REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 3.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.8 REMARK 3 NUMBER OF REFLECTIONS : 16142 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) : 0.232 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.300 REMARK 3 FREE R VALUE TEST SET COUNT : 819 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 11546 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) : 13.51 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.03900 REMARK 3 B22 (A**2) : -4.31400 REMARK 3 B33 (A**2) : 9.35200 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 5.70400 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.45 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 10.00 REMARK 3 REMARK 3 NCS MODEL : NULL 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 : CNS_TOPPAR:PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NON-CRYSTALLOGRAPHIC SYMMETRY REMARK 3 RESTRAINTS HAVE BEEN USED FOR POSITIONAL REFINEMENT. GROUP B REMARK 3 FACTORS WERE REFINED (2 PER RESIDUE). REMARK 4 REMARK 4 3ETB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-08. REMARK 100 THE RCSB ID CODE IS RCSB049740. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-JUN-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : BLUE MAX-FLUX CONFOCAL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18357 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 2.600 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 0.28300 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 3ESU, 1ACC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000, 0.05 M TRIS-HCL, PH REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 149.86000 REMARK 290 SMTRY3 2 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 300 REMARK: ASYMMETRIC UNIT CONTAINS 4 BIOLOGICAL UNITS. 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, J 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, K 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, M 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 F -4 REMARK 465 ALA F -3 REMARK 465 ASP F -2 REMARK 465 TYR F -1 REMARK 465 GLY F 110 REMARK 465 GLY F 111 REMARK 465 GLY F 112 REMARK 465 SER F 113 REMARK 465 GLY F 114 REMARK 465 GLY F 115 REMARK 465 GLY F 116 REMARK 465 GLY F 117 REMARK 465 SER F 118 REMARK 465 GLY F 119 REMARK 465 GLY F 120 REMARK 465 GLY F 121 REMARK 465 GLY F 122 REMARK 465 SER F 123 REMARK 465 GLY F 124 REMARK 465 GLY F 125 REMARK 465 GLY F 126 REMARK 465 GLY F 127 REMARK 465 SER F 128 REMARK 465 GLU F 1001 REMARK 465 MET G -4 REMARK 465 ALA G -3 REMARK 465 ASP G -2 REMARK 465 TYR G -1 REMARK 465 GLY G 110 REMARK 465 GLY G 111 REMARK 465 GLY G 112 REMARK 465 SER G 113 REMARK 465 GLY G 114 REMARK 465 GLY G 115 REMARK 465 GLY G 116 REMARK 465 GLY G 117 REMARK 465 SER G 118 REMARK 465 GLY G 119 REMARK 465 GLY G 120 REMARK 465 GLY G 121 REMARK 465 GLY G 122 REMARK 465 SER G 123 REMARK 465 GLY G 124 REMARK 465 GLY G 125 REMARK 465 GLY G 126 REMARK 465 GLY G 127 REMARK 465 SER G 128 REMARK 465 MET H -4 REMARK 465 ALA H -3 REMARK 465 ASP H -2 REMARK 465 TYR H -1 REMARK 465 GLY H 110 REMARK 465 GLY H 111 REMARK 465 GLY H 112 REMARK 465 SER H 113 REMARK 465 GLY H 114 REMARK 465 GLY H 115 REMARK 465 GLY H 116 REMARK 465 GLY H 117 REMARK 465 SER H 118 REMARK 465 GLY H 119 REMARK 465 GLY H 120 REMARK 465 GLY H 121 REMARK 465 GLY H 122 REMARK 465 SER H 123 REMARK 465 GLY H 124 REMARK 465 GLY H 125 REMARK 465 GLY H 126 REMARK 465 GLY H 127 REMARK 465 SER H 128 REMARK 465 MET I -4 REMARK 465 ALA I -3 REMARK 465 ASP I -2 REMARK 465 TYR I -1 REMARK 465 GLY I 110 REMARK 465 GLY I 111 REMARK 465 GLY I 112 REMARK 465 SER I 113 REMARK 465 GLY I 114 REMARK 465 GLY I 115 REMARK 465 GLY I 116 REMARK 465 GLY I 117 REMARK 465 SER I 118 REMARK 465 GLY I 119 REMARK 465 GLY I 120 REMARK 465 GLY I 121 REMARK 465 GLY I 122 REMARK 465 SER I 123 REMARK 465 GLY I 124 REMARK 465 GLY I 125 REMARK 465 GLY I 126 REMARK 465 GLY I 127 REMARK 465 SER I 128 REMARK 465 GLU I 1001 REMARK 465 ARG L 592 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN F 3 CG CD OE1 NE2 REMARK 470 LYS F 107 CG CD CE NZ REMARK 470 ARG F 108 CG CD NE CZ NH1 NH2 REMARK 470 GLY F 109 CA C O REMARK 470 VAL F1002 CG1 CG2 REMARK 470 SER F1113 OG REMARK 470 LYS G 0 CG CD CE NZ REMARK 470 GLN G 3 CG CD OE1 NE2 REMARK 470 LYS G 107 CG CD CE NZ REMARK 470 ARG G 108 CG CD NE CZ NH1 NH2 REMARK 470 GLY G 109 CA C O REMARK 470 GLU G1001 CG CD OE1 OE2 REMARK 470 VAL G1002 CG1 CG2 REMARK 470 SER G1113 OG REMARK 470 LYS H 0 CG CD CE NZ REMARK 470 LYS H 107 CG CD CE NZ REMARK 470 ARG H 108 CG CD NE CZ NH1 NH2 REMARK 470 GLY H 109 CA C O REMARK 470 GLU H1001 CG CD OE1 OE2 REMARK 470 VAL H1002 CG1 CG2 REMARK 470 GLN H1003 CG CD OE1 NE2 REMARK 470 SER H1113 OG REMARK 470 LYS I 0 CG CD CE NZ REMARK 470 GLN I 3 CG CD OE1 NE2 REMARK 470 ARG I 108 CG CD NE CZ NH1 NH2 REMARK 470 GLY I 109 CA C O REMARK 470 VAL I1002 CG1 CG2 REMARK 470 SER I1113 OG REMARK 470 ARG J 592 CG CD NE CZ NH1 NH2 REMARK 470 LYS J 594 CG CD CE NZ REMARK 470 ARG J 595 CG CD NE CZ NH1 NH2 REMARK 470 ARG K 592 CG CD NE CZ NH1 NH2 REMARK 470 LYS K 594 CG CD CE NZ REMARK 470 ARG K 595 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 593 CG OD1 OD2 REMARK 470 LYS L 594 CG CD CE NZ REMARK 470 ARG L 595 CG CD NE CZ NH1 NH2 REMARK 470 ARG M 592 CG CD NE CZ NH1 NH2 REMARK 470 LYS M 594 CG CD CE NZ REMARK 470 ARG M 595 CG CD NE CZ NH1 NH2 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 GLN F 6 77.90 -117.14 REMARK 500 SER F 14 170.57 -52.41 REMARK 500 ARG F 24 99.00 -170.12 REMARK 500 GLN F 27 124.86 171.83 REMARK 500 ASP F 28 112.53 -22.66 REMARK 500 ASN F 31 -23.14 75.96 REMARK 500 TYR F 32 74.41 -64.89 REMARK 500 LYS F 39 174.97 -50.37 REMARK 500 LEU F 47 -61.79 -104.91 REMARK 500 THR F 51 -58.41 74.81 REMARK 500 SER F 60 -18.38 -37.12 REMARK 500 SER F 63 134.97 166.72 REMARK 500 SER F 67 144.41 174.39 REMARK 500 ASN F 77 81.71 25.18 REMARK 500 LEU F 78 160.19 -45.64 REMARK 500 GLN F 80 -38.94 -32.62 REMARK 500 GLU F 81 30.60 -86.09 REMARK 500 GLU F 105 -139.55 -114.12 REMARK 500 SER F1007 -161.03 -79.76 REMARK 500 PRO F1014 96.50 -38.42 REMARK 500 PHE F1029 -67.18 -102.21 REMARK 500 TRP F1033 -160.30 -55.89 REMARK 500 MET F1034 98.80 -170.28 REMARK 500 GLN F1043 58.92 -109.50 REMARK 500 ASP F1054 -31.64 -149.66 REMARK 500 LYS F1066 -65.16 -169.33 REMARK 500 SER F1076 77.86 34.89 REMARK 500 LEU F1082 99.05 -53.39 REMARK 500 SER F1082B 81.15 54.89 REMARK 500 SER F1087 97.90 -49.34 REMARK 500 LEU F1097 87.87 62.91 REMARK 500 LEU F1098 87.95 121.35 REMARK 500 THR F1107 76.43 -160.04 REMARK 500 SER F1108 97.31 -41.47 REMARK 500 VAL F1109 71.54 -100.32 REMARK 500 SER F1112 -169.42 -67.03 REMARK 500 GLN G 6 76.87 -117.10 REMARK 500 SER G 14 170.35 -52.75 REMARK 500 ARG G 24 99.40 -171.88 REMARK 500 GLN G 27 125.04 171.26 REMARK 500 ASP G 28 112.78 -23.03 REMARK 500 ASN G 31 -21.61 74.96 REMARK 500 TYR G 32 74.65 -66.44 REMARK 500 LYS G 39 174.12 -50.54 REMARK 500 LEU G 47 -62.47 -104.23 REMARK 500 THR G 51 -59.11 74.93 REMARK 500 SER G 60 -19.17 -36.50 REMARK 500 SER G 63 133.55 166.18 REMARK 500 SER G 67 145.84 174.35 REMARK 500 ASN G 77 80.62 25.71 REMARK 500 LEU G 78 159.98 -44.31 REMARK 500 GLN G 80 -39.46 -31.94 REMARK 500 GLU G 105 -139.67 -113.58 REMARK 500 ILE G 106 88.88 -158.58 REMARK 500 LYS G 107 130.41 -39.98 REMARK 500 ARG G 108 -178.05 -60.27 REMARK 500 VAL G1002 -29.68 175.80 REMARK 500 GLN G1003 -95.14 44.97 REMARK 500 SER G1007 -160.25 -77.55 REMARK 500 PRO G1014 94.45 -40.68 REMARK 500 PHE G1029 -63.07 -100.27 REMARK 500 TRP G1033 -163.79 -56.79 REMARK 500 MET G1034 97.64 -165.24 REMARK 500 GLN G1043 59.69 -109.99 REMARK 500 ASP G1054 -31.43 -146.37 REMARK 500 LYS G1066 -64.19 -164.34 REMARK 500 SER G1076 76.25 33.49 REMARK 500 LEU G1082 92.32 -51.89 REMARK 500 SER G1082B 78.24 55.67 REMARK 500 SER G1087 96.03 -47.82 REMARK 500 LEU G1097 87.09 64.60 REMARK 500 LEU G1098 89.87 121.63 REMARK 500 THR G1107 77.91 -152.21 REMARK 500 SER G1108 97.78 -40.21 REMARK 500 VAL G1109 73.77 -101.15 REMARK 500 SER G1112 -169.57 -64.86 REMARK 500 GLN H 6 76.30 -116.56 REMARK 500 SER H 14 170.45 -52.82 REMARK 500 ARG H 24 98.85 -172.42 REMARK 500 GLN H 27 125.25 171.94 REMARK 500 ASP H 28 111.27 -22.95 REMARK 500 ASN H 31 -23.30 75.87 REMARK 500 TYR H 32 75.10 -65.52 REMARK 500 LYS H 39 173.64 -49.73 REMARK 500 ASP H 41 49.55 -70.81 REMARK 500 LEU H 47 -62.25 -104.95 REMARK 500 THR H 51 -58.78 74.50 REMARK 500 SER H 60 -19.34 -35.74 REMARK 500 SER H 63 133.35 165.82 REMARK 500 SER H 67 145.51 174.11 REMARK 500 ASN H 77 81.56 26.04 REMARK 500 LEU H 78 160.16 -45.28 REMARK 500 GLN H 80 -38.82 -31.86 REMARK 500 GLU H 81 31.12 -86.93 REMARK 500 ASN H 92 -61.00 -90.04 REMARK 500 GLU H 105 -138.60 -114.06 REMARK 500 LYS H 107 147.80 -32.00 REMARK 500 VAL H1002 -41.07 136.20 REMARK 500 GLN H1003 -76.81 35.60 REMARK 500 SER H1007 -159.64 -78.43 REMARK 500 PRO H1014 99.94 -36.44 REMARK 500 PHE H1029 -63.83 -102.72 REMARK 500 TRP H1033 -162.70 -54.69 REMARK 500 MET H1034 97.62 -168.61 REMARK 500 GLN H1043 61.57 -106.98 REMARK 500 ASP H1054 -32.30 -146.54 REMARK 500 LYS H1066 -64.04 -161.14 REMARK 500 SER H1076 75.43 37.01 REMARK 500 LEU H1082 95.59 -54.33 REMARK 500 SER H1082B 77.32 59.53 REMARK 500 SER H1084 -5.68 -59.26 REMARK 500 SER H1087 97.82 -48.51 REMARK 500 LEU H1097 88.45 66.24 REMARK 500 LEU H1098 89.82 119.28 REMARK 500 THR H1107 75.28 -159.30 REMARK 500 SER H1108 98.01 -37.82 REMARK 500 VAL H1109 77.12 -101.13 REMARK 500 SER H1112 -171.10 -69.00 REMARK 500 GLN I 6 76.95 -117.32 REMARK 500 SER I 14 170.65 -52.30 REMARK 500 ARG I 24 100.28 -170.17 REMARK 500 GLN I 27 125.17 172.39 REMARK 500 ASP I 28 113.00 -22.59 REMARK 500 ASN I 31 -22.57 74.51 REMARK 500 TYR I 32 75.01 -65.51 REMARK 500 LYS I 39 173.92 -49.66 REMARK 500 LEU I 47 -63.69 -103.39 REMARK 500 THR I 51 -58.72 75.90 REMARK 500 SER I 60 -18.17 -37.68 REMARK 500 SER I 63 133.31 165.67 REMARK 500 SER I 67 144.69 174.15 REMARK 500 ASN I 77 81.55 24.30 REMARK 500 LEU I 78 160.41 -44.93 REMARK 500 GLN I 80 -39.42 -32.58 REMARK 500 GLU I 81 30.48 -85.66 REMARK 500 ASN I 92 -60.15 -90.30 REMARK 500 GLU I 105 -139.62 -113.67 REMARK 500 ARG I 108 153.47 -28.39 REMARK 500 GLN I1003 -93.64 33.34 REMARK 500 SER I1007 -159.76 -78.04 REMARK 500 PRO I1014 96.39 -39.13 REMARK 500 PHE I1029 -66.46 -100.89 REMARK 500 ASN I1030 9.05 -69.05 REMARK 500 TRP I1033 -162.09 -54.58 REMARK 500 MET I1034 99.29 -166.44 REMARK 500 GLN I1043 59.08 -112.56 REMARK 500 ASP I1054 -29.65 -146.45 REMARK 500 LYS I1066 -64.30 -162.05 REMARK 500 SER I1076 73.89 36.20 REMARK 500 LEU I1082 95.63 -56.06 REMARK 500 SER I1082B 81.77 57.76 REMARK 500 SER I1087 95.13 -50.07 REMARK 500 LEU I1097 87.94 65.14 REMARK 500 LEU I1098 89.81 121.37 REMARK 500 THR I1107 76.08 -159.34 REMARK 500 SER I1108 95.48 -40.30 REMARK 500 SER I1112 -168.53 -65.57 REMARK 500 LYS J 594 -14.55 71.22 REMARK 500 TYR J 598 -143.05 -73.18 REMARK 500 ASP J 599 -146.01 174.35 REMARK 500 ASN J 601 -0.41 63.56 REMARK 500 ILE J 603 -143.43 -95.14 REMARK 500 ALA J 607 -164.87 -105.43 REMARK 500 SER J 610 -17.19 -46.74 REMARK 500 ASN J 621 137.52 -178.77 REMARK 500 THR J 624 12.07 -69.59 REMARK 500 LEU J 627 -159.08 -78.78 REMARK 500 LEU J 628 17.04 177.19 REMARK 500 LEU J 629 178.89 -49.74 REMARK 500 ARG J 636 -27.21 -35.26 REMARK 500 GLU J 650 -71.67 -56.05 REMARK 500 ASN J 657 48.84 -87.66 REMARK 500 ASP J 658 78.01 -60.62 REMARK 500 SER J 667 123.88 179.61 REMARK 500 ARG J 669 -157.93 -100.00 REMARK 500 ASN J 682 44.64 -100.69 REMARK 500 LYS J 684 9.49 58.58 REMARK 500 ASN J 691 112.40 178.76 REMARK 500 PRO J 692 -33.81 -34.60 REMARK 500 PRO J 710 -132.87 -60.54 REMARK 500 SER J 711 -149.44 -158.31 REMARK 500 GLU J 712 31.39 -98.20 REMARK 500 ASN J 713 -0.21 -144.06 REMARK 500 ILE J 721 106.86 -31.87 REMARK 500 LYS J 722 97.01 -66.53 REMARK 500 SER J 728 82.33 -166.11 REMARK 500 LYS J 730 -172.45 -52.75 REMARK 500 ILE J 734 -81.24 -79.33 REMARK 500 ASP K 593 104.76 164.93 REMARK 500 ARG K 600 -65.88 -20.15 REMARK 500 ASN K 601 34.18 -68.61 REMARK 500 ASN K 602 -8.89 58.25 REMARK 500 ALA K 607 -167.54 -104.38 REMARK 500 SER K 610 -15.23 -49.30 REMARK 500 ASN K 621 136.14 -178.16 REMARK 500 THR K 624 11.70 -66.33 REMARK 500 LEU K 627 -156.42 -70.18 REMARK 500 LEU K 628 15.97 175.46 REMARK 500 LEU K 629 179.17 -49.48 REMARK 500 ARG K 636 -27.56 -34.48 REMARK 500 ASN K 657 49.00 -90.66 REMARK 500 ASP K 658 80.02 -60.10 REMARK 500 SER K 667 115.96 178.87 REMARK 500 ARG K 669 -156.79 -100.52 REMARK 500 ASN K 682 41.71 -105.63 REMARK 500 LYS K 684 12.96 54.09 REMARK 500 ASN K 691 112.90 175.79 REMARK 500 PRO K 692 -36.05 -35.22 REMARK 500 PRO K 710 -133.18 -62.35 REMARK 500 SER K 711 -147.06 -153.41 REMARK 500 ILE K 721 102.31 -30.42 REMARK 500 LYS K 722 98.82 -63.13 REMARK 500 SER K 728 82.77 -164.94 REMARK 500 LYS K 730 177.92 -59.45 REMARK 500 ILE K 734 -85.05 -76.90 REMARK 500 ASN L 601 21.43 -61.93 REMARK 500 ASN L 602 64.24 32.15 REMARK 500 ALA L 607 -163.22 -104.56 REMARK 500 ASN L 621 135.04 -174.63 REMARK 500 LEU L 627 -160.77 -78.30 REMARK 500 LEU L 628 16.61 179.98 REMARK 500 LEU L 629 177.42 -49.00 REMARK 500 ARG L 636 -27.83 -33.11 REMARK 500 ASN L 657 42.51 -87.51 REMARK 500 ASP L 658 76.43 -54.88 REMARK 500 SER L 667 123.43 -176.04 REMARK 500 ASN L 682 43.41 -104.89 REMARK 500 LYS L 684 6.55 59.12 REMARK 500 ASN L 691 111.52 178.26 REMARK 500 PRO L 692 -32.89 -35.01 REMARK 500 PRO L 710 -136.38 -56.44 REMARK 500 SER L 711 -147.70 -153.95 REMARK 500 ILE L 721 104.75 -35.99 REMARK 500 LYS L 722 95.08 -64.42 REMARK 500 SER L 728 82.49 -164.06 REMARK 500 LYS L 730 -176.99 -55.84 REMARK 500 ILE L 734 -78.65 -83.48 REMARK 500 ASP M 593 -78.67 -147.47 REMARK 500 LYS M 594 4.16 -67.16 REMARK 500 ASN M 602 16.54 89.00 REMARK 500 VAL M 605 -2.00 -151.17 REMARK 500 ALA M 607 -169.08 -106.57 REMARK 500 SER M 610 -17.45 -48.80 REMARK 500 ASN M 621 136.46 -178.00 REMARK 500 LEU M 627 -159.20 -73.07 REMARK 500 LEU M 628 16.44 177.29 REMARK 500 LEU M 629 -179.28 -48.74 REMARK 500 ARG M 636 -27.15 -38.41 REMARK 500 GLU M 650 -74.13 -52.50 REMARK 500 ASN M 657 47.31 -89.53 REMARK 500 ASP M 658 80.18 -58.55 REMARK 500 SER M 667 118.73 179.57 REMARK 500 ARG M 669 -157.84 -100.34 REMARK 500 ASN M 682 46.08 -104.46 REMARK 500 LYS M 684 8.28 59.01 REMARK 500 ASN M 691 110.68 177.30 REMARK 500 PRO M 692 -37.01 -32.13 REMARK 500 PRO M 710 -134.81 -63.96 REMARK 500 SER M 711 -146.65 -152.71 REMARK 500 ILE M 721 103.19 -35.86 REMARK 500 ILE M 726 -17.45 -141.27 REMARK 500 SER M 728 79.29 -162.88 REMARK 500 LYS M 730 -178.46 -55.85 REMARK 500 ILE M 734 -79.52 -80.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ESU RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ANTHRAX-NEUTRALIZING SINGLE-CHAIN REMARK 900 ANTIBODY 14B7 REMARK 900 RELATED ID: 3ESV RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ENGINEERED NEUTRALIZING ANTIBODY REMARK 900 M18 REMARK 900 RELATED ID: 3ET9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ENGINEERED NEUTRALIZING ANTIBODY 1H REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUE NUMBERS FOR ANTIBODY M18 HEAVY CHAIN FRAGMENT REMARK 999 HAVE OFFSET 1000 TO DISTINGUISH THEM FROM THE ANTIBODY REMARK 999 M18 LIGHT CHAIN FRAGMENT WHICH HAS ORIGINAL RESIDUE REMARK 999 NUMBERING.