REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 30321 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) : 0.237 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.286 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1495 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) : 3.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1882 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.38 REMARK 3 BIN R VALUE (WORKING SET) : 0.3070 REMARK 3 BIN FREE R VALUE SET COUNT : 96 REMARK 3 BIN FREE R VALUE : 0.3620 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 9411 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 6 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.99 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.40000 REMARK 3 B22 (A**2) : -0.50000 REMARK 3 B33 (A**2) : -6.90000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 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): 0.501 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.397 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.401 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.902 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.850 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9669 ; 0.006 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13174 ; 1.077 ; 1.952 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1201 ; 3.204 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 397 ;27.985 ;23.829 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1524 ;12.486 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;14.718 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1459 ; 0.074 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7333 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4096 ; 0.246 ; 0.300 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6596 ; 0.328 ; 0.500 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 509 ; 0.199 ; 0.500 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): 49 ; 0.198 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.426 ; 0.500 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): 6142 ; 0.647 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9802 ; 1.139 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4075 ; 0.336 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3372 ; 0.548 ; 3.000 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 : 7 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : L C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 1 L 105 2 REMARK 3 1 C 1 C 105 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 3 H 51 2 REMARK 3 1 B 3 B 51 2 REMARK 3 2 H 53 H 81 2 REMARK 3 2 B 53 B 81 2 REMARK 3 3 H 83 H 99 2 REMARK 3 3 B 83 B 99 2 REMARK 3 4 H 101 H 110 4 REMARK 3 4 B 101 B 110 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : S A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 S 385 S 500 2 REMARK 3 1 A 385 A 500 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : H B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 H 117 H 215 2 REMARK 3 1 B 117 B 215 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : L C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 110 L 187 2 REMARK 3 1 C 110 C 187 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : L C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 L 189 L 210 2 REMARK 3 1 C 189 C 210 2 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : S A REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 1 S 324 S 355 4 REMARK 3 1 A 324 A 355 4 REMARK 3 2 S 358 S 384 4 REMARK 3 2 A 358 A 384 4 REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH 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 3BGF COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-07. REMARK 100 THE RCSB ID CODE IS RCSB045488. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-NOV-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X12C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35508 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.13200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 69.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : 0.75100 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: PDB ENTRIES 2DDB, 1KEG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 14% PEG 20000, 10-15% REMARK 280 GLYCEROL, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 91.84400 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.68250 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 91.84400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.68250 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5250 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, L, 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 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 ASN S 318 REMARK 465 ILE S 319 REMARK 465 THR S 320 REMARK 465 ASN S 321 REMARK 465 LEU S 322 REMARK 465 GLU S 502 REMARK 465 LEU S 503 REMARK 465 LEU S 504 REMARK 465 ASN S 505 REMARK 465 ALA S 506 REMARK 465 PRO S 507 REMARK 465 ALA S 508 REMARK 465 THR S 509 REMARK 465 VAL S 510 REMARK 465 ASN A 318 REMARK 465 ILE A 319 REMARK 465 THR A 320 REMARK 465 ASN A 321 REMARK 465 LEU A 322 REMARK 465 TYR A 356 REMARK 465 ASN A 357 REMARK 465 LEU A 503 REMARK 465 LEU A 504 REMARK 465 ASN A 505 REMARK 465 ALA A 506 REMARK 465 PRO A 507 REMARK 465 ALA A 508 REMARK 465 THR A 509 REMARK 465 VAL A 510 REMARK 465 GLY H 131 REMARK 465 ASP H 132 REMARK 465 THR H 133 REMARK 465 THR H 134 REMARK 465 ARG C 188 REMARK 465 ASN C 212 REMARK 465 GLY B 131 REMARK 465 ASP B 132 REMARK 465 THR B 133 REMARK 465 THR B 134 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 CYS S 348 -164.96 169.33 REMARK 500 ASP S 351 110.72 -38.56 REMARK 500 ASN S 357 42.94 -103.00 REMARK 500 VAL S 369 -155.36 -123.95 REMARK 500 PHE S 387 171.75 172.88 REMARK 500 ASN S 409 -50.64 -125.10 REMARK 500 PRO S 450 127.21 -33.99 REMARK 500 PRO S 459 130.72 -39.60 REMARK 500 PRO S 470 37.73 -85.47 REMARK 500 PHE A 325 -34.64 -143.90 REMARK 500 ALA A 339 42.96 -109.25 REMARK 500 ASN A 347 65.20 62.18 REMARK 500 CYS A 348 -176.34 165.24 REMARK 500 ASN A 375 1.79 -60.93 REMARK 500 PHE A 387 176.20 173.46 REMARK 500 ARG A 395 -9.46 -56.77 REMARK 500 ASN A 409 -50.91 -125.29 REMARK 500 PRO A 450 126.81 -31.42 REMARK 500 PRO A 470 38.23 -80.24 REMARK 500 TYR L 32 54.81 -90.06 REMARK 500 ASP L 41 0.71 -60.31 REMARK 500 LEU L 47 -69.60 -103.34 REMARK 500 ALA L 51 -47.50 78.14 REMARK 500 SER L 52 -6.88 -140.26 REMARK 500 ALA L 84 -155.17 -153.19 REMARK 500 SER L 127 32.16 -96.24 REMARK 500 ASN L 138 79.86 36.90 REMARK 500 GLN L 156 -63.78 -101.17 REMARK 500 LYS L 169 -64.97 -96.17 REMARK 500 PRO L 204 151.21 -48.52 REMARK 500 GLN H 43 -166.92 -109.92 REMARK 500 LEU H 82C 103.95 -57.49 REMARK 500 SER H 87 109.48 -56.03 REMARK 500 ALA H 88 -169.02 -172.08 REMARK 500 ARG H 100B 46.05 -92.52 REMARK 500 LEU H 100D -7.42 79.01 REMARK 500 PRO H 126 171.64 -59.29 REMARK 500 VAL H 127 -134.58 -73.22 REMARK 500 PHE H 148 132.65 179.72 REMARK 500 PRO H 149 -159.61 -98.69 REMARK 500 SER H 158 19.37 56.98 REMARK 500 SER H 162 -33.58 -132.50 REMARK 500 ASP H 175 -11.63 72.64 REMARK 500 SER H 187 -12.44 -47.05 REMARK 500 TYR C 32 56.89 -90.16 REMARK 500 ASP C 41 -1.79 -57.50 REMARK 500 LEU C 47 -71.01 -102.09 REMARK 500 ALA C 51 -42.33 76.33 REMARK 500 SER C 52 -7.42 -141.30 REMARK 500 ALA C 84 -152.00 -153.57 REMARK 500 ASN C 138 79.71 38.27 REMARK 500 ASP C 143 106.73 -59.17 REMARK 500 GLN C 156 -67.50 -98.01 REMARK 500 LYS C 169 -69.06 -97.74 REMARK 500 PRO C 204 150.95 -46.61 REMARK 500 GLN B 43 -167.29 -111.68 REMARK 500 ALA B 88 -169.32 -167.21 REMARK 500 ARG B 100B 43.69 -97.15 REMARK 500 VAL B 127 -136.35 -73.48 REMARK 500 PHE B 148 134.73 -177.09 REMARK 500 PRO B 149 -158.51 -97.52 REMARK 500 SER B 158 19.37 56.65 REMARK 500 SER B 162 -33.96 -132.13 REMARK 500 ASP B 175 -9.43 74.25 REMARK 500 SER B 187 -14.53 -44.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2AJF RELATED DB: PDB REMARK 900 S RECEPTOR BINDING DOMAIN IN COMPLEX WITH RECEPTOR REMARK 900 RELATED ID: 2DD8 RELATED DB: PDB REMARK 900 S RECEPTOR BINDING DOMAIN IN COMPLEX WITH NEUTRALIZING REMARK 900 ANTIBODY REMARK 900 RELATED ID: 2GHW RELATED DB: PDB REMARK 900 S RECEPTOR BINDING DOMAIN IN COMPLEX WITH NEUTRALIZING REMARK 900 ANTIBODY REMARK 900 RELATED ID: 2GHV RELATED DB: PDB REMARK 900 S RECEPTOR BINDING DOMAIN