Header list of 2bru.pdb file
Complete list - r 29 2 Bytes
HEADER OXIDOREDUCTASE 11-MAY-05 2BRU TITLE COMPLEX OF THE DOMAIN I AND DOMAIN III OF ESCHERICHIA COLI TITLE 2 TRANSHYDROGENASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: NAD(P) TRANSHYDROGENASE SUBUNIT ALPHA; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: DOMAIN I, RESIDUES 2-394; COMPND 5 SYNONYM: PYRIDINE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT ALPHA, COMPND 6 NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT ALPHA; COMPND 7 EC: 1.6.1.2; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NAD(P) TRANSHYDROGENASE SUBUNIT BETA; COMPND 11 CHAIN: C; COMPND 12 FRAGMENT: DOMAIN III, RESIDUES 286-462; COMPND 13 SYNONYM: PYRIDINE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT BETA, COMPND 14 NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT BETA; COMPND 15 EC: 1.6.1.2; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: JM109; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 10 ORGANISM_TAXID: 562; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS PARAMAGNETIC NMR, TRANSHYDROGENASE, INNER MEMBRANE, MEMBRANE, NAD, KEYWDS 2 NADP, OXIDOREDUCTASE, TRANSMEMBRANE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR T.JOHANSSON,A.PEDERSEN,J.LECKNER,B.G.KARLSSON REVDAT 3 29-MAR-17 2BRU 1 SOURCE REVDAT 2 24-FEB-09 2BRU 1 VERSN REVDAT 1 29-AUG-06 2BRU 0 JRNL AUTH T.JOHANSSON,A.PEDERSEN,J.LECKNER,B.G.KARLSSON JRNL TITL STRUCTURE DETERMINATION OF A TRANSIENT COMPLEX BY NMR USING JRNL TITL 2 PARAMAGNETIC DISTANCE RESTRAINTS - THE COMPLEX OF THE JRNL TITL 3 SOLUBLE DOMAINS OF ESCHERICHIA COLI TRANSHYDROGENASE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 2BRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-05. REMARK 100 THE PDBE ID CODE IS EBI-23838. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.0 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 110 REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 95% H2O/5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : UNITYINOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : RIGID BODY MINIMIZATION, REMARK 210 MOLECULAR DYNAMICS SIMULATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 10 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NONE REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 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 400 REMARK 400 COMPOUND REMARK 400 FUNCTION: PROTON PUMP ACROSS THE MEMBRANE 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 994 REMARK 465 HIS A 995 REMARK 465 HIS A 996 REMARK 465 HIS A 997 REMARK 465 HIS A 998 REMARK 465 HIS A 999 REMARK 465 LYS A 1217 REMARK 465 GLU A 1218 REMARK 465 GLU A 1219 REMARK 465 ALA A 1220 REMARK 465 GLY A 1221 REMARK 465 SER A 1222 REMARK 465 GLY A 1223 REMARK 465 GLN A 1374 REMARK 465 VAL A 1375 REMARK 465 SER A 1376 REMARK 465 ALA A 1377 REMARK 465 GLN A 1378 REMARK 465 PRO A 1379 REMARK 465 GLN A 1380 REMARK 465 ALA A 1381 REMARK 465 ALA A 1382 REMARK 465 GLN A 1383 REMARK 465 LYS A 1384 REMARK 465 ALA A 1385 REMARK 465 ALA A 1386 REMARK 465 PRO A 1387 REMARK 465 GLU A 1388 REMARK 465 VAL A 1389 REMARK 465 LYS A 1390 REMARK 465 THR A 1391 REMARK 465 GLU A 1392 REMARK 465 GLU A 1393 REMARK 465 LYS A 1394 REMARK 465 MET B 994 REMARK 465 HIS B 995 REMARK 465 HIS B 996 REMARK 465 HIS B 997 REMARK 465 PHE B 1216 REMARK 465 LYS B 1217 REMARK 465 GLU B 1218 REMARK 465 GLU B 1219 REMARK 465 ALA B 1220 REMARK 465 GLY B 1221 REMARK 465 SER B 1222 REMARK 465 GLY B 1223 REMARK 465 ASP B 1224 REMARK 465 GLY B 1225 REMARK 465 TYR B 1226 REMARK 465 ALA B 1227 REMARK 465 LYS B 1228 REMARK 465 VAL B 1229 REMARK 465 ALA B 1377 REMARK 465 GLN B 1378 REMARK 465 PRO B 1379 REMARK 465 GLN B 1380 REMARK 465 ALA B 1381 REMARK 465 ALA B 1382 REMARK 465 GLN B 1383 REMARK 465 LYS B 1384 REMARK 465 ALA B 1385 REMARK 465 ALA B 1386 REMARK 465 PRO B 1387 REMARK 465 GLU B 1388 REMARK 465 VAL B 1389 REMARK 465 LYS B 1390 REMARK 465 THR B 1391 REMARK 465 GLU B 1392 REMARK 465 GLU B 1393 REMARK 465 LYS B 1394 REMARK 465 MET C 1 REMARK 465 HIS C 2 REMARK 465 HIS C 3 REMARK 465 HIS C 4 REMARK 465 HIS C 5 REMARK 465 HIS C 6 REMARK 465 HIS C 7 REMARK 465 SER C 8 REMARK 465 SER C 9 REMARK 465 GLN C 10 REMARK 465 GLU C 11 REMARK 465 VAL C 12 REMARK 465 GLY C 13 REMARK 465 GLU C 14 REMARK 465 HIS C 15 REMARK 465 ARG C 16 REMARK 465 GLU C 17 REMARK 465 ILE C 18 REMARK 465 THR C 19 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-10 REMARK 470 RES CSSEQI ATOMS REMARK 470 LYS A1228 CG CD CE NZ REMARK 470 VAL A1229 CG1 CG2 REMARK 470 ILE A1373 CA C O CB CG1 CG2 CD1 REMARK 470 SER B1376 CA C O CB OG 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 HIS A1000 NE2 HIS A1000 CD2 -0.081 REMARK 500 1 HIS A1147 NE2 HIS A1147 CD2 -0.077 REMARK 500 1 HIS B 998 NE2 HIS B 998 CD2 -0.089 REMARK 500 1 HIS B 999 NE2 HIS B 999 CD2 -0.068 REMARK 500 1 HIS B1000 NE2 HIS B1000 CD2 -0.070 REMARK 500 1 HIS B1147 NE2 HIS B1147 CD2 -0.069 REMARK 500 1 HIS C 31 NE2 HIS C 31 CD2 -0.076 REMARK 500 1 HIS C 69 NE2 HIS C 69 CD2 -0.076 REMARK 500 1 HIS C 169 NE2 HIS C 169 CD2 -0.083 REMARK 500 2 HIS A1000 NE2 HIS A1000 CD2 -0.073 REMARK 500 2 HIS A1147 NE2 HIS A1147 CD2 -0.072 REMARK 500 2 HIS B 999 NE2 HIS B 999 CD2 -0.075 REMARK 500 2 HIS B1147 NE2 HIS B1147 CD2 -0.090 REMARK 500 2 HIS C 69 NE2 HIS C 69 CD2 -0.070 REMARK 500 2 HIS C 78 NE2 HIS C 78 CD2 -0.070 REMARK 500 2 HIS C 169 NE2 HIS C 169 CD2 -0.069 REMARK 500 3 HIS A1000 NE2 HIS A1000 CD2 -0.084 REMARK 500 3 HIS A1147 NE2 HIS A1147 CD2 -0.086 REMARK 500 3 HIS B 999 NE2 HIS B 999 CD2 -0.078 REMARK 500 3 HIS B1147 NE2 HIS B1147 CD2 -0.083 REMARK 500 3 HIS C 31 NE2 HIS C 31 CD2 -0.084 REMARK 500 3 HIS C 69 NE2 HIS C 69 CD2 -0.071 REMARK 500 4 HIS A1000 NE2 HIS A1000 CD2 -0.077 REMARK 500 4 HIS A1147 NE2 HIS A1147 CD2 -0.076 REMARK 500 4 HIS B1000 NE2 HIS B1000 CD2 -0.072 REMARK 500 4 HIS C 31 NE2 HIS C 31 CD2 -0.074 REMARK 500 4 HIS C 69 NE2 HIS C 69 CD2 -0.072 REMARK 500 4 HIS C 78 NE2 HIS C 78 CD2 -0.085 REMARK 500 4 HIS C 169 NE2 HIS C 169 CD2 -0.075 REMARK 500 5 HIS B 999 NE2 HIS B 999 CD2 -0.081 REMARK 500 5 HIS B1000 NE2 HIS B1000 CD2 -0.075 REMARK 500 5 HIS B1147 NE2 HIS B1147 CD2 -0.095 REMARK 500 5 HIS C 69 NE2 HIS C 69 CD2 -0.086 REMARK 500 5 HIS C 169 NE2 HIS C 169 CD2 -0.076 REMARK 500 6 HIS A1147 NE2 HIS A1147 CD2 -0.079 REMARK 500 6 HIS B 999 NE2 HIS B 999 CD2 -0.077 REMARK 500 6 HIS C 31 NE2 HIS C 31 CD2 -0.072 REMARK 500 6 HIS C 69 NE2 HIS C 69 CD2 -0.086 REMARK 500 6 HIS C 78 NE2 HIS C 78 CD2 -0.073 REMARK 500 7 HIS B 998 NE2 HIS B 998 CD2 -0.085 REMARK 500 7 HIS B1000 NE2 HIS B1000 CD2 -0.068 REMARK 500 7 HIS B1147 NE2 HIS B1147 CD2 -0.074 REMARK 500 7 HIS C 31 NE2 HIS C 31 CD2 -0.066 REMARK 500 7 HIS C 69 NE2 HIS C 69 CD2 -0.079 REMARK 500 7 HIS C 78 NE2 HIS C 78 CD2 -0.078 REMARK 500 7 HIS C 169 NE2 HIS C 169 CD2 -0.069 REMARK 500 8 HIS A1000 NE2 HIS A1000 CD2 -0.096 REMARK 500 8 HIS A1147 NE2 HIS A1147 CD2 -0.074 REMARK 500 8 HIS B 998 NE2 HIS B 998 CD2 -0.082 REMARK 500 8 HIS B1000 NE2 HIS B1000 CD2 -0.075 REMARK 500 REMARK 500 THIS ENTRY HAS 70 BOND DEVIATIONS. 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 ARG A1002 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 1 ARG A1002 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 TRP A1064 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES REMARK 500 1 TRP A1094 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES REMARK 500 1 TRP A1094 CE2 - CD2 - CG ANGL. DEV. = -6.7 DEGREES REMARK 500 1 TRP A1094 CG - CD2 - CE3 ANGL. DEV. = 5.7 DEGREES REMARK 500 1 ARG A1120 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 1 ARG A1123 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 ARG A1123 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 1 ARG A1140 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 1 HIS A1147 CB - CG - CD2 ANGL. DEV. = -11.1 DEGREES REMARK 500 1 PHE A1149 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 ARG A1197 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG A1269 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 1 ARG A1318 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 1 ARG A1318 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 1 TRP A1368 CD1 - CG - CD2 ANGL. DEV. = 7.4 DEGREES REMARK 500 1 TRP A1368 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES REMARK 500 1 TRP A1368 CE2 - CD2 - CG ANGL. DEV. = -7.0 DEGREES REMARK 500 1 TRP A1368 CG - CD2 - CE3 ANGL. DEV. = 7.0 DEGREES REMARK 500 1 GLU B1008 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES REMARK 500 1 ARG B1009 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 TRP B1064 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 1 TRP B1064 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES REMARK 500 1 TRP B1094 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES REMARK 500 1 TRP B1094 CE2 - CD2 - CG ANGL. DEV. = -7.1 DEGREES REMARK 500 1 ARG B1192 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 ARG B1197 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 1 MET B1230 CA - C - N ANGL. DEV. = 13.9 DEGREES REMARK 500 1 MET B1230 O - C - N ANGL. DEV. = -10.7 DEGREES REMARK 500 1 ARG B1269 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 1 ARG B1269 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 1 ARG B1356 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES REMARK 500 1 ARG B1356 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 TRP B1368 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES REMARK 500 1 TRP B1368 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 TYR C 39 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 1 TYR C 48 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 1 ARG C 74 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 1 ASP C 97 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 1 ASP C 124 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES REMARK 500 1 TRP C 139 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES REMARK 500 1 TRP C 139 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES REMARK 500 1 TRP C 139 CG - CD2 - CE3 ANGL. DEV. = 6.6 DEGREES REMARK 500 2 ARG A1007 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 2 ASP A1046 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 PHE A1050 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 2 TRP A1064 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 TRP A1064 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES REMARK 500 2 TRP A1094 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 350 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 SER A1037 96.09 -47.27 REMARK 500 1 PHE A1092 97.51 -58.79 REMARK 500 1 SER A1117 48.40 -80.38 REMARK 500 1 ASP A1128 89.32 -69.84 REMARK 500 1 THR A1154 92.24 -60.16 REMARK 500 1 LEU A1214 95.39 -62.55 REMARK 500 1 ASP A1215 90.67 -69.45 REMARK 500 1 LEU A1319 78.56 -110.47 REMARK 500 1 LYS A1342 77.42 55.10 REMARK 500 1 ASP A1343 -80.88 78.30 REMARK 500 1 PRO A1369 -150.69 -78.21 REMARK 500 1 SER B1044 25.24 46.89 REMARK 500 1 ASN B1073 -161.76 -105.95 REMARK 500 1 ASN B1098 58.41 -119.09 REMARK 500 1 SER B1117 48.16 -102.52 REMARK 500 1 PRO B1119 103.14 -58.06 REMARK 500 1 ILE B1121 -161.11 -104.48 REMARK 500 1 ALA B1173 -9.03 -59.05 REMARK 500 1 VAL B1175 -82.60 56.19 REMARK 500 1 SER B1231 -173.11 78.84 REMARK 500 1 ASP B1232 154.99 -43.25 REMARK 500 1 ALA B1233 -59.19 62.97 REMARK 500 1 ALA B1256 96.65 -47.79 REMARK 500 1 ASN B1288 48.10 -107.52 REMARK 500 1 THR B1295 105.17 -37.69 REMARK 500 1 ARG B1318 3.43 -52.52 REMARK 500 1 PRO B1320 -71.92 -26.57 REMARK 500 1 THR B1347 105.31 -59.21 REMARK 500 1 HIS C 31 -76.93 59.98 REMARK 500 1 PRO C 37 37.74 -74.17 REMARK 500 1 TYR C 39 -57.07 68.66 REMARK 500 1 GLN C 45 25.87 49.52 REMARK 500 1 VAL C 71 95.56 -68.23 REMARK 500 1 ALA C 72 109.91 -161.17 REMARK 500 1 LEU C 75 142.84 63.13 REMARK 500 1 HIS C 78 -84.32 48.55 REMARK 500 1 LYS C 87 62.13 63.10 REMARK 500 1 MET C 96 29.59 42.81 REMARK 500 1 ASP C 107 -102.68 -86.94 REMARK 500 1 THR C 108 91.77 -69.83 REMARK 500 1 ALA C 114 9.13 47.73 REMARK 500 1 ALA C 121 4.98 -69.58 REMARK 500 1 PRO C 126 46.58 -78.05 REMARK 500 1 ILE C 130 72.58 -65.61 REMARK 500 1 LYS C 140 46.37 37.19 REMARK 500 1 ALA C 141 -156.36 -73.50 REMARK 500 1 ALA C 156 -93.55 -165.54 REMARK 500 1 GLN C 159 16.31 43.20 REMARK 500 2 ASN A1012 -4.67 63.28 REMARK 500 2 PHE A1045 92.15 -172.31 REMARK 500 REMARK 500 THIS ENTRY HAS 489 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 PHE A 1045 ASP A 1046 2 -147.43 REMARK 500 PHE A 1045 ASP A 1046 5 -148.09 REMARK 500 PHE A 1045 ASP A 1046 8 -149.88 REMARK 500 THR A 1255 ALA A 1256 9 -140.26 REMARK 500 HIS B 998 HIS B 999 10 148.76 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A1108 0.09 SIDE CHAIN REMARK 500 1 ARG B1318 0.10 SIDE CHAIN REMARK 500 1 TYR C 90 0.08 SIDE CHAIN REMARK 500 2 TYR B1139 0.11 SIDE CHAIN REMARK 500 2 TYR B1312 0.09 SIDE CHAIN REMARK 500 2 TYR C 39 0.07 SIDE CHAIN REMARK 500 2 TYR C 48 0.07 SIDE CHAIN REMARK 500 3 ARG A1140 0.09 SIDE CHAIN REMARK 500 4 TYR A1294 0.07 SIDE CHAIN REMARK 500 4 ARG A1318 0.09 SIDE CHAIN REMARK 500 4 TYR A1327 0.07 SIDE CHAIN REMARK 500 4 TYR B1139 0.08 SIDE CHAIN REMARK 500 4 TYR B1312 0.07 SIDE CHAIN REMARK 500 4 ARG B1318 0.12 SIDE CHAIN REMARK 500 4 ARG C 60 0.09 SIDE CHAIN REMARK 500 5 TYR A1294 0.08 SIDE CHAIN REMARK 500 5 TYR B1327 0.07 SIDE CHAIN REMARK 500 5 TYR C 155 0.12 SIDE CHAIN REMARK 500 6 ARG A1123 0.09 SIDE CHAIN REMARK 500 6 TYR A1139 0.09 SIDE CHAIN REMARK 500 6 ARG A1362 0.09 SIDE CHAIN REMARK 500 6 TYR B1139 0.11 SIDE CHAIN REMARK 500 6 ARG C 58 0.12 SIDE CHAIN REMARK 500 6 TYR C 90 0.11 SIDE CHAIN REMARK 500 7 TYR B1312 0.07 SIDE CHAIN REMARK 500 8 ARG A1007 0.09 SIDE CHAIN REMARK 500 8 ARG A1140 0.10 SIDE CHAIN REMARK 500 8 ARG A1192 0.11 SIDE CHAIN REMARK 500 8 TYR A1294 0.10 SIDE CHAIN REMARK 500 8 ARG A1362 0.08 SIDE CHAIN REMARK 500 8 TYR B1139 0.09 SIDE CHAIN REMARK 500 9 ARG A1140 0.09 SIDE CHAIN REMARK 500 9 ARG A1269 0.09 SIDE CHAIN REMARK 500 9 TYR A1294 0.07 SIDE CHAIN REMARK 500 9 ARG A1318 0.09 SIDE CHAIN REMARK 500 9 TYR C 90 0.07 SIDE CHAIN REMARK 500 10 ARG B1318 0.12 SIDE CHAIN REMARK 500 10 TYR C 48 0.11 SIDE CHAIN 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 NAD B 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C1001 REMARK 999 REMARK 999 SEQUENCE REMARK 999 ALL CHAINS INCLUDE N-TERMINAL HIS-TAGS DBREF 2BRU A 994 1001 PDB 2BRU 2BRU 994 1001 DBREF 2BRU A 1002 1394 UNP P07001 PNTA_ECOLI 2 394 DBREF 2BRU B 994 1001 PDB 2BRU 2BRU 994 1001 DBREF 2BRU B 1002 1394 UNP P07001 PNTA_ECOLI 2 394 DBREF 2BRU C 1 9 PDB 2BRU 2BRU 1 9 DBREF 2BRU C 10 186 UNP P07002 PNTB_ECOLI 286 462 SEQRES 1 A 401 MET HIS HIS HIS HIS HIS HIS GLY ARG ILE GLY ILE PRO SEQRES 2 A 401 ARG GLU ARG LEU THR ASN GLU THR ARG VAL ALA ALA THR SEQRES 3 A 401 PRO LYS THR VAL GLU GLN LEU LEU LYS LEU GLY PHE THR SEQRES 4 A 401 VAL ALA VAL GLU SER GLY ALA GLY GLN LEU ALA SER PHE SEQRES 5 A 401 ASP ASP LYS ALA PHE VAL GLN ALA GLY ALA GLU ILE VAL SEQRES 6 A 401 GLU GLY ASN SER VAL TRP GLN SER GLU ILE ILE LEU LYS SEQRES 7 A 401 VAL ASN ALA PRO LEU ASP ASP GLU ILE ALA LEU LEU ASN SEQRES 8 A 401 PRO GLY THR THR LEU VAL SER PHE ILE TRP PRO ALA GLN SEQRES 9 A 401 ASN PRO GLU LEU MET GLN LYS LEU ALA GLU ARG ASN VAL SEQRES 10 A 401 THR VAL MET ALA MET ASP SER VAL PRO ARG ILE SER ARG SEQRES 11 A 401 ALA GLN SER LEU ASP ALA LEU SER SER MET ALA ASN ILE SEQRES 12 A 401 ALA GLY TYR ARG ALA ILE VAL GLU ALA ALA HIS GLU PHE SEQRES 13 A 401 GLY ARG PHE PHE THR GLY GLN ILE THR ALA ALA GLY LYS SEQRES 14 A 401 VAL PRO PRO ALA LYS VAL MET VAL ILE GLY ALA GLY VAL SEQRES 15 A 401 ALA GLY LEU ALA ALA ILE GLY ALA ALA ASN SER LEU GLY SEQRES 16 A 401 ALA ILE VAL ARG ALA PHE ASP THR ARG PRO GLU VAL LYS SEQRES 17 A 401 GLU GLN VAL GLN SER MET GLY ALA GLU PHE LEU GLU LEU SEQRES 18 A 401 ASP PHE LYS GLU GLU ALA GLY SER GLY ASP GLY TYR ALA SEQRES 19 A 401 LYS VAL MET SER ASP ALA PHE ILE LYS ALA GLU MET GLU SEQRES 20 A 401 LEU PHE ALA ALA GLN ALA LYS GLU VAL ASP ILE ILE VAL SEQRES 21 A 401 THR THR ALA LEU ILE PRO GLY LYS PRO ALA PRO LYS LEU SEQRES 22 A 401 ILE THR ARG GLU MET VAL ASP SER MET LYS ALA GLY SER SEQRES 23 A 401 VAL ILE VAL ASP LEU ALA ALA GLN ASN GLY GLY ASN CYS SEQRES 24 A 401 GLU TYR THR VAL PRO GLY GLU ILE PHE THR THR GLU ASN SEQRES 25 A 401 GLY VAL LYS VAL ILE GLY TYR THR ASP LEU PRO GLY ARG SEQRES 26 A 401 LEU PRO THR GLN SER SER GLN LEU TYR GLY THR ASN LEU SEQRES 27 A 401 VAL ASN LEU LEU LYS LEU LEU CYS LYS GLU LYS ASP GLY SEQRES 28 A 401 ASN ILE THR VAL ASP PHE ASP ASP VAL VAL ILE ARG GLY SEQRES 29 A 401 VAL THR VAL ILE ARG ALA GLY GLU ILE THR TRP PRO ALA SEQRES 30 A 401 PRO PRO ILE GLN VAL SER ALA GLN PRO GLN ALA ALA GLN SEQRES 31 A 401 LYS ALA ALA PRO GLU VAL LYS THR GLU GLU LYS SEQRES 1 B 401 MET HIS HIS HIS HIS HIS HIS GLY ARG ILE GLY ILE PRO SEQRES 2 B 401 ARG GLU ARG LEU THR ASN GLU THR ARG VAL ALA ALA THR SEQRES 3 B 401 PRO LYS THR VAL GLU GLN LEU LEU LYS LEU GLY PHE THR SEQRES 4 B 401 VAL ALA VAL GLU SER GLY ALA GLY GLN LEU ALA SER PHE SEQRES 5 B 401 ASP ASP LYS ALA PHE VAL GLN ALA GLY ALA GLU ILE VAL SEQRES 6 B 401 GLU GLY ASN SER VAL TRP GLN SER GLU ILE ILE LEU LYS SEQRES 7 B 401 VAL ASN ALA PRO LEU ASP ASP GLU ILE ALA LEU LEU ASN SEQRES 8 B 401 PRO GLY THR THR LEU VAL SER PHE ILE TRP PRO ALA GLN SEQRES 9 B 401 ASN PRO GLU LEU MET GLN LYS LEU ALA GLU ARG ASN VAL SEQRES 10 B 401 THR VAL MET ALA MET ASP SER VAL PRO ARG ILE SER ARG SEQRES 11 B 401 ALA GLN SER LEU ASP ALA LEU SER SER MET ALA ASN ILE SEQRES 12 B 401 ALA GLY TYR ARG ALA ILE VAL GLU ALA ALA HIS GLU PHE SEQRES 13 B 401 GLY ARG PHE PHE THR GLY GLN ILE THR ALA ALA GLY LYS SEQRES 14 B 401 VAL PRO PRO ALA LYS VAL MET VAL ILE GLY ALA GLY VAL SEQRES 15 B 401 ALA GLY LEU ALA ALA ILE GLY ALA ALA ASN SER LEU GLY SEQRES 16 B 401 ALA ILE VAL ARG ALA PHE ASP THR ARG PRO GLU VAL LYS SEQRES 17 B 401 GLU GLN VAL GLN SER MET GLY ALA GLU PHE LEU GLU LEU SEQRES 18 B 401 ASP PHE LYS GLU GLU ALA GLY SER GLY ASP GLY TYR ALA SEQRES 19 B 401 LYS VAL MET SER ASP ALA PHE ILE LYS ALA GLU MET GLU SEQRES 20 B 401 LEU PHE ALA ALA GLN ALA LYS GLU VAL ASP ILE ILE VAL SEQRES 21 B 401 THR THR ALA LEU ILE PRO GLY LYS PRO ALA PRO LYS LEU SEQRES 22 B 401 ILE THR ARG GLU MET VAL ASP SER MET LYS ALA GLY SER SEQRES 23 B 401 VAL ILE VAL ASP LEU ALA ALA GLN ASN GLY GLY ASN CYS SEQRES 24 B 401 GLU TYR THR VAL PRO GLY GLU ILE PHE THR THR GLU ASN SEQRES 25 B 401 GLY VAL LYS VAL ILE GLY TYR THR ASP LEU PRO GLY ARG SEQRES 26 B 401 LEU PRO THR GLN SER SER GLN LEU TYR GLY THR ASN LEU SEQRES 27 B 401 VAL ASN LEU LEU LYS LEU LEU CYS LYS GLU LYS ASP GLY SEQRES 28 B 401 ASN ILE THR VAL ASP PHE ASP ASP VAL VAL ILE ARG GLY SEQRES 29 B 401 VAL THR VAL ILE ARG ALA GLY GLU ILE THR TRP PRO ALA SEQRES 30 B 401 PRO PRO ILE GLN VAL SER ALA GLN PRO GLN ALA ALA GLN SEQRES 31 B 401 LYS ALA ALA PRO GLU VAL LYS THR GLU GLU LYS SEQRES 1 C 186 MET HIS HIS HIS HIS HIS HIS SER SER GLN GLU VAL GLY SEQRES 2 C 186 GLU HIS ARG GLU ILE THR ALA GLU GLU THR ALA GLU LEU SEQRES 3 C 186 LEU LYS ASN SER HIS SER VAL ILE ILE THR PRO GLY TYR SEQRES 4 C 186 GLY MET ALA VAL ALA GLN ALA GLN TYR PRO VAL ALA GLU SEQRES 5 C 186 ILE THR GLU LYS LEU ARG ALA ARG GLY ILE ASN VAL ARG SEQRES 6 C 186 PHE GLY ILE HIS PRO VAL ALA GLY ARG LEU PRO GLY HIS SEQRES 7 C 186 MET ASN VAL LEU LEU ALA GLU ALA LYS VAL PRO TYR ASP SEQRES 8 C 186 ILE VAL LEU GLU MET ASP GLU ILE ASN ASP ASP PHE ALA SEQRES 9 C 186 ASP THR ASP THR VAL LEU VAL ILE GLY ALA ASN ASP THR SEQRES 10 C 186 VAL ASN PRO ALA ALA GLN ASP ASP PRO LYS SER PRO ILE SEQRES 11 C 186 ALA GLY MET PRO VAL LEU GLU VAL TRP LYS ALA GLN ASN SEQRES 12 C 186 VAL ILE VAL PHE LYS ARG SER MET ASN THR GLY TYR ALA SEQRES 13 C 186 GLY VAL GLN ASN PRO LEU PHE PHE LYS GLU ASN THR HIS SEQRES 14 C 186 MET LEU PHE GLY ASP ALA LYS ALA SER VAL ASP ALA ILE SEQRES 15 C 186 LEU LYS ALA LEU HET NAD B 1 52 HET NAP C1001 55 HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE FORMUL 4 NAD C21 H27 N7 O14 P2 FORMUL 5 NAP C21 H28 N7 O17 P3 HELIX 1 1 THR A 1019 LEU A 1029 1 11 HELIX 2 2 GLN A 1041 SER A 1044 5 4 HELIX 3 3 ASP A 1046 GLY A 1054 1 9 HELIX 4 4 GLU A 1059 GLN A 1065 5 7 HELIX 5 5 LEU A 1076 LEU A 1083 1 8 HELIX 6 6 TRP A 1094 GLN A 1097 5 4 HELIX 7 7 ASN A 1098 ARG A 1108 1 11 HELIX 8 8 SER A 1122 LEU A 1127 5 6 HELIX 9 9 ASP A 1128 PHE A 1149 1 22 HELIX 10 10 GLY A 1174 GLY A 1188 1 15 HELIX 11 11 ARG A 1197 GLU A 1199 5 3 HELIX 12 12 VAL A 1200 GLY A 1208 1 9 HELIX 13 13 ASP A 1224 SER A 1231 1 8 HELIX 14 14 SER A 1231 VAL A 1249 1 19 HELIX 15 15 THR A 1268 SER A 1274 1 7 HELIX 16 16 ALA A 1285 ASN A 1288 5 4 HELIX 17 17 LEU A 1319 CYS A 1339 1 21 HELIX 18 18 ASP A 1352 VAL A 1358 1 7 HELIX 19 19 THR B 1019 LEU B 1029 1 11 HELIX 20 20 GLY B 1038 ALA B 1043 1 6 HELIX 21 21 ASP B 1047 GLY B 1054 1 8 HELIX 22 22 GLY B 1060 GLN B 1065 5 6 HELIX 23 23 LEU B 1076 LEU B 1083 1 8 HELIX 24 24 ASN B 1098 ARG B 1108 1 11 HELIX 25 25 ILE B 1121 ASP B 1128 1 8 HELIX 26 26 ASP B 1128 PHE B 1149 1 22 HELIX 27 27 VAL B 1175 GLY B 1188 1 14 HELIX 28 28 PRO B 1198 MET B 1207 1 10 HELIX 29 29 ALA B 1233 VAL B 1249 1 17 HELIX 30 30 THR B 1268 ASP B 1273 1 6 HELIX 31 31 LEU B 1319 CYS B 1339 1 21 HELIX 32 32 ASP B 1352 THR B 1359 1 8 HELIX 33 33 ALA C 20 SER C 30 1 11 HELIX 34 34 TYR C 39 ALA C 44 1 6 HELIX 35 35 ALA C 46 GLY C 61 1 16 HELIX 36 36 HIS C 78 LYS C 87 1 10 HELIX 37 37 ILE C 99 THR C 106 1 8 HELIX 38 38 ALA C 114 ASN C 119 5 6 HELIX 39 39 ASN C 119 GLN C 123 5 5 HELIX 40 40 ASP C 174 LEU C 186 1 13 SHEET 1 AA 8 GLU A1056 VAL A1058 0 SHEET 2 AA 8 THR A1032 GLU A1036 1 O VAL A1033 N GLU A1056 SHEET 3 AA 8 ARG A1002 ILE A1005 1 O ILE A1003 N ALA A1034 SHEET 4 AA 8 ILE A1068 LEU A1070 1 O ILE A1068 N GLY A1004 SHEET 5 AA 8 THR A1088 SER A1091 1 O THR A1088 N ILE A1069 SHEET 6 AA 8 THR A1111 ALA A1114 1 O THR A1111 N LEU A1089 SHEET 7 AA 8 THR A1359 ARG A1362 -1 O ILE A1361 N VAL A1112 SHEET 8 AA 8 GLU A1365 ILE A1366 -1 O GLU A1365 N ARG A1362 SHEET 1 AB 2 GLN A1156 ILE A1157 0 SHEET 2 AB 2 LYS A1162 VAL A1163 -1 O VAL A1163 N GLN A1156 SHEET 1 AC 7 ALA A1209 PHE A1211 0 SHEET 2 AC 7 ILE A1190 PHE A1194 1 O VAL A1191 N GLU A1210 SHEET 3 AC 7 LYS A1167 ILE A1171 1 O VAL A1168 N ARG A1192 SHEET 4 AC 7 ILE A1251 THR A1254 1 O ILE A1251 N MET A1169 SHEET 5 AC 7 SER A1279 ASP A1283 1 O VAL A1280 N ILE A1252 SHEET 6 AC 7 VAL A1307 ILE A1310 1 O LYS A1308 N ILE A1281 SHEET 7 AC 7 ILE A1300 THR A1303 -1 O PHE A1301 N VAL A1309 SHEET 1 BA 6 ALA B1055 VAL B1058 0 SHEET 2 BA 6 THR B1032 GLU B1036 1 O VAL B1033 N GLU B1056 SHEET 3 BA 6 ARG B1002 ILE B1005 1 O ILE B1003 N ALA B1034 SHEET 4 BA 6 ILE B1068 LEU B1070 1 O ILE B1068 N GLY B1004 SHEET 5 BA 6 GLY B1086 SER B1091 1 O THR B1088 N ILE B1069 SHEET 6 BA 6 VAL B1110 ALA B1114 1 O THR B1111 N LEU B1089 SHEET 1 BB 7 GLU B1210 PHE B1211 0 SHEET 2 BB 7 ILE B1190 PHE B1194 1 O VAL B1191 N GLU B1210 SHEET 3 BB 7 LYS B1167 ILE B1171 1 O VAL B1168 N ARG B1192 SHEET 4 BB 7 ILE B1251 THR B1254 1 O ILE B1251 N MET B1169 SHEET 5 BB 7 SER B1279 ASP B1283 1 O VAL B1280 N ILE B1252 SHEET 6 BB 7 VAL B1307 ILE B1310 1 O LYS B1308 N ILE B1281 SHEET 7 BB 7 ILE B1300 THR B1302 -1 O PHE B1301 N VAL B1309 SHEET 1 CA 6 VAL C 93 GLU C 95 0 SHEET 2 CA 6 ASN C 63 ILE C 68 1 O PHE C 66 N LEU C 94 SHEET 3 CA 6 SER C 32 THR C 36 1 O VAL C 33 N ARG C 65 SHEET 4 CA 6 THR C 108 VAL C 111 1 O LEU C 110 N THR C 36 SHEET 5 CA 6 ASN C 143 PHE C 147 1 O ASN C 143 N VAL C 109 SHEET 6 CA 6 THR C 168 LEU C 171 1 O HIS C 169 N VAL C 146 CISPEP 1 LYS A 1342 ASP A 1343 1 -6.64 CISPEP 2 TRP A 1368 PRO A 1369 1 -8.81 CISPEP 3 MET B 1230 SER B 1231 1 -17.20 CISPEP 4 TRP B 1368 PRO B 1369 1 -9.13 CISPEP 5 LYS A 1342 ASP A 1343 2 -10.65 CISPEP 6 TRP A 1368 PRO A 1369 2 -6.10 CISPEP 7 MET B 1230 SER B 1231 2 0.63 CISPEP 8 TRP B 1368 PRO B 1369 2 -7.96 CISPEP 9 LYS A 1342 ASP A 1343 3 21.31 CISPEP 10 TRP A 1368 PRO A 1369 3 -7.27 CISPEP 11 MET B 1230 SER B 1231 3 -10.13 CISPEP 12 TRP B 1368 PRO B 1369 3 -11.46 CISPEP 13 LYS A 1342 ASP A 1343 4 -17.33 CISPEP 14 TRP A 1368 PRO A 1369 4 4.24 CISPEP 15 MET B 1230 SER B 1231 4 -1.58 CISPEP 16 TRP B 1368 PRO B 1369 4 -5.59 CISPEP 17 LYS A 1342 ASP A 1343 5 8.51 CISPEP 18 TRP A 1368 PRO A 1369 5 -0.59 CISPEP 19 MET B 1230 SER B 1231 5 -8.60 CISPEP 20 TRP B 1368 PRO B 1369 5 -3.39 CISPEP 21 LYS A 1342 ASP A 1343 6 -19.35 CISPEP 22 TRP A 1368 PRO A 1369 6 -0.33 CISPEP 23 MET B 1230 SER B 1231 6 2.15 CISPEP 24 TRP B 1368 PRO B 1369 6 9.40 CISPEP 25 LYS A 1342 ASP A 1343 7 -0.18 CISPEP 26 TRP A 1368 PRO A 1369 7 5.84 CISPEP 27 MET B 1230 SER B 1231 7 -10.32 CISPEP 28 TRP B 1368 PRO B 1369 7 4.85 CISPEP 29 LYS A 1342 ASP A 1343 8 -6.08 CISPEP 30 TRP A 1368 PRO A 1369 8 2.56 CISPEP 31 MET B 1230 SER B 1231 8 -9.92 CISPEP 32 TRP B 1368 PRO B 1369 8 -5.86 CISPEP 33 LYS A 1342 ASP A 1343 9 4.49 CISPEP 34 TRP A 1368 PRO A 1369 9 4.17 CISPEP 35 MET B 1230 SER B 1231 9 -18.34 CISPEP 36 TRP B 1368 PRO B 1369 9 10.24 CISPEP 37 LYS A 1342 ASP A 1343 10 9.59 CISPEP 38 TRP A 1368 PRO A 1369 10 -4.13 CISPEP 39 MET B 1230 SER B 1231 10 -0.03 CISPEP 40 TRP B 1368 PRO B 1369 10 -2.36 SITE 1 AC1 17 ARG B1120 SER B1122 GLN B1125 GLY B1172 SITE 2 AC1 17 GLY B1174 VAL B1175 PHE B1194 ASP B1195 SITE 3 AC1 17 THR B1196 ARG B1197 GLU B1238 ALA B1256 SITE 4 AC1 17 LEU B1257 VAL B1375 VAL C 71 MET C 133 SITE 5 AC1 17 NAP C1001 SITE 1 AC2 31 NAD B 1 GLN B1203 GLY C 38 TYR C 39 SITE 2 AC2 31 GLY C 40 VAL C 43 ALA C 44 PRO C 70 SITE 3 AC2 31 VAL C 71 ALA C 72 GLY C 73 ARG C 74 SITE 4 AC2 31 LEU C 75 PRO C 76 GLY C 113 ALA C 114 SITE 5 AC2 31 ASN C 115 ASP C 116 THR C 117 ILE C 130 SITE 6 AC2 31 MET C 133 PHE C 147 LYS C 148 ARG C 149 SITE 7 AC2 31 SER C 150 ASN C 152 GLY C 154 TYR C 155 SITE 8 AC2 31 GLY C 173 ASP C 174 ALA C 175 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1
Complete list - r 29 2 Bytes