REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR_NIH REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: JOINT CALCULATION OF DSBB C41S FAB WITH REMARK 3 SOLID-STATE NMR RESTRAINTS AND X-RAY REFLECTIONS (X-RAY DATA ARE REMARK 3 FROM PDB ID: 2ZUQ) REMARK 4 REMARK 4 2LTQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-12. REMARK 100 THE RCSB ID CODE IS RCSB102821. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 261 REMARK 210 PH : 7.8 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 7 MG [U-100% 13C; U-100% 15N] REMARK 210 DSBB, 2 MG DDM, 7 MG E. COLI REMARK 210 LIPIDS, 90% H2O/10% D2O; 5 MG [2- REMARK 210 13C-GLYCEROL; U-15N] DSBB, 2 MG REMARK 210 DDM, 7 MG E. COLI LIPIDS, 90% REMARK 210 H2O/10% D2O; 4 MG [1,3-13C- REMARK 210 GLYCEROL; U-15N] DSBB, 2 MG DDM, REMARK 210 7 MG E. COLI LIPIDS, 90% H2O/10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D CC DARR; 3D NCACX; 3D NCOCX REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; VXRS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY, NMRPIPE, X-PLOR_NIH, REMARK 210 TALOS+, VNMRJ REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: CHEMICAL SHIFTS ASSIGNMENTS AND CC CORRELATIONS PROVIDE REMARK 210 DIHEDRAL ANGLE AND DISTANCE RESTRAINTS. REMARK 217 REMARK 217 SOLID STATE NMR STUDY REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 217 THESE RECORDS ARE MEANINGLESS. 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 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 APPLY THE FOLLOWING TO CHAINS: 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. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-10 REMARK 465 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 LEU A 2 REMARK 465 ARG A 3 REMARK 465 PHE A 4 REMARK 465 LEU A 5 REMARK 465 ASN A 6 REMARK 465 GLN A 7 REMARK 465 ALA A 8 REMARK 465 SER A 9 REMARK 465 ARG A 109 REMARK 465 PHE A 110 REMARK 465 PRO A 111 REMARK 465 GLU A 112 REMARK 465 TRP A 113 REMARK 465 SER A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 PHE A 166 REMARK 465 LYS A 167 REMARK 465 ALA A 168 REMARK 465 LYS A 169 REMARK 465 LYS A 170 REMARK 465 ARG A 171 REMARK 465 ASP A 172 REMARK 465 LEU A 173 REMARK 465 PHE A 174 REMARK 465 GLY A 175 REMARK 465 ARG A 176 REMARK 465 MET B 1 REMARK 465 ASP B 2 REMARK 465 SER B 3 REMARK 465 GLN B 4 REMARK 465 ALA B 5 REMARK 465 GLN B 6 REMARK 465 VAL B 7 REMARK 465 LEU B 8 REMARK 465 ILE B 9 REMARK 465 LEU B 10 REMARK 465 LEU B 11 REMARK 465 LEU B 12 REMARK 465 LEU B 13 REMARK 465 TRP B 14 REMARK 465 VAL B 15 REMARK 465 SER B 16 REMARK 465 GLY B 17 REMARK 465 THR B 18 REMARK 465 CYS B 19 REMARK 465 GLY B 20 REMARK 465 ARG B 133 REMARK 465 TYR C 101 REMARK 465 ARG C 102 REMARK 465 SER C 103 REMARK 465 TYR C 104 REMARK 465 ALA C 120 REMARK 465 MET D 1 REMARK 465 LEU D 2 REMARK 465 ARG D 3 REMARK 465 PHE D 4 REMARK 465 LEU D 5 REMARK 465 ASN D 6 REMARK 465 GLN D 7 REMARK 465 ALA D 8 REMARK 465 SER D 9 REMARK 465 ARG D 109 REMARK 465 PHE D 110 REMARK 465 PRO D 111 REMARK 465 GLU D 112 REMARK 465 TRP D 113 REMARK 465 SER D 163 REMARK 465 GLN D 164 REMARK 465 PRO D 165 REMARK 465 PHE D 166 REMARK 465 LYS D 167 REMARK 465 ALA D 168 REMARK 465 LYS D 169 REMARK 465 LYS D 170 REMARK 465 ARG D 171 REMARK 465 ASP D 172 REMARK 465 LEU D 173 REMARK 465 PHE D 174 REMARK 465 GLY D 175 REMARK 465 ARG D 176 REMARK 465 MET E 1 REMARK 465 ASP E 2 REMARK 465 SER E 3 REMARK 465 GLN E 4 REMARK 465 ALA E 5 REMARK 465 GLN E 6 REMARK 465 VAL E 7 REMARK 465 LEU E 8 REMARK 465 ILE E 9 REMARK 465 LEU E 10 REMARK 465 LEU E 11 REMARK 465 LEU E 12 REMARK 465 LEU E 13 REMARK 465 TRP E 14 REMARK 465 VAL E 15 REMARK 465 SER E 16 REMARK 465 GLY E 17 REMARK 465 THR E 18 REMARK 465 CYS E 19 REMARK 465 GLY E 20 REMARK 465 ARG E 133 REMARK 465 ALA F 120 REMARK 465 ILE F 216 REMARK 465 GLU F 217 REMARK 465 PRO F 218 REMARK 465 ARG F 219 REMARK 465 GLY F 220 REMARK 465 PRO F 221 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 HD21 ASN E 237 H GLU E 238 1.01 REMARK 500 HD21 ASN B 237 H GLU B 238 1.02 REMARK 500 H SER C 162 HD22 ASN C 202 1.03 REMARK 500 HD23 LEU E 72 HB3 ALA F 105 1.10 REMARK 500 HG3 LYS F 149 HG21 THR F 182 1.16 REMARK 500 HG12 VAL C 175 H LEU C 176 1.18 REMARK 500 H MET A 142 HD2 PRO A 143 1.20 REMARK 500 HG22 THR B 40 HB THR B 100 1.21 REMARK 500 HE22 GLN B 116 H ASN B 119 1.22 REMARK 500 HE21 GLN B 26 H GLY B 126 1.23 REMARK 500 HE22 GLN B 26 H GLY B 126 1.24 REMARK 500 HE22 GLN E 116 H ASN E 119 1.25 REMARK 500 HZ3 LYS B 44 OD1 ASP B 96 1.26 REMARK 500 HG SER F 118 HE2 LYS F 121 1.28 REMARK 500 H ARG F 67 H PHE F 68 1.29 REMARK 500 HB2 LYS C 19 HE21 GLN C 82 1.30 REMARK 500 HD22 ASN B 162 HG SER C 186 1.31 REMARK 500 HE1 HIS F 205 HB2 ALA F 207 1.34 REMARK 500 O LEU D 51 H LEU D 55 1.35 REMARK 500 NE2 GLN B 26 H GLY B 126 1.39 REMARK 500 H CYS F 201 O LYS F 214 1.40 REMARK 500 O ILE A 151 H ILE A 155 1.47 REMARK 500 O TYR B 75 H ALA B 77 1.49 REMARK 500 O PRO D 68 H TYR D 71 1.50 REMARK 500 O GLN F 3 H SER F 25 1.52 REMARK 500 H ALA E 60 O LYS E 115 1.53 REMARK 500 O VAL D 54 H ALA D 58 1.53 REMARK 500 O GLN B 63 H LYS B 71 1.54 REMARK 500 O VAL D 75 H TYR D 79 1.55 REMARK 500 HH12 ARG E 87 OD2 ASP E 108 1.55 REMARK 500 O ARG D 70 H MET D 74 1.57 REMARK 500 O LEU F 20 H LEU F 81 1.58 REMARK 500 O VAL A 75 H TYR A 79 1.59 REMARK 500 NH1 ARG C 44 H LEU C 45 1.59 REMARK 500 O ALA D 24 H THR D 28 1.59 REMARK 500 O LEU D 25 H ALA D 29 1.59 REMARK 500 OE2 GLU F 6 H GLY F 112 1.59 REMARK 500 O VAL A 158 H ILE A 162 1.59 REMARK 500 H TYR B 62 O TYR B 113 1.60 REMARK 500 O PRO E 166 HE2 HIS E 223 1.60 REMARK 500 O SER B 29 H LYS B 128 1.60 REMARK 500 O ILE B 175 H GLY B 177 1.60 REMARK 500 NZ LYS B 44 OD1 ASP B 96 1.85 REMARK 500 O ALA D 50 OG SER D 80 2.10 REMARK 500 O ALA D 64 N THR D 67 2.12 REMARK 500 O LEU D 147 CD1 PHE D 150 2.13 REMARK 500 O ALA C 28 OG SER C 31 2.14 REMARK 500 O GLN D 33 C LEU D 37 2.18 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 1 LYS A 66 N LYS A 66 CA -0.148 REMARK 500 1 ILE A 155 CA ILE A 155 C 0.163 REMARK 500 1 LEU D 37 CA LEU D 37 C 0.182 REMARK 500 1 LYS D 66 N LYS D 66 CA -0.123 REMARK 500 2 LEU A 37 CA LEU A 37 C 0.171 REMARK 500 2 LEU A 37 C LEU A 38 N 0.166 REMARK 500 2 LYS A 66 N LYS A 66 CA -0.160 REMARK 500 2 ILE A 155 CA ILE A 155 C 0.163 REMARK 500 2 LEU D 37 CA LEU D 37 C 0.165 REMARK 500 2 LYS D 66 N LYS D 66 CA -0.135 REMARK 500 2 ILE D 155 CA ILE D 155 C 0.157 REMARK 500 3 LYS A 66 N LYS A 66 CA -0.153 REMARK 500 3 ILE A 155 CA ILE A 155 C 0.165 REMARK 500 3 LEU D 37 CA LEU D 37 C 0.189 REMARK 500 3 LYS D 66 N LYS D 66 CA -0.133 REMARK 500 3 ILE D 155 CA ILE D 155 C 0.159 REMARK 500 4 LYS A 66 N LYS A 66 CA -0.171 REMARK 500 4 ILE A 155 CA ILE A 155 C 0.162 REMARK 500 4 LEU D 37 CA LEU D 37 C 0.165 REMARK 500 4 LYS D 66 N LYS D 66 CA -0.125 REMARK 500 5 LYS A 66 N LYS A 66 CA -0.166 REMARK 500 5 ILE A 155 CA ILE A 155 C 0.161 REMARK 500 5 LEU D 37 CA LEU D 37 C 0.165 REMARK 500 5 LYS D 66 N LYS D 66 CA -0.136 REMARK 500 6 LEU A 37 CA LEU A 37 C 0.156 REMARK 500 6 LEU A 38 CA LEU A 38 CB 0.140 REMARK 500 6 LYS A 66 N LYS A 66 CA -0.172 REMARK 500 6 ILE A 155 CA ILE A 155 C 0.164 REMARK 500 6 LYS D 66 N LYS D 66 CA -0.147 REMARK 500 6 ILE D 155 CA ILE D 155 C 0.156 REMARK 500 7 LYS A 66 N LYS A 66 CA -0.156 REMARK 500 7 ILE A 155 CA ILE A 155 C 0.161 REMARK 500 7 LEU D 37 CA LEU D 37 C 0.185 REMARK 500 7 LYS D 66 N LYS D 66 CA -0.146 REMARK 500 7 ILE D 155 CA ILE D 155 C 0.156 REMARK 500 8 LEU A 37 CA LEU A 37 C 0.159 REMARK 500 8 LYS A 66 N LYS A 66 CA -0.147 REMARK 500 8 ILE A 155 CA ILE A 155 C 0.162 REMARK 500 8 LYS D 66 N LYS D 66 CA -0.134 REMARK 500 9 LYS A 66 N LYS A 66 CA -0.169 REMARK 500 9 ILE A 155 CA ILE A 155 C 0.156 REMARK 500 9 LYS D 66 N LYS D 66 CA -0.144 REMARK 500 10 LEU A 37 CA LEU A 37 C 0.174 REMARK 500 10 LYS A 66 N LYS A 66 CA -0.166 REMARK 500 10 ILE A 155 CA ILE A 155 C 0.157 REMARK 500 10 LEU D 37 CA LEU D 37 C 0.179 REMARK 500 10 LYS D 66 N LYS D 66 CA -0.137 REMARK 500 10 ILE D 155 CA ILE D 155 C 0.157 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 1 LEU A 37 CB - CA - C ANGL. DEV. = -15.1 DEGREES REMARK 500 1 LEU A 37 CA - C - O ANGL. DEV. = -12.7 DEGREES REMARK 500 1 LEU A 37 CA - C - N ANGL. DEV. = -15.9 DEGREES REMARK 500 1 LYS A 66 N - CA - CB ANGL. DEV. = -18.2 DEGREES REMARK 500 1 PRO A 65 O - C - N ANGL. DEV. = -14.0 DEGREES REMARK 500 1 LYS A 66 C - N - CA ANGL. DEV. = 22.3 DEGREES REMARK 500 1 CYS C 134 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 1 PRO C 195 C - N - CD ANGL. DEV. = -12.7 DEGREES REMARK 500 1 LEU D 37 CA - C - O ANGL. DEV. = -13.5 DEGREES REMARK 500 1 LEU D 38 N - CA - CB ANGL. DEV. = 17.2 DEGREES REMARK 500 1 LEU D 37 CA - C - N ANGL. DEV. = -18.2 DEGREES REMARK 500 1 PRO D 65 O - C - N ANGL. DEV. = -11.0 DEGREES REMARK 500 1 LYS D 66 C - N - CA ANGL. DEV. = 16.8 DEGREES REMARK 500 2 LEU A 37 CA - C - O ANGL. DEV. = -13.2 DEGREES REMARK 500 2 LEU A 38 N - CA - CB ANGL. DEV. = 14.1 DEGREES REMARK 500 2 LEU A 37 CA - C - N ANGL. DEV. = -16.0 DEGREES REMARK 500 2 LYS A 66 N - CA - C ANGL. DEV. = -22.2 DEGREES REMARK 500 2 PRO A 65 O - C - N ANGL. DEV. = -14.0 DEGREES REMARK 500 2 LYS A 66 C - N - CA ANGL. DEV. = 20.7 DEGREES REMARK 500 2 PRO C 195 C - N - CD ANGL. DEV. = -12.7 DEGREES REMARK 500 2 LEU D 37 CB - CA - C ANGL. DEV. = -13.6 DEGREES REMARK 500 2 LEU D 37 CA - C - O ANGL. DEV. = -12.6 DEGREES REMARK 500 2 LEU D 37 CA - C - N ANGL. DEV. = -17.0 DEGREES REMARK 500 2 LYS D 66 N - CA - CB ANGL. DEV. = -15.6 DEGREES REMARK 500 2 PRO D 65 O - C - N ANGL. DEV. = -12.7 DEGREES REMARK 500 2 LYS D 66 C - N - CA ANGL. DEV. = 18.2 DEGREES REMARK 500 3 LEU A 37 CA - C - O ANGL. DEV. = -13.1 DEGREES REMARK 500 3 LEU A 38 N - CA - CB ANGL. DEV. = 15.8 DEGREES REMARK 500 3 LEU A 37 CA - C - N ANGL. DEV. = -15.5 DEGREES REMARK 500 3 LYS A 66 N - CA - CB ANGL. DEV. = 15.7 DEGREES REMARK 500 3 PRO A 65 O - C - N ANGL. DEV. = -13.4 DEGREES REMARK 500 3 LYS A 66 C - N - CA ANGL. DEV. = 17.5 DEGREES REMARK 500 3 CYS C 134 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 3 PRO C 195 C - N - CD ANGL. DEV. = -12.7 DEGREES REMARK 500 3 LEU D 37 CB - CA - C ANGL. DEV. = -15.0 DEGREES REMARK 500 3 LEU D 37 CA - C - O ANGL. DEV. = -12.7 DEGREES REMARK 500 3 LEU D 38 N - CA - CB ANGL. DEV. = -12.1 DEGREES REMARK 500 3 LEU D 38 N - CA - C ANGL. DEV. = 20.8 DEGREES REMARK 500 3 LEU D 37 CA - C - N ANGL. DEV. = -18.4 DEGREES REMARK 500 3 PRO D 65 O - C - N ANGL. DEV. = -12.0 DEGREES REMARK 500 4 LEU A 38 C - N - CA ANGL. DEV. = 15.5 DEGREES REMARK 500 4 LYS A 66 N - CA - CB ANGL. DEV. = 14.8 DEGREES REMARK 500 4 LYS A 66 N - CA - C ANGL. DEV. = -20.8 DEGREES REMARK 500 4 PRO A 65 O - C - N ANGL. DEV. = -14.5 DEGREES REMARK 500 4 LYS A 66 C - N - CA ANGL. DEV. = 21.7 DEGREES REMARK 500 4 CYS C 134 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 4 PRO C 195 C - N - CD ANGL. DEV. = -12.7 DEGREES REMARK 500 4 LEU D 37 CA - C - O ANGL. DEV. = -12.6 DEGREES REMARK 500 4 LEU D 38 N - CA - CB ANGL. DEV. = 12.9 DEGREES REMARK 500 4 LEU D 37 CA - C - N ANGL. DEV. = -16.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 130 ANGLE DEVIATIONS. 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 1 PHE A 32 -20.03 56.45 REMARK 500 1 GLN A 33 -39.24 -38.16 REMARK 500 1 LYS A 39 -48.93 -170.51 REMARK 500 1 VAL A 42 -141.99 58.91 REMARK 500 1 ILE A 63 -34.73 -31.08 REMARK 500 1 ALA A 64 114.81 150.47 REMARK 500 1 PRO A 65 41.48 -80.74 REMARK 500 1 LYS A 66 -124.08 -146.24 REMARK 500 1 ARG A 70 16.20 -55.94 REMARK 500 1 TYR A 71 -18.56 -38.89 REMARK 500 1 LEU A 94 -4.90 -56.25 REMARK 500 1 TYR A 97 85.44 -176.00 REMARK 500 1 PHE A 106 49.57 72.03 REMARK 500 1 MET A 107 16.36 -153.45 REMARK 500 1 PRO A 115 -150.09 -75.59 REMARK 500 1 LEU A 116 144.25 58.46 REMARK 500 1 ASP A 117 131.47 179.56 REMARK 500 1 LYS A 118 -37.61 -35.11 REMARK 500 1 TRP A 119 -73.02 -77.04 REMARK 500 1 VAL A 123 -30.58 -39.55 REMARK 500 1 ALA A 126 -13.76 -143.07 REMARK 500 1 GLU A 132 -104.75 -130.98 REMARK 500 1 GLN A 134 100.07 11.99 REMARK 500 1 ASP A 136 -86.04 51.72 REMARK 500 1 PHE A 137 -1.66 76.28 REMARK 500 1 GLU A 141 -162.67 38.31 REMARK 500 1 MET A 142 -31.32 -169.94 REMARK 500 1 PRO A 143 11.17 -68.26 REMARK 500 1 ALA B 35 93.32 -55.11 REMARK 500 1 THR B 54 126.30 62.23 REMARK 500 1 ARG B 55 101.81 -54.76 REMARK 500 1 LEU B 73 -51.99 -128.35 REMARK 500 1 TRP B 76 -44.46 55.54 REMARK 500 1 ALA B 77 -35.40 159.00 REMARK 500 1 SER B 82 101.80 -25.21 REMARK 500 1 ASP B 86 -26.93 -38.13 REMARK 500 1 SER B 93 135.04 175.58 REMARK 500 1 VAL B 104 100.89 -53.76 REMARK 500 1 LEU B 120 -170.22 63.56 REMARK 500 1 THR B 139 76.31 -115.64 REMARK 500 1 SER B 141 115.57 -169.14 REMARK 500 1 PRO B 145 162.37 -46.84 REMARK 500 1 SER B 147 -59.50 -24.92 REMARK 500 1 LEU B 161 74.39 -119.79 REMARK 500 1 TYR B 165 131.61 -174.12 REMARK 500 1 ASP B 176 -25.04 50.09 REMARK 500 1 GLN B 181 -40.99 -131.21 REMARK 500 1 ASN B 182 101.06 -47.72 REMARK 500 1 SER B 187 125.66 -170.41 REMARK 500 1 GLN B 191 129.89 -20.28 REMARK 500 REMARK 500 THIS ENTRY HAS 1848 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LEU A 37 LEU A 38 1 144.77 REMARK 500 TRP C 194 PRO C 195 1 -136.60 REMARK 500 LEU D 37 LEU D 38 1 -144.73 REMARK 500 ASN E 57 TYR E 58 1 49.06 REMARK 500 TRP F 194 PRO F 195 1 -138.64 REMARK 500 LEU A 37 LEU A 38 2 141.16 REMARK 500 TRP C 194 PRO C 195 2 -136.64 REMARK 500 LEU D 37 LEU D 38 2 -142.36 REMARK 500 ASN E 57 TYR E 58 2 49.13 REMARK 500 TRP F 194 PRO F 195 2 -138.71 REMARK 500 LEU A 37 LEU A 38 3 136.09 REMARK 500 TRP C 194 PRO C 195 3 -136.66 REMARK 500 LEU D 37 LEU D 38 3 -140.57 REMARK 500 ASN E 57 TYR E 58 3 48.98 REMARK 500 TRP F 194 PRO F 195 3 -138.67 REMARK 500 LEU A 37 LEU A 38 4 133.29 REMARK 500 TRP C 194 PRO C 195 4 -136.67 REMARK 500 LEU D 37 LEU D 38 4 -138.72 REMARK 500 ASN E 57 TYR E 58 4 49.02 REMARK 500 TRP F 194 PRO F 195 4 -138.66 REMARK 500 LEU A 37 LEU A 38 5 138.45 REMARK 500 TRP C 194 PRO C 195 5 -136.68 REMARK 500 LEU D 37 LEU D 38 5 -142.73 REMARK 500 ASN E 57 TYR E 58 5 49.07 REMARK 500 TRP F 194 PRO F 195 5 -138.64 REMARK 500 LEU A 37 LEU A 38 6 145.56 REMARK 500 TRP C 194 PRO C 195 6 -136.71 REMARK 500 LEU D 37 LEU D 38 6 -147.85 REMARK 500 ASN E 57 TYR E 58 6 49.04 REMARK 500 TRP F 194 PRO F 195 6 -138.65 REMARK 500 LEU A 37 LEU A 38 7 139.99 REMARK 500 TRP C 194 PRO C 195 7 -136.67 REMARK 500 LEU D 37 LEU D 38 7 -140.87 REMARK 500 ASN E 57 TYR E 58 7 48.98 REMARK 500 TRP F 194 PRO F 195 7 -138.63 REMARK 500 LEU A 37 LEU A 38 8 139.80 REMARK 500 TRP C 194 PRO C 195 8 -136.61 REMARK 500 LEU D 37 LEU D 38 8 -142.60 REMARK 500 ASN E 57 TYR E 58 8 48.96 REMARK 500 TRP F 194 PRO F 195 8 -138.63 REMARK 500 LEU A 37 LEU A 38 9 142.36 REMARK 500 TRP C 194 PRO C 195 9 -136.67 REMARK 500 LEU D 37 LEU D 38 9 -146.18 REMARK 500 ASN E 57 TYR E 58 9 49.04 REMARK 500 TRP F 194 PRO F 195 9 -138.70 REMARK 500 LEU A 37 LEU A 38 10 146.12 REMARK 500 TRP C 194 PRO C 195 10 -136.66 REMARK 500 LEU D 37 LEU D 38 10 -145.59 REMARK 500 ASN E 57 TYR E 58 10 49.04 REMARK 500 TRP F 194 PRO F 195 10 -138.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 1 LEU A 37 -31.83 REMARK 500 1 PRO A 65 29.81 REMARK 500 1 LEU D 37 32.36 REMARK 500 1 PRO D 65 26.09 REMARK 500 2 LEU A 37 -32.05 REMARK 500 2 PRO A 65 30.48 REMARK 500 2 LEU D 37 31.58 REMARK 500 2 PRO D 65 26.37 REMARK 500 3 LEU A 37 -32.25 REMARK 500 3 PRO A 65 31.05 REMARK 500 3 LEU D 37 32.44 REMARK 500 3 PRO D 65 28.02 REMARK 500 4 LEU A 37 -31.00 REMARK 500 4 PRO A 65 30.99 REMARK 500 4 LEU D 37 31.12 REMARK 500 4 PRO D 65 27.24 REMARK 500 5 LEU A 37 -31.28 REMARK 500 5 PRO A 65 30.70 REMARK 500 5 LEU D 37 31.23 REMARK 500 5 PRO D 65 28.45 REMARK 500 6 LEU A 37 -30.88 REMARK 500 6 PRO A 65 30.88 REMARK 500 6 LEU D 37 31.97 REMARK 500 6 PRO D 65 28.25 REMARK 500 7 LEU A 37 -30.05 REMARK 500 7 PRO A 65 30.91 REMARK 500 7 LEU D 37 31.76 REMARK 500 7 PRO D 65 26.64 REMARK 500 8 LEU A 37 -30.40 REMARK 500 8 PRO A 65 31.02 REMARK 500 8 LEU D 37 31.88 REMARK 500 8 PRO D 65 28.47 REMARK 500 9 LEU A 37 -31.55 REMARK 500 9 PRO A 65 31.18 REMARK 500 9 LEU D 37 32.06 REMARK 500 9 PRO D 65 27.31 REMARK 500 10 LEU A 37 -31.38 REMARK 500 10 PRO A 65 31.45 REMARK 500 10 LEU D 37 31.98 REMARK 500 10 PRO D 65 26.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 1 ASN B 57 23.6 L L OUTSIDE RANGE REMARK 500 1 LEU D 38 21.4 L L OUTSIDE RANGE REMARK 500 2 LEU A 38 11.1 L L OUTSIDE RANGE REMARK 500 2 ASN B 57 23.6 L L OUTSIDE RANGE REMARK 500 3 LEU A 37 45.2 L L OUTSIDE RANGE REMARK 500 3 LYS A 66 22.4 L L OUTSIDE RANGE REMARK 500 3 ASN B 57 23.5 L L OUTSIDE RANGE REMARK 500 3 LYS D 66 23.4 L L OUTSIDE RANGE REMARK 500 4 ASN B 57 23.5 L L OUTSIDE RANGE REMARK 500 4 LEU D 38 18.1 L L OUTSIDE RANGE REMARK 500 5 LEU A 38 14.3 L L OUTSIDE RANGE REMARK 500 5 ASN B 57 23.6 L L OUTSIDE RANGE REMARK 500 5 LEU D 38 23.1 L L OUTSIDE RANGE REMARK 500 5 LYS D 66 23.5 L L OUTSIDE RANGE REMARK 500 6 ASN B 57 23.5 L L OUTSIDE RANGE REMARK 500 6 LEU D 38 23.2 L L OUTSIDE RANGE REMARK 500 7 ASN B 57 23.6 L L OUTSIDE RANGE REMARK 500 7 LEU D 38 13.9 L L OUTSIDE RANGE REMARK 500 8 ASN B 57 23.5 L L OUTSIDE RANGE REMARK 500 8 LEU D 38 19.0 L L OUTSIDE RANGE REMARK 500 8 LYS D 66 24.0 L L OUTSIDE RANGE REMARK 500 9 LEU A 38 21.3 L L OUTSIDE RANGE REMARK 500 9 ASN B 57 23.6 L L OUTSIDE RANGE REMARK 500 10 LEU A 37 22.9 L L OUTSIDE RANGE REMARK 500 10 LEU A 38 18.5 L L OUTSIDE RANGE REMARK 500 10 LYS A 66 21.9 L L OUTSIDE RANGE REMARK 500 10 ASN B 57 23.6 L L OUTSIDE RANGE REMARK 500 10 LEU D 38 17.4 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ1 A 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ1 D 201 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2LEG RELATED DB: PDB REMARK 900 SIMILAR REFINEMENT METHOD REMARK 900 RELATED ID: 2ZUQ RELATED DB: PDB REMARK 900 THE SOURCE OF X-RAY DATA REMARK 900 RELATED ID: 18493 RELATED DB: BMRB