HEADER IMMUNOGLOBULIN 26-APR-99 1CK0
TITLE ANTI-ANTI-IDIOTYPIC ANTIBODY AGAINST HUMAN ANGIOTENSIN II, UNLIGANDED
TITLE 2 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (IGG1-KAPPA ANTIBODY 131 (LIGHT CHAIN));
COMPND 3 CHAIN: L;
COMPND 4 FRAGMENT: FAB;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PROTEIN (IGG1-KAPPA ANTIBODY 131 (HEAVY CHAIN));
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 CELL: HYBRIDOMA;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 8 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 9 ORGANISM_TAXID: 10090;
SOURCE 10 CELL: HYBRIDOMA
KEYWDS IMMUNOGLOBULIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.PAN,L.M.AMZEL
REVDAT 3 27-DEC-23 1CK0 1 REMARK
REVDAT 2 24-FEB-09 1CK0 1 VERSN
REVDAT 1 05-AUG-03 1CK0 0
JRNL AUTH Y.H.PAN,K.H.LEE,M.LI,P.RONCO,L.M.AMZEL
JRNL TITL STRUCTURES OF ANGIOTENSIN II AND A PHAGE-DISPLAY SELECTED
JRNL TITL 2 CYCLIC PEPTIDE IN COMPLEX WITH FAB131: MAKING ANGIOTENSIN II
JRNL TITL 3 ANALOGS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.0
REMARK 3 NUMBER OF REFLECTIONS : 14063
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) : 0.192
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 677
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 : 3291
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.00
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.450
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.210
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM11.WAT
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH11.WAT
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: GLY H131 - SER H138:
REMARK 3 THESE EIGHT RESIDUES WERE COMPLETELY DISORDERED IN THE
REMARK 3 STRUCTURE.
REMARK 3
REMARK 3 TER
REMARK 3 ASN: THE SITE OF THE PROTEOLYSIS AT THE C TERMINUS OF THE
REMARK 3 HEAVY IS UNDEFINED, SO IT IS NOT KNOWN WEATHER THERE ARE
REMARK 3 RESIDUES MISSING THERE.
REMARK 4
REMARK 4 1CK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000939.
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 : 7.5
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16538
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 71.03000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.92500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.92500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 106.54500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.92500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.92500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 35.51500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.92500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.92500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 106.54500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.92500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.92500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 35.51500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 71.03000
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: 3110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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 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 GLY H 131
REMARK 465 SER H 132
REMARK 465 ALA H 133
REMARK 465 ALA H 134
REMARK 465 GLN H 135
REMARK 465 THR H 136
REMARK 465 ASN H 137
REMARK 465 SER H 138
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 ALA L 51 -21.68 63.52
REMARK 500 SER L 52 -1.92 -151.05
REMARK 500 ASP L 60 4.90 -64.93
REMARK 500 ALA L 84 -176.81 -177.53
REMARK 500 LEU L 94 -147.94 63.21
REMARK 500 ARG L 107 -168.84 -123.91
REMARK 500 ASN L 137 76.77 47.37
REMARK 500 ASP L 150 -27.23 75.58
REMARK 500 LYS L 168 -70.21 -79.94
REMARK 500 ASN L 189 -76.63 -102.81
REMARK 500 THR L 199 24.74 -76.47
REMARK 500 ASP H 65 -3.52 69.70
REMARK 500 GLU H 102 -122.17 -98.01
REMARK 500 ASP H 105 -72.76 -62.34
REMARK 500 PHE H 150 136.82 -174.96
REMARK 500 SER H 160 0.61 56.66
REMARK 500 PRO H 191 11.87 -58.25
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 TYR L 139 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CK0 L 1 210 PDB 1CK0 1CK0 1 210
DBREF 1CK0 H 1 216 PDB 1CK0 1CK0 1 216
SEQRES 1 L 216 ASP ILE GLN LEU THR GLN SER PRO SER SER LEU ALA VAL
SEQRES 2 L 216 SER ALA GLY GLU LYS VAL THR MET ASN CYS LYS SER SER
SEQRES 3 L 216 GLN ASN LEU LEU HIS SER ILE THR ARG LYS ASN TYR LEU
SEQRES 4 L 216 ALA TRP TYR ARG GLN LYS PRO GLY GLN SER PRO LYS LEU
SEQRES 5 L 216 LEU ILE TYR TRP ALA SER THR ARG GLY SER GLY VAL PRO
SEQRES 6 L 216 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR
SEQRES 7 L 216 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA VAL
SEQRES 8 L 216 TYR TYR CYS LYS GLN SER TYR ASN LEU TYR THR PHE GLY
SEQRES 9 L 216 GLY 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 ARG 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 219 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 219 PRO ARG GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 219 PHE THR PHE ASN THR ASP ALA MET ASN TRP VAL ARG GLN
SEQRES 4 H 219 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ARG ILE ARG
SEQRES 5 H 219 SER LYS GLY PHE ASN PHE ALA THR TYR TYR ALA ASP SER
SEQRES 6 H 219 VAL ARG ASP ARG PHE THR ILE SER ARG ASP ASP SER GLN
SEQRES 7 H 219 SER MET LEU TYR LEU GLN MET ASN ASN LEU LYS THR GLU
SEQRES 8 H 219 ASP THR GLY ILE TYR TYR CYS VAL ARG GLY ARG ASP GLY
SEQRES 9 H 219 GLU ALA MET ASP TYR TRP GLY GLN GLY THR THR LEU THR
SEQRES 10 H 219 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 H 219 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL
SEQRES 12 H 219 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 H 219 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY
SEQRES 14 H 219 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR
SEQRES 15 H 219 THR LEU SER SER SER VAL THR VAL PRO SER SER PRO ARG
SEQRES 16 H 219 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 H 219 SER SER THR LYS VAL ASP LYS LYS ILE VAL ASN
FORMUL 3 HOH *33(H2 O)
HELIX 1 1 ALA L 80 ASP L 82 5 3
HELIX 2 2 SER L 121 SER L 126 1 6
HELIX 3 3 LYS L 182 GLU L 186 1 5
HELIX 4 4 LYS H 52B PHE H 53 5 3
HELIX 5 5 THR H 87 ASP H 89 5 3
HELIX 6 6 ASN H 159 GLY H 161 5 3
HELIX 7 7 PRO H 204 SER H 206 5 3
SHEET 1 A 4 LEU L 4 SER L 7 0
SHEET 2 A 4 VAL L 19 SER L 25 -1 N LYS L 24 O THR L 5
SHEET 3 A 4 ASP 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 ASP L 70
SHEET 1 B 5 SER L 10 VAL L 13 0
SHEET 2 B 5 THR L 101 ILE L 105 1 N LYS L 102 O LEU L 11
SHEET 3 B 5 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 101
SHEET 4 B 5 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL 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 113 PHE L 117 0
SHEET 2 C 4 GLY L 128 ASN L 136 -1 N ASN L 136 O THR L 113
SHEET 3 C 4 MET L 174 THR L 181 -1 N LEU L 180 O ALA L 129
SHEET 4 C 4 VAL L 158 TRP L 162 -1 N SER L 161 O SER L 175
SHEET 1 D 4 SER L 152 ARG L 154 0
SHEET 2 D 4 ASN L 144 ILE L 149 -1 N ILE L 149 O SER L 152
SHEET 3 D 4 SER L 190 THR L 196 -1 N THR L 196 O ASN L 144
SHEET 4 D 4 ILE L 204 ASN L 209 -1 N PHE L 208 O TYR L 191
SHEET 1 E 4 GLN H 3 SER H 7 0
SHEET 2 E 4 LEU H 18 SER H 25 -1 N SER H 25 O GLN H 3
SHEET 3 E 4 MET H 77 MET H 82 -1 N MET H 82 O LEU H 18
SHEET 4 E 4 PHE H 67 ASP H 72 -1 N ASP H 72 O MET H 77
SHEET 1 F 6 GLY H 10 VAL H 12 0
SHEET 2 F 6 THR H 111 VAL H 115 1 N THR H 114 O GLY H 10
SHEET 3 F 6 GLY H 91 ARG H 97 -1 N TYR H 93 O THR H 111
SHEET 4 F 6 MET H 34 GLN H 39 -1 N GLN H 39 O ILE H 92
SHEET 5 F 6 LEU H 45 ILE H 51 -1 N ILE H 51 O MET H 34
SHEET 6 F 6 THR H 57 TYR H 59 -1 N TYR H 58 O ARG H 50
SHEET 1 G 4 SER H 124 LEU H 128 0
SHEET 2 G 4 VAL H 140 TYR H 149 -1 N LYS H 147 O SER H 124
SHEET 3 G 4 TYR H 179 VAL H 187 -1 N VAL H 187 O VAL H 140
SHEET 4 G 4 VAL H 167 THR H 169 -1 N HIS H 168 O SER H 184
SHEET 1 H 3 THR H 155 TRP H 158 0
SHEET 2 H 3 THR H 198 HIS H 203 -1 N ALA H 202 O THR H 155
SHEET 3 H 3 THR H 208 LYS H 213 -1 N LYS H 212 O CYS H 199
SHEET 1 I 2 VAL H 173 GLN H 175 0
SHEET 2 I 2 LEU H 178 THR H 180 -1 N THR H 180 O VAL H 173
SHEET 1 J 2 VAL H 96 GLY H 98 0
SHEET 2 J 2 MET H 104 TRP H 107 -1 N TYR H 106 O ARG H 97
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 2 CYS L 133 CYS L 193 1555 1555 2.03
SSBOND 3 CYS H 22 CYS H 95 1555 1555 2.02
SSBOND 4 CYS H 144 CYS H 199 1555 1555 2.04
CISPEP 1 SER L 7 PRO L 8 0 -0.41
CISPEP 2 TYR L 139 PRO L 140 0 0.19
CISPEP 3 PHE H 150 PRO H 151 0 -0.26
CISPEP 4 GLU H 152 PRO H 153 0 -0.09
CISPEP 5 ARG H 192 PRO H 193 0 0.19
CRYST1 83.850 83.850 142.060 90.00 90.00 90.00 P 43 21 2 8
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 0.011926 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011926 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007039 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
