500 VAL A 376 -10.28 -48.35 REMARK 500 GLU A 377 -68.68 -100.39 REMARK 500 ALA A 386 -43.50 -29.30 REMARK 500 SER A 401 -73.21 -91.18 REMARK 500 ASN A 418 69.71 -110.28 REMARK 500 PRO A 443 103.51 -55.49 REMARK 500 ALA A 454 -73.48 -39.02 REMARK 500 LYS A 455 -31.24 -35.36 REMARK 500 GLU A 457 35.10 -88.95 REMARK 500 ALA A 458 -51.38 -126.93 REMARK 500 ARG B 19 -32.42 -36.62 REMARK 500 ASP B 29 72.09 47.48 REMARK 500 LYS B 30 54.08 -142.23 REMARK 500 TRP B 59 -36.06 -35.69 REMARK 500 PHE B 95 -76.33 -56.09 REMARK 500 LEU B 96 -29.47 -36.22 REMARK 500 LYS B 99 -71.32 -70.23 REMARK 500 ALA B 101 92.00 -166.29 REMARK 500 VAL B 122 72.09 -107.58 REMARK 500 ARG B 126 -70.10 -107.07 REMARK 500 LEU B 128 -71.76 -46.89 REMARK 500 PHE B 132 -80.59 -57.31 REMARK 500 ILE B 165 -75.59 -34.64 REMARK 500 ARG B 167 119.43 61.94 REMARK 500 GLU B 172 -72.59 -69.62 REMARK 500 THR B 176 -78.76 -59.77 REMARK 500 ILE B 200 -73.48 -53.72 REMARK 500 ILE B 201 28.62 -62.47 REMARK 500 GLU B 202 -26.44 -149.30 REMARK 500 GLU B 203 -61.86 -131.79 REMARK 500 PRO B 206 106.62 -45.79 REMARK 500 VAL B 236 118.71 -160.53 REMARK 500 SER B 245 -166.35 -72.67 REMARK 500 ASP B 278 -74.79 -69.43 REMARK 500 ARG B 282 -75.24 -50.25 REMARK 500 VAL B 283 -46.32 -20.02 REMARK 500 PHE B 307 -60.59 -127.30 REMARK 500 ALA B 309 64.83 -157.84 REMARK 500 PRO B 310 -32.04 -29.29 REMARK 500 SER B 313 -157.32 -86.18 REMARK 500 ASN B 318 -39.80 -25.97 REMARK 500 MET B 332 -30.04 -39.52 REMARK 500 PHE B 335 -72.59 -54.22 REMARK 500 PHE B 337 -72.16 -61.65 REMARK 500 LEU B 346 -71.75 -47.89 REMARK 500 SER B 350 41.78 -82.18 REMARK 500 VAL B 376 -10.53 -49.95 REMARK 500 GLU B 377 -72.25 -99.36 REMARK 500 SER B 401 -74.75 -89.32 REMARK 500 ASN B 418 71.09 -110.74 REMARK 500 PRO B 443 102.39 -55.25 REMARK 500 GLN B 456 6.04 -61.51 REMARK 500 SER C 30 -166.65 -79.29 REMARK 500 ARG C 31 -6.95 53.98 REMARK 500 PRO C 53 -91.27 -61.34 REMARK 500 VAL C 54 -14.47 -38.90 REMARK 500 LYS C 65 -30.42 -22.40 REMARK 500 ASP C 66 26.40 -163.44 REMARK 500 ASP C 109 -77.17 -50.44 REMARK 500 ALA C 138 105.73 -50.80 REMARK 500 SER C 142 -74.93 -34.38 REMARK 500 LEU C 146 -129.37 -124.18 REMARK 500 PHE C 154 139.51 -176.70 REMARK 500 PRO C 155 -159.91 -98.52 REMARK 500 SER C 166 34.39 -74.66 REMARK 500 LEU C 167 35.27 -149.49 REMARK 500 ALA C 180 57.20 34.39 REMARK 500 PRO C 197 -1.63 -59.51 REMARK 500 SER C 198 -84.13 -40.78 REMARK 500 GLU C 199 -125.15 -73.57 REMARK 500 LYS C 213 112.17 -163.99 REMARK 500 PRO C 220 169.73 -45.90 REMARK 500 SER D 7 -106.57 -87.30 REMARK 500 MET D 11 136.63 169.55 REMARK 500 ASP D 17 135.14 166.98 REMARK 500 SER D 27 164.57 168.55 REMARK 500 SER D 28 151.03 -46.33 REMARK 500 SER D 39 125.97 -38.96 REMARK 500 TRP D 46 -98.63 -85.77 REMARK 500 THR D 50 -47.06 67.72 REMARK 500 SER D 51 -39.62 -131.84 REMARK 500 SER D 55 107.69 -43.07 REMARK 500 THR D 76 94.89 69.90 REMARK 500 GLU D 78 -147.78 -91.21 REMARK 500 GLU D 80 28.28 -62.50 REMARK 500 ALA D 83 -139.31 -163.08 REMARK 500 TRP D 90 42.88 -158.22 REMARK 500 THR D 125 46.23 -88.03 REMARK 500 SER D 126 30.98 -179.82 REMARK 500 ASN D 137 108.41 47.53 REMARK 500 PRO D 140 -157.74 -66.40 REMARK 500 SER D 152 123.72 -4.50 REMARK 500 LEU D 159 64.08 -152.91 REMARK 500 GLN D 165 110.74 23.24 REMARK 500 SER D 167 23.72 -70.19 REMARK 500 LYS D 168 35.42 -159.50 REMARK 500 ASP D 169 -29.17 172.81 REMARK 500 GLU D 186 0.62 -55.65 REMARK 500 TYR D 191 83.89 -154.09 REMARK 500 CYS D 193 80.40 -157.08 REMARK 500 LYS D 198 -43.59 -16.04 REMARK 500 THR D 199 20.00 -74.00 REMARK 500 ILE D 204 78.07 -100.28 REMARK 500 LYS D 206 95.30 -176.16 REMARK 500 SER D 207 -164.26 -122.58 REMARK 500 TYR E 29 -36.71 -36.33 REMARK 500 PRO E 41 93.14 22.72 REMARK 500 ILE E 51 102.31 -175.89 REMARK 500 PRO E 53 -48.05 -23.43 REMARK 500 ILE E 58 79.97 -158.40 REMARK 500 PRO E 62 87.75 -47.09 REMARK 500 ASP E 66 19.69 165.79 REMARK 500 ASP E 73 75.33 -119.33 REMARK 500 ARG E 87 -169.95 -117.13 REMARK 500 ASP E 90 32.31 -99.74 REMARK 500 ALA E 92 -159.04 -151.54 REMARK 500 ALA E 122 -144.77 -37.52 REMARK 500 ALA E 138 100.92 -53.59 REMARK 500 ALA E 140 80.76 33.16 REMARK 500 LEU E 146 -156.97 -107.87 REMARK 500 ALA E 180 67.42 76.65 REMARK 500 VAL E 189 101.57 179.36 REMARK 500 GLU E 199 -157.58 -105.61 REMARK 500 SER E 211 58.49 36.98 REMARK 500 SER F 7 -113.78 -32.09 REMARK 500 TYR F 31 71.79 53.07 REMARK 500 SER F 39 128.53 -26.56 REMARK 500 TRP F 46 -60.18 -97.08 REMARK 500 THR F 50 -43.61 68.40 REMARK 500 SER F 51 44.02 -154.77 REMARK 500 THR F 54 -171.94 -64.15 REMARK 500 SER F 62 -150.60 -91.98 REMARK 500 SER F 64 -135.81 -152.63 REMARK 500 SER F 66 125.31 145.69 REMARK 500 THR F 76 74.45 65.03 REMARK 500 TRP F 90 2.69 40.53 REMARK 500 SER F 91 51.83 -104.71 REMARK 500 SER F 92 43.25 171.31 REMARK 500 HIS F 93 126.95 -17.70 REMARK 500 PRO F 112 175.55 -56.72 REMARK 500 CYS F 133 106.93 -163.54 REMARK 500 LEU F 135 66.29 -168.82 REMARK 500 ASN F 137 82.09 33.34 REMARK 500 PRO F 140 178.50 -57.37 REMARK 500 GLN F 155 -42.70 -132.47 REMARK 500 GLN F 165 153.14 -43.10 REMARK 500 SER F 170 23.18 88.65 REMARK 500 LYS F 182 -75.07 -38.53 REMARK 500 GLU F 184 -38.28 -32.06 REMARK 500 ASN F 189 -43.48 -136.52 REMARK 500 LYS F 198 -34.27 -21.63 REMARK 500 SER F 200 135.97 -171.40 REMARK 500 PRO F 203 110.61 -36.51 REMARK 500 ARG F 210 -18.72 -31.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 SEK A 466 REMARK 610 SEK B 466 REMARK 610 SEK A 467 REMARK 610 SEK B 467 REMARK 610 SEK A 468 REMARK 610 SEK B 468 REMARK 610 SEK A 469 REMARK 610 SEK B 469 REMARK 615 REMARK 615 ZERO OCCUPANCY ATOM REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 615 M RES C SSEQI REMARK 615 SEK A 467 REMARK 615 SEK B 467 REMARK 615 SEK A 468 REMARK 615 SEK B 468 REMARK 615 SEK A 469 REMARK 615 SEK B 469 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEK A 466 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEK B 466 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OTS RELATED DB: PDB REMARK 900 WILDTYPE CLC-EC1 REMARK 900 RELATED ID: 2H2S RELATED DB: PDB