HEADER IMMUNE SYSTEM 08-DEC-99 1DL7 TITLE THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE RESPONSE TO TITLE 2 PHOSPHOCHOLINE CAVEAT 1DL7 SER 112 H HAS INCORRECT CHIRALITY COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (ANTIBODY M3C65 (LIGHT CHAIN)); COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FV (SINGLE CHAIN); COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: COMBINED LIGHT AND HEAVY CHAIN VIA (G4S)3 LINKER; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: PROTEIN (ANTIBODY M3C65 (HEAVY CHAIN)); COMPND 9 CHAIN: H; COMPND 10 FRAGMENT: FV (SINGLE CHAIN); COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: HYBRIDOMA M3C65; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 12 ORGANISM_COMMON: MOUSE; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 GENE: HYBRIDOMA M3C65; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS SINGLE CHAIN FV, REPERTOIRE SHIFT, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.SCHUMACHER,M.BROWN REVDAT 3 02-OCT-13 1DL7 1 SOURCE VERSN REVDAT 2 24-FEB-09 1DL7 1 VERSN REVDAT 1 13-DEC-00 1DL7 0 JRNL AUTH M.BROWN,M.A.SCHUMACHER,G.D.WIENS,R.G.BRENNAN,M.B.RITTENBERG JRNL TITL THE STRUCTURAL BASIS OF REPERTOIRE SHIFT IN AN IMMUNE JRNL TITL 2 RESPONSE TO PHOSPHOCHOLINE. JRNL REF J.EXP.MED. V. 191 2101 2000 JRNL REFN ISSN 0022-1007 JRNL PMID 10859335 JRNL DOI 10.1084/JEM.191.12.2101 REMARK 2 REMARK 2 RESOLUTION. 2.35 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TNT REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 84.0 REMARK 3 NUMBER OF REFLECTIONS : 8983 REMARK 3 REMARK 3 USING DATA ABOVE SIGMA CUTOFF. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.265 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 43 REMARK 3 REMARK 3 USING ALL DATA, NO SIGMA CUTOFF. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 47930 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1680 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 20 REMARK 3 SOLVENT ATOMS : 79 REMARK 3 REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 20.000 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT REMARK 3 BOND LENGTHS (A) : 0.014 ; NULL ; NULL REMARK 3 BOND ANGLES (DEGREES) : 1.900 ; NULL ; NULL REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL REMARK 3 REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : NULL REMARK 3 REMARK 3 RESTRAINT LIBRARIES. REMARK 3 STEREOCHEMISTRY : ENGH AND HUBER REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-99. REMARK 100 THE RCSB ID CODE IS RCSB010178. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 298. REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 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 : BIOTEX REMARK 200 DATA SCALING SOFTWARE : BIOTEX REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8983 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0 REMARK 200 DATA REDUNDANCY : 2.000 REMARK 200 R MERGE (I) : 0.07300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 52.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.30000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: EPMR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.43 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM/POTASSIUM PHOSPHATE, HEPES, PH REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 65.45000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.22500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 17.95000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.22500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.45000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 17.95000 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 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER OF ONE LIGHT CHAIN AND REMARK 300 ONE HEAVY CHAIN. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10840 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 OD1 ASP L 71 O SER H 112 1554 0.98 REMARK 500 CG ASP L 71 O SER H 112 1554 1.85 REMARK 500 N ASP L 71 O SER H 112 1554 1.94 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 SER H 112 N SER H 112 CA 1.319 REMARK 500 SER H 112 CA SER H 112 C 1.433 REMARK 500 SER H 112 C SER H 112 O 3.813 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 PRO H 41 C - N - CD ANGL. DEV. = -17.0 DEGREES REMARK 500 ARG H 92 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 SER H 112 N - CA - C ANGL. DEV. = 26.8 DEGREES REMARK 500 SER H 112 CA - C - O ANGL. DEV. = -16.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 TYR L 34 58.86 29.50 REMARK 500 THR L 53 -42.45 56.37 REMARK 500 LYS L 54 39.57 -150.62 REMARK 500 PRO L 58 77.82 -55.92 REMARK 500 SER L 67 178.42 179.29 REMARK 500 ASP L 71 35.76 -94.05 REMARK 500 ALA L 86 -175.40 -178.34 REMARK 500 TYR L 94 51.57 -105.91 REMARK 500 SER L 95 -45.31 81.13 REMARK 500 ASN L 96 -4.08 -141.01 REMARK 500 HIS L 97 -146.53 -126.79 REMARK 500 GLN H 3 119.54 -174.12 REMARK 500 LYS H 5 103.72 -166.92 REMARK 500 GLU H 6 75.25 -68.14 REMARK 500 SER H 15 -32.89 88.90 REMARK 500 PHE H 27 162.57 177.80 REMARK 500 TRP H 52 151.39 -43.89 REMARK 500 SER H 61 -55.54 -21.41 REMARK 500 ASN H 68 93.73 -173.91 REMARK 500 ASP H 88 22.42 -67.20 REMARK 500 ASP H 98 -175.32 -68.20 REMARK 500 TYR H 99 6.94 42.50 REMARK 500 THR H 107 111.86 175.17 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 THR L 5 24.1 L L OUTSIDE RANGE REMARK 500 ALA L 35 17.9 L L OUTSIDE RANGE REMARK 500 SER L 95 0.6 L L EXPECTING SP3 REMARK 500 LEU L 109 16.8 L L OUTSIDE RANGE REMARK 500 GLU H 6 12.9 L L OUTSIDE RANGE REMARK 500 LEU H 67 24.6 L L OUTSIDE RANGE REMARK 500 ASN H 68 15.4 L L OUTSIDE RANGE REMARK 500 THR H 87 19.1 L L OUTSIDE RANGE REMARK 500 SER H 112 -15.2 L D WRONG HAND 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 H 118 DISTANCE = 8.02 ANGSTROMS REMARK 525 HOH H 121 DISTANCE = 6.03 ANGSTROMS REMARK 525 HOH H 126 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH H 128 DISTANCE = 5.01 ANGSTROMS REMARK 525 HOH H 132 DISTANCE = 8.47 ANGSTROMS REMARK 525 HOH L1006 DISTANCE = 7.12 ANGSTROMS REMARK 525 HOH L1019 DISTANCE = 6.85 ANGSTROMS REMARK 525 HOH L1024 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH L1028 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH L1047 DISTANCE = 5.19 ANGSTROMS REMARK 525 HOH L1051 DISTANCE = 6.88 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCH L 999 DBREF 1DL7 L 1 109 PDB 1DL7 1DL7 1 109 DBREF 1DL7 H 1 112 PDB 1DL7 1DL7 1 112 SEQRES 1 L 109 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 L 109 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 L 109 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN SEQRES 4 L 109 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY SEQRES 5 L 109 THR LYS HIS ARG THR PRO GLY ALA PRO ALA ARG PHE SER SEQRES 6 L 109 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 L 109 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 L 109 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY THR SEQRES 9 L 109 LYS LEU THR VAL LEU SEQRES 1 H 112 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 H 112 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 H 112 PHE SER LEU THR GLY TYR GLY VAL ASN TRP VAL ARG GLN SEQRES 4 H 112 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY MET ILE TRP SEQRES 5 H 112 GLY ASP GLY SER THR ASP TYR ASN SER ALA LEU LYS SER SEQRES 6 H 112 ARG LEU ASN ILE SER LYS ASP LYS SER LYS SER GLN VAL SEQRES 7 H 112 PHE LEU ARG MET TYR SER LEU GLN THR ASP ASP THR ALA SEQRES 8 H 112 ARG TYR TYR CYS ALA ARG ASP TYR GLY PRO TYR TRP GLY SEQRES 9 H 112 GLN GLY THR LEU VAL THR VAL SER HET NCH L 999 20 HETNAM NCH P-NITROPHENYL-PHOSPHOCHOLINE FORMUL 3 NCH C11 H18 N2 O6 P 1+ FORMUL 4 HOH *79(H2 O) HELIX 1 1 GLN L 81 GLU L 85 5 5 HELIX 2 2 SER H 61 LYS H 64 5 4 HELIX 3 3 GLN H 86 THR H 90 5 5 SHEET 1 A 2 VAL L 4 THR L 5 0 SHEET 2 A 2 ARG L 23 SER L 24 -1 N ARG L 23 O THR L 5 SHEET 1 B 5 HIS L 55 ARG L 56 0 SHEET 2 B 5 LEU L 45 GLY L 51 -1 O GLY L 51 N HIS L 55 SHEET 3 B 5 ASN L 36 LYS L 41 -1 O TRP L 37 N LEU L 49 SHEET 4 B 5 ALA L 86 LEU L 92 -1 O ILE L 87 N GLU L 40 SHEET 5 B 5 VAL L 99 PHE L 100 -1 O VAL L 99 N LEU L 92 SHEET 1 B1 6 HIS L 55 ARG L 56 0 SHEET 2 B1 6 LEU L 45 GLY L 51 -1 O GLY L 51 N HIS L 55 SHEET 3 B1 6 ASN L 36 LYS L 41 -1 O TRP L 37 N LEU L 49 SHEET 4 B1 6 ALA L 86 LEU L 92 -1 O ILE L 87 N GLU L 40 SHEET 5 B1 6 THR L 104 VAL L 108 -1 O THR L 104 N TYR L 88 SHEET 6 B1 6 ALA L 9 THR L 12 1 N LEU L 10 O LYS L 105 SHEET 1 C 3 THR L 17 LEU L 20 0 SHEET 2 C 3 LYS L 72 THR L 78 -1 O LEU L 75 N LEU L 20 SHEET 3 C 3 PHE L 64 ILE L 69 -1 O SER L 65 N THR L 76 SHEET 1 D 3 LEU H 18 THR H 23 0 SHEET 2 D 3 GLN H 77 MET H 82 -1 O VAL H 78 N CYS H 22 SHEET 3 D 3 SER H 70 ASP H 72 -1 O SER H 70 N PHE H 79 SHEET 1 E 5 THR H 57 TYR H 59 0 SHEET 2 E 5 GLU H 46 ILE H 51 -1 N MET H 50 O ASP H 58 SHEET 3 E 5 VAL H 34 GLN H 39 -1 O VAL H 34 N ILE H 51 SHEET 4 E 5 ALA H 91 ARG H 97 -1 O ARG H 92 N GLN H 39 SHEET 5 E 5 LEU H 108 VAL H 109 -1 N VAL H 109 O ALA H 91 SSBOND 1 CYS L 22 CYS L 90 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 95 1555 1555 2.04 CISPEP 1 GLY H 100 PRO H 101 0 -1.03 SITE 1 AC1 12 TRP H 52 TYR H 83 ASP H 98 TYR H 99 SITE 2 AC1 12 TYR L 34 ASN L 36 GLY L 51 GLY L 52 SITE 3 AC1 12 HIS L 55 TRP L 93 HOH L1023 HOH L1026 CRYST1 130.900 35.900 50.450 90.00 90.00 90.00 P 21 21 21 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 0.007639 0.000000 0.000000 0.00000 SCALE2 0.000000 0.027855 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019822 0.00000