REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.3, X-PLOR 3.1 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.5 REMARK 3 NUMBER OF REFLECTIONS : 47690 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) : 0.192 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.600 REMARK 3 FREE R VALUE TEST SET COUNT : 1919 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.69 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 43.60 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2175 REMARK 3 BIN R VALUE (WORKING SET) : 0.2960 REMARK 3 BIN FREE R VALUE : 0.3560 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.10 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 109 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13136 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 388 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 53.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 4.67400 REMARK 3 B22 (A**2) : 0.65700 REMARK 3 B33 (A**2) : -5.33100 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36 REMARK 3 ESD FROM SIGMAA (A) : 0.23 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.34 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.017 REMARK 3 BOND ANGLES (DEGREES) : 2.18 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.10 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) : 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 : COMBINATION REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 50.00 REMARK 3 REMARK 3 NCS MODEL : RESTRAINTS 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.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: EACH OF FAB DOMAINS VL, CL, VH AND REMARK 3 CH1 COORDINATES AND TEMPERATURE FACTORS RESTRAINED TO BE EQUAL REMARK 3 IN EACH OF FOUR MOLECULES WITH CNS NCS POSITIONAL RESTRAINTS = REMARK 3 300.00 KCAL/MOL-A**2 AND B FACTOR TARGET DEVIATION = 0.5A**2. REMARK 3 NO NCS RESTRAINTS APPLIED TO RESIDUES IN ELBOW REGION OF EACH REMARK 3 FAB. REMARK 4 REMARK 4 1BFO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : DEC-94 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SRS REMARK 200 BEAMLINE : PX9.5 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.900 REMARK 200 MONOCHROMATOR : MONOCHROMATOR REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47690 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.07700 REMARK 200 R SYM (I) : 0.07700 REMARK 200 FOR THE DATA SET : 5.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 78.6 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.33000 REMARK 200 R SYM FOR SHELL (I) : 0.33000 REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNS 0.3, X-PLOR 3.1 REMARK 200 STARTING MODEL: PARTIALLY REFINED CAMPATH-1H REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 36.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 47.14000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.33500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.07500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.33500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.14000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.07500 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, 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18970 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18990 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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 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 VAL F 216 O HOH F 260 1.99 REMARK 500 O VAL H 216 O HOH H 257 2.10 REMARK 500 O HIS E 197 N THR E 199 2.12 REMARK 500 O SER A 67 O HOH A 254 2.13 REMARK 500 O HOH F 217 O HOH F 250 2.14 REMARK 500 O HIS C 197 N THR C 199 2.14 REMARK 500 OD1 ASN A 160 NZ LYS H 3 2.15 REMARK 500 O ASN A 156 O HOH A 228 2.16 REMARK 500 O THR E 199 N SER E 201 2.17 REMARK 500 O HIS A 197 N THR A 199 2.17 REMARK 500 O THR C 199 N SER C 201 2.18 REMARK 500 O THR A 199 N SER A 201 2.18 REMARK 500 OE1 GLU A 105 OH TYR A 172 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 TRP B 194 CB TRP B 194 CG 0.136 REMARK 500 TRP D 194 CB TRP D 194 CG 0.125 REMARK 500 TRP F 194 CB TRP F 194 CG 0.139 REMARK 500 TRP H 194 CB TRP H 194 CG 0.140 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 SER B 192 N - CA - C ANGL. DEV. = -16.6 DEGREES REMARK 500 LEU D 185 CA - CB - CG ANGL. DEV. = 13.9 DEGREES REMARK 500 LEU F 185 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 LEU F 185 CB - CG - CD2 ANGL. DEV. = -12.0 DEGREES REMARK 500 LEU H 185 CA - CB - CG ANGL. DEV. = 14.7 DEGREES REMARK 500 LEU H 185 CB - CG - CD2 ANGL. DEV. = -11.3 DEGREES REMARK 500 SER H 192 N - CA - C ANGL. DEV. = -17.0 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 ASP A 30 -116.89 56.16 REMARK 500 ASN A 50 69.24 65.94 REMARK 500 THR A 51 -30.30 47.57 REMARK 500 ASN A 52 30.32 -151.10 REMARK 500 SER A 65 -166.05 -165.99 REMARK 500 ALA A 84 -172.28 179.59 REMARK 500 ALA A 126 4.59 -49.44 REMARK 500 ASN A 189 -45.63 -130.75 REMARK 500 LYS A 198 81.31 -49.02 REMARK 500 THR A 199 -132.88 147.50 REMARK 500 SER A 200 -48.00 13.62 REMARK 500 PRO A 203 8.28 -58.55 REMARK 500 VAL A 204 158.06 53.05 REMARK 500 GLU A 213 142.02 88.77 REMARK 500 VAL B 2 -76.43 -13.20 REMARK 500 ARG B 52 -173.05 -67.39 REMARK 500 ASP B 53 -167.15 -56.88 REMARK 500 LYS B 67 138.99 -21.94 REMARK 500 ASP B 75 56.82 -144.08 REMARK 500 ASN B 76 -25.85 -35.01 REMARK 500 THR B 104 -85.06 56.76 REMARK 500 ALA B 105 95.47 -61.44 REMARK 500 THR B 124 105.56 -56.37 REMARK 500 CYS B 136 89.12 -43.77 REMARK 500 THR B 139 -76.34 -36.07 REMARK 500 THR B 140 140.61 72.26 REMARK 500 SER B 169 -118.94 -47.59 REMARK 500 TRP B 194 -85.60 -44.83 REMARK 500 THR B 198 117.89 95.99 REMARK 500 ALA B 207 1.57 -52.58 REMARK 500 ASP C 30 -137.95 79.19 REMARK 500 ASN C 50 69.95 65.80 REMARK 500 THR C 51 -29.97 46.95 REMARK 500 ASN C 52 32.36 -151.63 REMARK 500 SER C 65 -164.29 -167.11 REMARK 500 SER C 67 144.60 -170.64 REMARK 500 ALA C 84 -171.47 -179.85 REMARK 500 ALA C 126 3.45 -52.88 REMARK 500 ASP C 169 10.31 -144.51 REMARK 500 ASN C 189 -45.02 -130.14 REMARK 500 LYS C 198 82.72 -48.08 REMARK 500 THR C 199 -134.10 146.97 REMARK 500 SER C 200 -45.81 14.07 REMARK 500 PRO C 203 8.89 -59.99 REMARK 500 VAL C 204 159.59 52.97 REMARK 500 ASN C 212 44.76 -72.16 REMARK 500 GLU C 213 96.51 52.01 REMARK 500 VAL D 2 -76.91 -12.12 REMARK 500 ASP D 53 -165.92 -52.75 REMARK 500 LYS D 67 136.92 -21.37 REMARK 500 ASP D 75 56.36 -140.70 REMARK 500 ASN D 76 -25.53 -33.97 REMARK 500 THR D 104 -84.79 57.96 REMARK 500 ALA D 105 94.74 -62.45 REMARK 500 PHE D 108 55.70 72.93 REMARK 500 SER D 121 -92.67 -79.70 REMARK 500 ALA D 122 146.71 19.95 REMARK 500 THR D 124 95.79 -55.22 REMARK 500 CYS D 136 84.43 -22.19 REMARK 500 THR D 140 154.68 59.72 REMARK 500 PHE D 154 138.44 -171.54 REMARK 500 SER D 169 -117.61 -48.80 REMARK 500 TRP D 194 -84.59 -44.38 REMARK 500 THR D 198 119.19 98.22 REMARK 500 ALA D 207 0.14 -54.11 REMARK 500 SER D 208 13.12 -145.31 REMARK 500 ASP E 30 -127.45 65.43 REMARK 500 ASN E 50 70.10 64.49 REMARK 500 THR E 51 -32.27 47.69 REMARK 500 ASN E 52 32.94 -150.19 REMARK 500 SER E 65 -162.94 -167.92 REMARK 500 ALA E 84 -172.99 177.35 REMARK 500 LYS E 107 137.75 -33.64 REMARK 500 ALA E 126 0.22 -52.57 REMARK 500 ALA E 130 111.20 -161.19 REMARK 500 LYS E 198 83.19 -46.21 REMARK 500 THR E 199 -134.44 147.12 REMARK 500 SER E 200 -45.40 13.53 REMARK 500 PRO E 203 7.72 -59.93 REMARK 500 VAL E 204 154.49 52.61 REMARK 500 ASN E 212 42.71 -73.93 REMARK 500 GLU E 213 87.83 52.88 REMARK 500 VAL F 2 -76.79 -11.14 REMARK 500 ARG F 52 -176.40 -67.10 REMARK 500 ASP F 53 -166.69 -55.29 REMARK 500 LYS F 67 137.74 -24.69 REMARK 500 ASP F 75 56.06 -143.82 REMARK 500 ASN F 76 -25.66 -34.44 REMARK 500 THR F 104 -85.55 57.69 REMARK 500 ALA F 105 92.71 -61.99 REMARK 500 PHE F 108 53.81 72.64 REMARK 500 ALA F 122 176.94 -57.22 REMARK 500 CYS F 136 67.48 16.73 REMARK 500 THR F 139 -72.60 1.24 REMARK 500 THR F 140 126.16 70.97 REMARK 500 SER F 169 -119.70 -51.05 REMARK 500 TRP F 194 -83.84 -47.16 REMARK 500 THR F 198 117.79 92.63 REMARK 500 ALA F 207 -1.36 -54.78 REMARK 500 SER F 208 10.77 -142.79 REMARK 500 ASP G 30 -119.89 56.15 REMARK 500 ASN G 50 70.09 64.09 REMARK 500 THR G 51 -30.60 48.67 REMARK 500 ASN G 52 31.06 -151.76 REMARK 500 SER G 65 -164.28 -165.20 REMARK 500 ALA G 84 -174.39 175.32 REMARK 500 ALA G 126 1.09 -49.98 REMARK 500 ALA G 130 115.62 -160.63 REMARK 500 LYS G 198 82.08 -47.41 REMARK 500 THR G 199 -132.71 147.68 REMARK 500 SER G 200 -48.02 12.24 REMARK 500 PRO G 203 6.97 -59.74 REMARK 500 VAL G 204 155.11 52.87 REMARK 500 GLU G 213 50.77 20.49 REMARK 500 VAL H 2 -76.96 -12.47 REMARK 500 ASP H 53 -167.80 -55.27 REMARK 500 LYS H 67 137.20 -22.39 REMARK 500 ASP H 75 57.97 -144.88 REMARK 500 ASN H 76 -25.97 -35.89 REMARK 500 ALA H 94 -178.91 -174.41 REMARK 500 THR H 104 -84.31 58.09 REMARK 500 ALA H 105 93.23 -61.98 REMARK 500 THR H 124 98.21 -59.29 REMARK 500 CYS H 136 83.98 -30.37 REMARK 500 THR H 140 134.37 63.11 REMARK 500 SER H 141 -167.07 -73.13 REMARK 500 SER H 169 -120.24 -48.65 REMARK 500 TRP H 194 -83.69 -46.19 REMARK 500 THR H 198 118.71 93.60 REMARK 500 ALA H 207 2.50 -55.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH E 229 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH H 233 DISTANCE = 5.34 ANGSTROMS REMARK 525 HOH H 241 DISTANCE = 5.76 ANGSTROMS REMARK 525 HOH D 243 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH G 244 DISTANCE = 6.22 ANGSTROMS REMARK 525 HOH H 247 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH G 261 DISTANCE = 5.76 ANGSTROMS REMARK 525 HOH H 269 DISTANCE = 5.34 ANGSTROMS