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HEADER IMMUNOGLOBULIN 21-JUN-93 1TET TITLE CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE COMPLEX TITLE 2 AT 2.3 ANGSTROMS COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG1 TE33 FAB (LIGHT CHAIN); COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG1 TE33 FAB (HEAVY CHAIN); COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CHOLERA TOXIN PEPTIDE 3 (CTP3); COMPND 11 CHAIN: P; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 MOL_ID: 2; SOURCE 3 MOL_ID: 3 KEYWDS IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR M.SHOHAM REVDAT 2 01-APR-03 1TET 1 JRNL REVDAT 1 31-JAN-94 1TET 0 JRNL AUTH M.SHOHAM JRNL TITL CRYSTAL STRUCTURE OF AN ANTICHOLERA TOXIN PEPTIDE JRNL TITL 2 COMPLEX AT 2.3 A. JRNL REF J.MOL.BIOL. V. 232 1169 1993 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.SHOHAM,P.PROCTOR,D.HUGHES,E.T.BALDWIN REMARK 1 TITL CRYSTAL PARAMETERS AND MOLECULAR REPLACEMENT OF AN REMARK 1 TITL 2 ANTICHOLERA TOXIN PEPTIDE COMPLEX REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 11 218 1991 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 13714 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.148 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3377 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 13 REMARK 3 SOLVENT ATOMS : 151 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.015 REMARK 3 BOND ANGLES (DEGREES) : 3.58 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL 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 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TET COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-17) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.26 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 1/2-X,1/2+Y,-Z REMARK 290 4555 1/2+X,1/2-Y,-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 52.07500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.30500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.07500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.30500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: L, H, P 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 VAL P 1 REMARK 465 GLU P 2 REMARK 465 ALA P 15 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLY H 127 CA C O 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 REMARK 500 NZ LYS H 143 O HOH 101 1.80 REMARK 500 CG2 THR H 116 O HOH 102 1.82 REMARK 500 N GLY H 127 O HOH 30 2.18 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 CD1 LEU H 159 O HOH 100 1556 2.14 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 SER P 6 N - CA - C ANGL. DEV. = 20.3 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 VAL L 51 -52.33 71.90 REMARK 500 LYS L 183 -50.88 79.51 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 SER H 186 PRO H 187 145.25 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 28 DISTANCE = 6.33 ANGSTROMS REMARK 525 HOH 31 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH 33 DISTANCE = 6.61 ANGSTROMS REMARK 525 HOH 36 DISTANCE = 5.27 ANGSTROMS REMARK 525 HOH 38 DISTANCE = 6.81 ANGSTROMS REMARK 525 HOH 46 DISTANCE = 6.31 ANGSTROMS REMARK 525 HOH 48 DISTANCE = 7.97 ANGSTROMS REMARK 525 HOH 50 DISTANCE = 5.37 ANGSTROMS REMARK 525 HOH 61 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH 63 DISTANCE = 7.38 ANGSTROMS REMARK 525 HOH 71 DISTANCE = 5.03 ANGSTROMS REMARK 525 HOH 98 DISTANCE = 7.02 ANGSTROMS REMARK 525 HOH 112 DISTANCE = 5.09 ANGSTROMS REMARK 525 HOH 116 DISTANCE = 6.09 ANGSTROMS REMARK 525 HOH 140 DISTANCE = 7.24 ANGSTROMS REMARK 525 HOH 142 DISTANCE = 5.40 ANGSTROMS REMARK 525 HOH 149 DISTANCE = 5.10 ANGSTROMS DBREF 1TET L 1 211 PIR PC4203 PC4203 1 216 DBREF 1TET H 1 213 GB 2072131 AAB53773 12 227 DBREF 1TET P 1 15 UNP P32890 ELBP_ECOLI 71 85 SEQADV 1TET LYS L 24 PIR PC4203 ARG 24 CONFLICT SEQADV 1TET SER L 31A PIR PC4203 THR 32 CONFLICT SEQADV 1TET SER L 31B PIR PC4203 ASN 33 CONFLICT SEQADV 1TET PHE L 33 PIR PC4203 LEU 38 CONFLICT SEQADV 1TET ILE L 94 PIR PC4203 VAL 99 CONFLICT SEQADV 1TET PHE L 96 PIR PC4203 ARG 101 CONFLICT SEQADV 1TET SER L 100 PIR PC4203 GLY 105 CONFLICT SEQADV 1TET TRP L 188 PIR PC4203 ARG 193 CONFLICT SEQADV 1TET THR H 13 GB 2072131 LYS 24 CONFLICT SEQADV 1TET GLY H 26 GB 2072131 ASP 37 CONFLICT SEQADV 1TET THR H 28 GB 2072131 SER 39 CONFLICT SEQADV 1TET THR H 30 GB 2072131 MET 41 CONFLICT SEQADV 1TET TYR H 32 GB 2072131 SER 43 CONFLICT SEQADV 1TET SER H 35 GB 2072131 GLN 46 CONFLICT SEQADV 1TET LYS H 38 GB 2072131 GLN 49 CONFLICT SEQADV 1TET THR H 40 GB 2072131 MET 51 CONFLICT SEQADV 1TET PHE H 45 GB 2072131 LEU 56 CONFLICT SEQADV 1TET MET H 48 GB 2072131 ILE 59 CONFLICT SEQADV 1TET ILE H 51 GB 2072131 LEU 62 CONFLICT SEQADV 1TET TYR H 53 GB 2072131 GLN 65 CONFLICT SEQADV 1TET THR H 58 GB 2072131 GLU 70 CONFLICT SEQADV 1TET ASP H 61 GB 2072131 GLU 73 CONFLICT SEQADV 1TET SER H 76 GB 2072131 THR 88 CONFLICT SEQADV 1TET H GB 2072131 THR 109 DELETION SEQADV 1TET H GB 2072131 TRP 110 DELETION SEQADV 1TET H GB 2072131 GLY 111 DELETION SEQADV 1TET ARG H 94 GB 2072131 GLY 112 CONFLICT SEQADV 1TET ARG H 95 GB 2072131 ASN 113 CONFLICT SEQADV 1TET TRP H 100A GB 2072131 ALA 115 CONFLICT SEQADV 1TET PHE H 100C GB 2072131 INSERTION SEQADV 1TET ASP H 101 GB 2072131 INSERTION SEQADV 1TET VAL H 102 GB 2072131 INSERTION SEQADV 1TET THR H 105 GB 2072131 GLN 119 CONFLICT SEQADV 1TET VAL H 109 GB 2072131 LEU 123 CONFLICT SEQADV 1TET H GB 2072131 SER 142 DELETION SEQADV 1TET H GB 2072131 ALA 143 DELETION SEQADV 1TET H GB 2072131 ALA 144 DELETION SEQADV 1TET H GB 2072131 GLN 145 DELETION SEQADV 1TET H GB 2072131 THR 146 DELETION SEQADV 1TET H GB 2072131 ASN 147 DELETION SEQADV 1TET PRO H 187 GB 2072131 THR 201 CONFLICT SEQADV 1TET ARG H 188 GB 2072131 TRP 202 CONFLICT SEQRES 1 L 216 ASP VAL LEU MET THR GLN THR PRO LEU SER LEU PRO VAL SEQRES 2 L 216 SER LEU GLY ASP GLN ALA SER ILE SER CYS LYS SER SER SEQRES 3 L 216 GLN SER ILE VAL HIS SER SER GLY ASN THR TYR PHE GLU SEQRES 4 L 216 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 L 216 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 216 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 216 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 216 TYR CYS PHE GLN GLY SER HIS ILE PRO PHE THR PHE GLY SEQRES 9 L 216 SER GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA SEQRES 10 L 216 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU SEQRES 11 L 216 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN SEQRES 12 L 216 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP SEQRES 13 L 216 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR SEQRES 14 L 216 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER SEQRES 15 L 216 THR LEU THR LEU THR LYS ASP GLU TYR GLU TRP HIS ASN SEQRES 16 L 216 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER SEQRES 17 L 216 PRO ILE VAL LYS SER PHE ASN ARG SEQRES 1 H 210 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS THR SEQRES 2 H 210 PRO GLY GLU THR VAL ARG ILE SER CYS LYS ALA SER GLY SEQRES 3 H 210 TYR THR PHE THR THR TYR GLY MET SER TRP VAL LYS GLN SEQRES 4 H 210 THR PRO GLY LYS GLY PHE LYS TRP MET GLY TRP ILE ASN SEQRES 5 H 210 THR TYR SER GLY VAL PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 H 210 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 H 210 ALA TYR LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 H 210 ALA THR TYR PHE CYS ALA ARG ARG SER TRP TYR PHE ASP SEQRES 9 H 210 VAL TRP GLY THR GLY THR THR VAL THR VAL SER SER ALA SEQRES 10 H 210 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY SEQRES 11 H 210 SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE SEQRES 12 H 210 PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SEQRES 13 H 210 SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 14 H 210 ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO SER SEQRES 15 H 210 SER PRO ARG PRO SER GLU THR VAL THR CYS ASN VAL ALA SEQRES 16 H 210 HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL SEQRES 17 H 210 PRO ARG SEQRES 1 P 15 VAL GLU VAL PRO GLY SER GLN HIS ILE ASP SER GLN LYS SEQRES 2 P 15 LYS ALA FTNOTE 1 CIS PROLINE - PRO L 8 FTNOTE 2 CIS PROLINE - PRO L 95 FTNOTE 3 CIS PROLINE - PRO L 141 FTNOTE 4 CIS PROLINE - PRO H 147 FTNOTE 5 CIS PROLINE - PRO H 149 FTNOTE 6 SER H 186 - PRO H 187 OMEGA = 145.25 PEPTIDE BOND DEVIATES FTNOTE 6 SIGNIFICANTLY FROM TRANS CONFORMATION FTNOTE 7 CIS PROLINE - PRO H 189 HET CIT 1 13 HETNAM CIT CITRIC ACID FORMUL 4 CIT C6 H8 O7 FORMUL 5 HOH *151(H2 O) HELIX 1 1 GLU L 79 LEU L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 TRP L 188 1 6 HELIX 4 4 THR H 28 TYR H 32 5 5 HELIX 5 5 ASP H 61 LYS H 64 5 4 HELIX 6 6 LYS H 83 THR H 87 5 5 HELIX 7 7 SER H 156 SER H 158 5 3 HELIX 8 8 PRO H 200 SER H 203 5 4 SHEET 1 A 4 MET L 4 THR L 7 0 SHEET 2 A 4 ALA L 19 SER L 25 -1 O SER L 22 N THR L 7 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 O SER L 63 N LYS L 74 SHEET 1 B 6 SER L 10 SER L 14 0 SHEET 2 B 6 THR L 102 LYS L 107 1 O LYS L 103 N LEU L 11 SHEET 3 B 6 GLY L 84 GLN L 90 -1 O GLY L 84 N LEU L 104 SHEET 4 B 6 PHE L 33 GLN L 38 -1 N GLU L 34 O PHE L 89 SHEET 5 B 6 LYS L 45 TYR L 49 -1 N LYS L 45 O LEU L 37 SHEET 6 B 6 ASN L 53 ARG L 54 -1 N ASN L 53 O TYR L 49 SHEET 1 C 4 SER L 10 SER L 14 0 SHEET 2 C 4 THR L 102 LYS L 107 1 O LYS L 103 N LEU L 11 SHEET 3 C 4 GLY L 84 GLN L 90 -1 O GLY L 84 N LEU L 104 SHEET 4 C 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 D 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 139 SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 E 4 SER L 153 ARG L 155 0 SHEET 2 E 4 ASN L 145 ILE L 150 -1 O TRP L 148 N ARG L 155 SHEET 3 E 4 SER L 191 THR L 197 -1 N THR L 193 O LYS L 149 SHEET 4 E 4 ILE L 205 ASN L 210 -1 N ILE L 205 O ALA L 196 SHEET 1 F 4 GLN H 3 GLN H 6 0 SHEET 2 F 4 VAL H 18 SER H 25 -1 N LYS H 23 O VAL H 5 SHEET 3 F 4 THR H 77 ILE H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 F 4 PHE H 67 GLU H 72 -1 O ALA H 68 N GLN H 81 SHEET 1 G 5 PRO H 57 TYR H 59 0 SHEET 2 G 5 GLY H 44 ILE H 51 -1 O TRP H 50 N THR H 58 SHEET 3 G 5 GLY H 33 THR H 40 -1 N MET H 34 O ILE H 51 SHEET 4 G 5 ALA H 88 ARG H 95 -1 O THR H 89 N GLN H 39 SHEET 1 H 6 PRO H 57 TYR H 59 0 SHEET 2 H 6 GLY H 44 ILE H 51 -1 O TRP H 50 N THR H 58 SHEET 3 H 6 GLY H 33 THR H 40 -1 N MET H 34 O ILE H 51 SHEET 4 H 6 ALA H 88 ARG H 95 -1 O THR H 89 N GLN H 39 SHEET 5 H 6 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SHEET 6 H 6 GLU H 10 LYS H 12 1 N GLU H 10 O THR H 108 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 I 4 LEU H 174 PRO H 184 -1 N TYR H 175 O TYR H 145 SHEET 4 I 4 VAL H 163 THR H 165 -1 O HIS H 164 N SER H 180 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 MET H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 J 4 LEU H 174 PRO H 184 -1 N TYR H 175 O TYR H 145 SHEET 4 J 4 VAL H 169 GLN H 171 -1 N VAL H 169 O THR H 176 SHEET 1 K 3 THR H 151 TRP H 154 0 SHEET 2 K 3 THR H 194 HIS H 199 -1 N ASN H 196 O THR H 153 SHEET 3 K 3 THR H 204 LYS H 209 -1 O THR H 204 N HIS H 199 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 140 CYS H 195 CISPEP 1 THR L 7 PRO L 8 0 -20.84 CISPEP 2 ILE L 94 PRO L 95 0 4.76 CISPEP 3 TYR L 140 PRO L 141 0 -0.33 CISPEP 4 PHE H 146 PRO H 147 0 -12.42 CISPEP 5 GLU H 148 PRO H 149 0 7.85 CISPEP 6 ARG H 188 PRO H 189 0 -4.90 CRYST1 104.150 110.610 40.680 90.00 90.00 90.00 P 21 21 2 4 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 0.009602 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009041 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024582 0.00000