HEADER CATALYTIC ANTIBODY 18-MAR-98 25C8
TITLE CATALYTIC ANTIBODY 5C8, FAB-HAPTEN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IGG 5C8;
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: FAB;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: IGG 5C8;
COMPND 7 CHAIN: H;
COMPND 8 FRAGMENT: FAB
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090
KEYWDS CATALYTIC ANTIBODY, FAB, RING CLOSURE REACTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.GRUBER,I.A.WILSON
REVDAT 4 03-APR-24 25C8 1 REMARK SEQADV
REVDAT 3 24-FEB-09 25C8 1 VERSN
REVDAT 2 09-JUL-99 25C8 1 JRNL
REVDAT 1 23-MAR-99 25C8 0
JRNL AUTH K.GRUBER,B.ZHOU,K.N.HOUK,R.A.LERNER,C.G.SHEVLIN,I.A.WILSON
JRNL TITL STRUCTURAL BASIS FOR ANTIBODY CATALYSIS OF A DISFAVORED RING
JRNL TITL 2 CLOSURE REACTION.
JRNL REF BIOCHEMISTRY V. 38 7062 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10353817
JRNL DOI 10.1021/BI990210S
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.GRUBER,A.HEINE,E.A.STURA,C.G.SHEVLIN,I.A.WILSON
REMARK 1 TITL LIGAND-INDUCED CONFORMATIONAL CHANGES IN A CATALYTIC
REMARK 1 TITL 2 ANTIBODY: COMPARISON OF THE BOUND AND UNBOUND STRUCTURE OF
REMARK 1 TITL 3 FAB 5C8
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 33080
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2505
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1473
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 117
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.037
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3251
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 232
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.72000
REMARK 3 B22 (A**2) : 7.70000
REMARK 3 B33 (A**2) : 10.93000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.84000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 30.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.050 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.290 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.690 ; 2.500
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NME.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : NME.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 25C8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177671.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : DEC-96
REMARK 200 TEMPERATURE (KELVIN) : 97
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : PT COATED FUSED SILICA MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33080
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: FREE FAB 5C8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 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 56.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.00000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.00000
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 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: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH L 213 LIES ON A SPECIAL POSITION.
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER H 128
REMARK 475 ALA H 129
REMARK 475 ALA H 130
REMARK 475 GLN H 133
REMARK 475 THR H 134
REMARK 475 ASN H 135
REMARK 475 SER H 136
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 THR L 51 -52.77 73.57
REMARK 500 ALA L 84 -168.14 -177.40
REMARK 500 ASP L 110 153.74 -49.71
REMARK 500 SER L 116 115.88 -160.21
REMARK 500 ASN L 138 80.82 41.40
REMARK 500 PRO L 141 -167.69 -68.92
REMARK 500 GLU L 154 128.92 -37.54
REMARK 500 LYS L 169 -61.32 -90.87
REMARK 500 GLU L 185 -38.62 -35.83
REMARK 500 THR H 32 -159.06 -143.68
REMARK 500 GLN H 43 -160.32 -122.25
REMARK 500 ILE H 48 -60.55 -100.67
REMARK 500 PHE H 63 45.97 -100.18
REMARK 500 GLN H 64 100.82 -52.57
REMARK 500 ALA H 88 -176.89 173.17
REMARK 500 SER H 128 -90.03 32.28
REMARK 500 THR H 134 -40.24 -163.04
REMARK 500 ASN H 135 137.83 64.93
REMARK 500 SER H 136 -35.85 70.21
REMARK 500 SER H 163 61.21 39.53
REMARK 500 ASP H 183 -10.74 73.80
REMARK 500 SER H 195 11.35 -62.86
REMARK 500 PRO H 200 32.18 -84.85
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 GEP L 212
DBREF 25C8 L 2 211 UNP P01837 KAC_MOUSE 24 234
DBREF 25C8 H 2 226 UNP P01869 IGH1M_MOUSE 2 217
SEQADV 25C8 ASN L 32 UNP P01837 TYR 55 CONFLICT
SEQADV 25C8 SER L 94 UNP P01837 PHE 117 CONFLICT
SEQADV 25C8 TYR L 96 UNP P01837 HIS 119 CONFLICT
SEQADV 25C8 GLN H 3 UNP P01869 LYS 3 CONFLICT
SEQADV 25C8 GLN H 5 UNP P01869 LEU 5 CONFLICT
SEQADV 25C8 GLN H 6 UNP P01869 GLU 6 CONFLICT
SEQADV 25C8 PRO H 14 UNP P01869 SER 14 CONFLICT
SEQADV 25C8 LYS H 40 UNP P01869 ARG 40 CONFLICT
SEQADV 25C8 ALA H 49 UNP P01869 GLY 49 CONFLICT
SEQADV 25C8 GLN H 50 UNP P01869 ARG 50 CONFLICT
SEQADV 25C8 ASN H 56 UNP P01869 GLU 57 CONFLICT
SEQADV 25C8 THR H 57 UNP P01869 ILE 58 CONFLICT
SEQADV 25C8 LYS H 66 UNP P01869 THR 67 CONFLICT
SEQADV 25C8 SER H 75 UNP P01869 THR 76 CONFLICT
SEQADV 25C8 HIS H 81 UNP P01869 GLN 82 CONFLICT
SEQADV 25C8 SER H 87 UNP P01869 THR 91 CONFLICT
SEQADV 25C8 ALA H 93 UNP P01869 VAL 97 CONFLICT
SEQADV 25C8 ALA H 94 UNP P01869 ARG 98 CONFLICT
SEQADV 25C8 ASP H 95 UNP P01869 ARG 99 CONFLICT
SEQADV 25C8 PRO H 96 UNP P01869 GLY 100 CONFLICT
SEQADV 25C8 PRO H 97 UNP P01869 TYR 101 CONFLICT
SEQADV 25C8 TYR H 98 UNP P01869 GLY 102 CONFLICT
SEQADV 25C8 TYR H 99 UNP P01869 SER 103 CONFLICT
SEQADV 25C8 GLY H 100 UNP P01869 SER 104 CONFLICT
SEQADV 25C8 HIS H 100A UNP P01869 GLN 105 CONFLICT
SEQADV 25C8 GLY H 100B UNP P01869 GLU 106 CONFLICT
SEQADV 25C8 ASP H 101 UNP P01869 PRO 107 CONFLICT
SEQRES 1 L 212 ASP ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 L 212 SER LEU GLY GLU ARG VAL THR MET THR CYS THR ALA SER
SEQRES 3 L 212 SER SER VAL SER SER SER ASN LEU HIS TRP TYR GLN GLN
SEQRES 4 L 212 LYS PRO GLY SER SER PRO LYS LEU TRP ILE TYR SER THR
SEQRES 5 L 212 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY
SEQRES 6 L 212 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER
SEQRES 7 L 212 MET GLU ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN
SEQRES 8 L 212 TYR HIS ARG SER PRO TYR THR PHE GLY GLY GLY THR LYS
SEQRES 9 L 212 LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER
SEQRES 10 L 212 ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY
SEQRES 11 L 212 ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS
SEQRES 12 L 212 ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG
SEQRES 13 L 212 GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER
SEQRES 14 L 212 LYS ASP SER THR TYR SER MET SER SER THR LEU THR LEU
SEQRES 15 L 212 THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS
SEQRES 16 L 212 GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS
SEQRES 17 L 212 SER PHE ASN ARG
SEQRES 1 H 217 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 H 217 PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY
SEQRES 3 H 217 PHE ASN ILE LYS ASP THR TYR MET HIS TRP VAL LYS GLN
SEQRES 4 H 217 LYS PRO GLU GLN GLY LEU GLU TRP ILE ALA GLN ILE ASP
SEQRES 5 H 217 PRO ALA ASN GLY ASN THR LYS TYR ASP PRO LYS PHE GLN
SEQRES 6 H 217 GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR
SEQRES 7 H 217 ALA TYR LEU HIS LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 H 217 ALA VAL TYR TYR CYS ALA ALA ASP PRO PRO TYR TYR GLY
SEQRES 9 H 217 HIS GLY ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL
SEQRES 10 H 217 SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU
SEQRES 11 H 217 ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR
SEQRES 12 H 217 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL
SEQRES 13 H 217 THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL
SEQRES 14 H 217 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR
SEQRES 15 H 217 LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO
SEQRES 16 H 217 SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER
SEQRES 17 H 217 SER THR LYS VAL ASP LYS LYS ILE VAL
HET GEP L 212 24
HETNAM GEP N-METHYL-N-(PARA-GLUTARAMIDOPHENYL-ETHYL)-PIPERIDINIUM
HETNAM 2 GEP ION
FORMUL 3 GEP C19 H29 N2 O3 1+
FORMUL 4 HOH *232(H2 O)
HELIX 1 1 SER L 122 SER L 127 1 6
HELIX 2 2 ASP L 184 GLU L 187 1 4
SHEET 1 A 4 LEU L 4 SER L 7 0
SHEET 2 A 4 VAL L 19 ALA L 25 -1 N THR L 24 O THR L 5
SHEET 3 A 4 SER L 70 ILE L 75 -1 N ILE L 75 O VAL L 19
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 67 O SER L 70
SHEET 1 B 5 ILE L 10 ALA L 13 0
SHEET 2 B 5 THR L 102 ILE L 106 1 N LYS L 103 O MET L 11
SHEET 3 B 5 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 4 B 5 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85
SHEET 5 B 5 LYS L 45 ILE L 48 -1 N ILE L 48 O TRP L 35
SHEET 1 C 4 THR L 114 PHE L 118 0
SHEET 2 C 4 GLY L 129 ASN L 137 -1 N ASN L 137 O THR L 114
SHEET 3 C 4 MET L 175 THR L 182 -1 N LEU L 181 O ALA L 130
SHEET 4 C 4 VAL L 159 TRP L 163 -1 N SER L 162 O SER L 176
SHEET 1 D 4 SER L 153 ARG L 155 0
SHEET 2 D 4 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 D 4 SER L 191 HIS L 198 -1 N THR L 197 O ASN L 145
SHEET 4 D 4 ILE L 205 ASN L 210 -1 N PHE L 209 O TYR L 192
SHEET 1 E 4 GLN H 3 GLN H 6 0
SHEET 2 E 4 VAL H 18 SER H 25 -1 N SER H 25 O GLN H 3
SHEET 3 E 4 THR H 77 LEU H 82 -1 N LEU H 82 O VAL H 18
SHEET 4 E 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 F 6 GLU H 10 VAL H 12 0
SHEET 2 F 6 THR H 107 VAL H 111 1 N THR H 110 O GLU H 10
SHEET 3 F 6 ALA H 88 ALA H 94 -1 N TYR H 90 O THR H 107
SHEET 4 F 6 MET H 34 GLN H 39 -1 N GLN H 39 O VAL H 89
SHEET 5 F 6 LEU H 45 ASP H 52 -1 N ILE H 51 O MET H 34
SHEET 6 F 6 ASN H 56 TYR H 59 -1 N LYS H 58 O GLN H 50
SHEET 1 G 4 SER H 120 LEU H 124 0
SHEET 2 G 4 MET H 137 TYR H 147 -1 N LYS H 145 O SER H 120
SHEET 3 G 4 TYR H 185 PRO H 194 -1 N VAL H 193 O VAL H 138
SHEET 4 G 4 VAL H 171 THR H 173 -1 N HIS H 172 O SER H 190
SHEET 1 H 3 VAL H 152 TRP H 157 0
SHEET 2 H 3 VAL H 205 HIS H 212 -1 N ALA H 211 O THR H 153
SHEET 3 H 3 THR H 217 ILE H 223 -1 N ILE H 223 O VAL H 205
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.04
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.04
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.03
CISPEP 1 SER L 7 PRO L 8 0 -0.23
CISPEP 2 SER L 94 PRO L 95 0 0.11
CISPEP 3 TYR L 140 PRO L 141 0 -0.03
CISPEP 4 PHE H 148 PRO H 149 0 -0.26
CISPEP 5 GLU H 150 PRO H 151 0 -0.34
CISPEP 6 TRP H 199 PRO H 200 0 0.28
SITE 1 AC1 12 HIS H 35 ALA H 93 ASP H 95 PRO H 96
SITE 2 AC1 12 GLY H 100 HIS H 100A GLY H 100B ASP H 101
SITE 3 AC1 12 TYR L 36 LEU L 46 TYR L 49 TYR L 91
CRYST1 112.000 80.000 64.900 90.00 118.00 90.00 C 1 2 1 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 0.008929 0.000000 0.004747 0.00000
SCALE2 0.000000 0.012500 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017451 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
