REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH H.L.MONACO,M.RIZZI,A.CODA REMARK 1 TITL STRUCTURE OF A COMPLEX OF TWO PLASMA PROTEINS: REMARK 1 TITL 2 TRANSTHYRETIN AND RETINOL-BINDING PROTEIN. REMARK 1 REF SCIENCE V. 268 1039 1995 REMARK 1 REFN ISSN 0036-8075 REMARK 1 PMID 7754382 REMARK 1 REFERENCE 2 REMARK 1 AUTH H.M.NAYLOR,M.E.NEWCOMER REMARK 1 TITL THE STRUCTURE OF HUMAN RETINOL-BINDING PROTEIN REMARK 1 TITL 2 (RBP) WITH ITS CARRIER PROTEIN TRANSTHYRETIN REMARK 1 TITL 3 REVEALS AN INTERACTION WITH THE CARBOXY TERMINUS REMARK 1 TITL 4 OF RBP. REMARK 1 REF BIOCHEMISTRY V. 38 2647 1999 REMARK 1 REFN ISSN 0006-2960 REMARK 1 PMID 10052934 REMARK 1 DOI 10.1021/BI982291I REMARK 1 REFERENCE 3 REMARK 1 AUTH G.MALPELI,G.ZANOTTI,F.GLIUBICH,A.RIZZOTTO, REMARK 1 AUTH 2 S.K.NISHIDA,C.FOLLI,R.BERNI REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DATA FOR THE REMARK 1 TITL 2 HUMAN TRANSTHYRETIN-RETINOL-BINDING PROTEIN (RBP) REMARK 1 TITL 3 COMPLEX BOUND TO AN ANTI-RBP FAB. REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 276 1999 REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 10089423 REMARK 1 DOI 10.1107/S0907444998007860 REMARK 2 REMARK 2 RESOLUTION. 3.38 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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 : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.38 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.72 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 8281753.410 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 78.8 REMARK 3 NUMBER OF REFLECTIONS : 24044 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) : 0.239 REMARK 3 FREE R VALUE : 0.312 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1190 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.36 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.57 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.80 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2760 REMARK 3 BIN R VALUE (WORKING SET) : 0.3130 REMARK 3 BIN FREE R VALUE : 0.3570 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.80 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 108 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 13052 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 42 REMARK 3 SOLVENT ATOMS : 334 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -16.97000 REMARK 3 B22 (A**2) : 8.37000 REMARK 3 B33 (A**2) : 8.59000 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) : 0.44 REMARK 3 ESD FROM SIGMAA (A) : 0.62 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) : 0.55 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.78 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.50 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.90 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.03 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 : FLAT MODEL REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 48.98 REMARK 3 REMARK 3 NCS MODEL : CONSTR 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 : PARAM19X_RET.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : PARAM19X_RET.TOP REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3BSZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JAN-08. REMARK 100 THE RCSB ID CODE IS RCSB045930. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-OCT-97 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 5.2R REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.3 REMARK 200 MONOCHROMATOR : SI (111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 180 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25746 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.360 REMARK 200 RESOLUTION RANGE LOW (A) : 55.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.4 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.36 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.51 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.7 REMARK 200 DATA REDUNDANCY IN SHELL : 2.60 REMARK 200 R MERGE FOR SHELL (I) : 0.34000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 1RBP, 1F41 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.04 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.35M AMMONIUM PHOSPHATE, 10MM REMARK 280 SODIUM CITRATE, 10MM BETA-MERCAPTOETHANOL, PH 5.0, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 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,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y+1/2,-Z REMARK 290 8555 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 79.81000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 111.59000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 79.81000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 111.59000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 79.81000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 111.59000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 79.81000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 111.59000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: N 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 GLY A 1 REMARK 465 PRO A 2 REMARK 465 THR A 3 REMARK 465 GLY A 4 REMARK 465 THR A 5 REMARK 465 GLY A 6 REMARK 465 LYS A 126 REMARK 465 GLU A 127 REMARK 465 GLY B 1 REMARK 465 PRO B 2 REMARK 465 THR B 3 REMARK 465 GLY B 4 REMARK 465 THR B 5 REMARK 465 GLY B 6 REMARK 465 LYS B 126 REMARK 465 GLU B 127 REMARK 465 GLY C 1 REMARK 465 PRO C 2 REMARK 465 THR C 3 REMARK 465 GLY C 4 REMARK 465 THR C 5 REMARK 465 GLY C 6 REMARK 465 LYS C 126 REMARK 465 GLU C 127 REMARK 465 GLY D 1 REMARK 465 PRO D 2 REMARK 465 THR D 3 REMARK 465 GLY D 4 REMARK 465 THR D 5 REMARK 465 GLY D 6 REMARK 465 LYS D 126 REMARK 465 GLU D 127 REMARK 465 ASP E 175 REMARK 465 GLY E 176 REMARK 465 ASP F 175 REMARK 465 GLY F 176 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 SER L 181 O HOH L 236 2.08 REMARK 500 O GLY L 133 O HOH L 222 2.10 REMARK 500 O PRO F 146 O HOH F 194 2.12 REMARK 500 O MET N 34 O HOH N 228 2.12 REMARK 500 O SER M 166 O HOH M 262 2.12 REMARK 500 O SER E 132 O HOH E 190 2.12 REMARK 500 O CYS D 10 O HOH D 139 2.14 REMARK 500 O GLY A 83 O ASN F 66 2.14 REMARK 500 O LEU M 183 O HOH M 236 2.16 REMARK 500 O ALA D 36 O HOH D 130 2.18 REMARK 500 O THR N 181 O HOH N 256 2.19 REMARK 500 OG1 THR D 60 O HOH D 153 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 SER A 8 -152.21 -168.25 REMARK 500 ASP A 38 0.18 -170.11 REMARK 500 ASP A 39 4.69 82.61 REMARK 500 PRO A 43 109.89 -51.35 REMARK 500 ALA A 45 149.45 171.71 REMARK 500 THR A 59 -157.10 -143.99 REMARK 500 ASP A 74 79.33 -69.50 REMARK 500 TYR A 78 -76.40 -78.94 REMARK 500 ASN A 98 56.58 26.70 REMARK 500 SER A 115 143.66 179.74 REMARK 500 SER B 8 -124.46 64.27 REMARK 500 ASP B 38 -75.00 -80.18 REMARK 500 ASP B 39 6.93 171.08 REMARK 500 LEU B 58 -83.75 -60.81 REMARK 500 GLU B 61 21.87 -75.59 REMARK 500 GLU B 62 -30.56 -154.72 REMARK 500 PHE B 64 66.38 -69.44 REMARK 500 VAL B 65 -157.37 -55.73 REMARK 500 LYS B 76 -76.68 -59.86 REMARK 500 TYR B 78 -70.83 -52.08 REMARK 500 LEU B 82 38.74 -86.70 REMARK 500 HIS B 90 163.14 162.44 REMARK 500 ASN B 98 30.80 33.35 REMARK 500 THR B 123 -162.89 -128.16 REMARK 500 ASN B 124 -67.60 -135.39 REMARK 500 SER C 8 -150.66 -169.96 REMARK 500 ASN C 27 11.54 82.25 REMARK 500 ASP C 38 1.72 -172.89 REMARK 500 ASP C 39 6.81 80.30 REMARK 500 PRO C 43 109.57 -51.21 REMARK 500 ALA C 45 149.23 171.85 REMARK 500 THR C 59 -157.38 -143.77 REMARK 500 TYR C 78 -77.87 -79.81 REMARK 500 ASN C 98 58.01 25.09 REMARK 500 SER C 115 146.44 177.36 REMARK 500 SER D 8 -120.70 62.56 REMARK 500 ASP D 38 -73.36 -80.38 REMARK 500 ASP D 39 5.68 170.94 REMARK 500 LEU D 58 -84.77 -59.76 REMARK 500 GLU D 61 24.30 -75.53 REMARK 500 GLU D 62 -34.08 -154.19 REMARK 500 PHE D 64 67.06 -67.85 REMARK 500 VAL D 65 -157.60 -54.40 REMARK 500 LYS D 76 -74.18 -64.02 REMARK 500 LEU D 82 39.79 -87.99 REMARK 500 HIS D 90 164.58 163.12 REMARK 500 ASN D 98 30.34 32.37 REMARK 500 THR D 123 -164.15 -129.85 REMARK 500 ASN D 124 -64.64 -135.05 REMARK 500 ARG E 2 -110.08 -67.73 REMARK 500 ASP E 3 -174.00 84.65 REMARK 500 CYS E 4 51.71 86.59 REMARK 500 PHE E 9 136.15 -37.99 REMARK 500 ASN E 14 64.52 62.02 REMARK 500 ALA E 18 -75.76 -59.16 REMARK 500 SER E 21 157.23 -42.75 REMARK 500 GLN E 38 -95.41 -80.30 REMARK 500 SER E 46 110.31 -176.57 REMARK 500 ARG E 62 47.71 -84.79 REMARK 500 LEU E 64 -79.67 72.71 REMARK 500 ASN E 65 138.54 158.93 REMARK 500 ASN E 66 -6.14 63.02 REMARK 500 GLU E 81 23.42 -57.65 REMARK 500 TRP E 91 178.04 169.77 REMARK 500 GLN E 98 122.54 -28.54 REMARK 500 HIS E 104 106.48 -162.59 REMARK 500 THR E 109 170.42 177.40 REMARK 500 TYR E 111 -45.80 69.54 REMARK 500 LEU E 125 -59.22 -24.95 REMARK 500 ALA E 130 -79.09 -85.87 REMARK 500 LEU E 144 130.48 -174.17 REMARK 500 GLN E 154 -76.41 -40.04 REMARK 500 ARG E 155 -57.58 -29.77 REMARK 500 ARG E 163 -44.08 70.92 REMARK 500 GLN E 164 16.43 -57.00 REMARK 500 TYR E 173 -39.67 -34.04 REMARK 500 ARG F 2 -110.38 -66.87 REMARK 500 ASP F 3 -174.07 84.90 REMARK 500 CYS F 4 51.98 86.68 REMARK 500 PHE F 9 136.14 -36.88 REMARK 500 ALA F 18 -80.17 -56.85 REMARK 500 SER F 21 154.50 -39.23 REMARK 500 GLN F 38 -93.02 -83.71 REMARK 500 SER F 46 109.16 -173.28 REMARK 500 ARG F 62 46.51 -85.74 REMARK 500 LEU F 64 -76.94 71.57 REMARK 500 ASN F 65 137.46 153.69 REMARK 500 ASN F 66 -5.41 64.30 REMARK 500 GLU F 81 22.16 -55.69 REMARK 500 TRP F 91 176.12 168.97 REMARK 500 GLN F 98 121.43 -27.98 REMARK 500 HIS F 104 104.93 -163.32 REMARK 500 THR F 109 170.89 177.37 REMARK 500 TYR F 111 -48.98 68.14 REMARK 500 LEU F 125 -56.24 -26.18 REMARK 500 ALA F 130 -78.30 -83.46 REMARK 500 LEU F 144 134.62 -175.24 REMARK 500 GLN F 154 -75.91 -41.08 REMARK 500 ARG F 155 -57.86 -29.95 REMARK 500 ALA F 162 143.14 -39.32 REMARK 500 ARG F 163 -46.23 73.47 REMARK 500 GLN F 164 14.47 -53.18 REMARK 500 TYR F 173 -39.55 -32.06 REMARK 500 SER L 7 -88.40 -35.47 REMARK 500 CYS L 23 93.47 -175.06 REMARK 500 TYR L 32 16.33 30.22 REMARK 500 ASN L 34 -155.52 -136.57 REMARK 500 ARG L 54 62.38 69.17 REMARK 500 ALA L 55 50.87 15.21 REMARK 500 SER L 56 -38.70 172.26 REMARK 500 SER L 67 134.54 173.33 REMARK 500 SER L 71 174.73 163.88 REMARK 500 ARG L 72 -104.88 47.23 REMARK 500 ASN L 80 127.06 -171.93 REMARK 500 ALA L 88 -166.04 -167.07 REMARK 500 SER L 95 45.29 -145.10 REMARK 500 ASP L 114 156.50 -44.75 REMARK 500 PRO L 124 120.84 -36.08 REMARK 500 SER L 125 -172.75 -59.94 REMARK 500 THR L 130 28.62 -65.17 REMARK 500 ASN L 142 84.58 28.52 REMARK 500 TYR L 144 147.57 -174.94 REMARK 500 ASP L 155 60.80 72.37 REMARK 500 SER L 166 129.14 -173.34 REMARK 500 ASP L 171 -175.68 -56.95 REMARK 500 SER L 175 62.31 36.98 REMARK 500 THR L 176 -145.86 -109.25 REMARK 500 GLU L 189 5.88 -62.02 REMARK 500 GLU L 191 42.13 -108.08 REMARK 500 THR L 204 -9.29 -57.14 REMARK 500 VAL H 2 83.90 -37.23 REMARK 500 THR H 9 151.96 -47.80 REMARK 500 ALA H 16 -138.33 -61.74 REMARK 500 CYS H 22 73.66 -176.57 REMARK 500 SER H 25 100.52 -160.08 REMARK 500 TRP H 33 -127.05 -101.07 REMARK 500 MET H 34 103.37 151.29 REMARK 500 PRO H 41 -113.10 -16.92 REMARK 500 GLN H 43 -80.70 -122.23 REMARK 500 SER H 56 11.95 55.50 REMARK 500 GLN H 62 -24.72 -37.59 REMARK 500 ALA H 72 126.77 -177.36 REMARK 500 SER H 85 73.01 14.13 REMARK 500 THR H 87 -162.90 -129.02 REMARK 500 ALA H 92 -179.96 -177.91 REMARK 500 PHE H 101 22.69 -77.59 REMARK 500 ASP H 102 -24.08 -157.16 REMARK 500 TYR H 103 -116.00 -128.91 REMARK 500 ASN H 105 135.69 160.35 REMARK 500 GLU H 106 -68.75 -175.83 REMARK 500 VAL H 116 53.15 -118.13 REMARK 500 SER H 117 -150.51 -94.56 REMARK 500 SER H 118 -9.72 -141.89 REMARK 500 PRO H 124 -163.71 -60.53 REMARK 500 SER H 125 106.78 -162.53 REMARK 500 SER H 133 154.56 155.87 REMARK 500 ALA H 134 -9.30 -58.82 REMARK 500 ALA H 135 49.57 76.78 REMARK 500 GLN H 136 171.60 32.06 REMARK 500 ASN H 138 -13.78 46.41 REMARK 500 PHE H 151 141.28 -178.00 REMARK 500 PRO H 152 -152.89 -87.98 REMARK 500 PRO H 154 -143.52 -94.34 REMARK 500 VAL H 155 80.24 -177.07 REMARK 500 SER H 161 18.17 54.34 REMARK 500 SER H 165 -40.15 -145.40 REMARK 500 PRO H 172 -178.85 -61.20 REMARK 500 SER H 177 -112.27 64.48 REMARK 500 ALA H 206 -34.09 -30.67 REMARK 500 LYS H 214 -166.72 -74.67 REMARK 500 SER M 7 -88.23 -33.71 REMARK 500 CYS M 23 94.75 -177.14 REMARK 500 TYR M 32 18.70 30.94 REMARK 500 ASN M 34 -157.50 -137.99 REMARK 500 ARG M 54 62.40 67.34 REMARK 500 ALA M 55 51.87 16.84 REMARK 500 SER M 56 -37.19 169.89 REMARK 500 SER M 67 135.76 172.17 REMARK 500 SER M 71 176.23 163.10 REMARK 500 ARG M 72 -106.76 45.37 REMARK 500 ASN M 80 127.09 -173.96 REMARK 500 ALA M 88 -165.65 -165.16 REMARK 500 SER M 95 45.24 -144.39 REMARK 500 ASP M 114 157.61 -39.73 REMARK 500 ALA M 115 115.68 -161.19 REMARK 500 PRO M 124 121.33 -37.96 REMARK 500 SER M 125 -172.46 -60.97 REMARK 500 THR M 130 26.57 -66.10 REMARK 500 SER M 135 102.32 -161.71 REMARK 500 ASN M 142 85.10 28.31 REMARK 500 TYR M 144 147.11 -176.73 REMARK 500 ASP M 155 58.89 72.93 REMARK 500 SER M 166 128.74 -171.48 REMARK 500 ASP M 171 -176.56 -55.29 REMARK 500 SER M 175 60.70 39.70 REMARK 500 THR M 176 -147.15 -109.83 REMARK 500 GLU M 189 4.37 -61.23 REMARK 500 VAL N 2 85.74 -36.08 REMARK 500 THR N 9 152.76 -49.10 REMARK 500 ALA N 16 -137.12 -63.53 REMARK 500 CYS N 22 76.69 -179.13 REMARK 500 SER N 25 100.49 -161.11 REMARK 500 TRP N 33 -129.06 -101.67 REMARK 500 MET N 34 102.03 151.79 REMARK 500 PRO N 41 -113.00 -17.59 REMARK 500 GLN N 43 -77.52 -123.10 REMARK 500 ILE N 48 -63.35 -109.86 REMARK 500 SER N 56 13.93 56.02 REMARK 500 GLN N 62 -23.18 -38.73 REMARK 500 ALA N 72 127.82 -178.29 REMARK 500 SER N 85 71.90 12.59 REMARK 500 THR N 87 -161.62 -125.79 REMARK 500 ALA N 92 -179.02 -177.72 REMARK 500 PHE N 101 21.99 -76.55 REMARK 500 ASP N 102 -26.02 -157.26 REMARK 500 TYR N 103 -122.06 -120.58 REMARK 500 ASN N 105 125.37 87.69 REMARK 500 GLU N 106 -72.85 -175.34 REMARK 500 VAL N 116 52.82 -116.01 REMARK 500 SER N 117 -152.02 -91.71 REMARK 500 SER N 118 -11.16 -141.24 REMARK 500 PRO N 124 -164.02 -59.47 REMARK 500 SER N 125 104.86 -164.72 REMARK 500 SER N 133 153.70 154.31 REMARK 500 ALA N 135 48.84 77.74 REMARK 500 GLN N 136 172.82 30.92 REMARK 500 ASN N 138 -14.31 47.27 REMARK 500 PHE N 151 140.35 -178.27 REMARK 500 PRO N 152 -147.87 -90.05 REMARK 500 PRO N 154 -144.53 -91.60 REMARK 500 VAL N 155 81.35 -176.39 REMARK 500 SER N 161 19.99 53.69 REMARK 500 SER N 165 -36.75 -147.20 REMARK 500 GLN N 176 99.85 -60.54 REMARK 500 SER N 177 -112.83 66.90 REMARK 500 PRO N 189 158.07 -49.37 REMARK 500 ALA N 206 -33.03 -31.88 REMARK 500 LYS N 214 -169.24 -74.37 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 D 135 DISTANCE = 5.00 ANGSTROMS REMARK 525 HOH L 224 DISTANCE = 6.00 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RTL E 177 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RTL F 178 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1RLB RELATED DB: PDB REMARK 900 RBP-TTR COMPLEX REMARK 900 RELATED ID: 1QAB RELATED DB: PDB REMARK 900 RBP-TTR COMPLEX REMARK 900 RELATED ID: 1F41 RELATED DB: PDB REMARK 900 HUMAN TTR REMARK 900 RELATED ID: 1KT7 RELATED DB: PDB REMARK 900 BOVINE PLASMA RBP REMARK 900 RELATED ID: 1RBP RELATED DB: PDB REMARK 900 HUMAN PLASMA RBP REMARK 900 RELATED ID: 3BT0 RELATED DB: PDB