HEADER IMMUNOGLOBULIN 19-JAN-95 1FLR
TITLE 4-4-20 FAB FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-4-20 (IG*G2A=KAPPA=) FAB FRAGMENT;
COMPND 3 CHAIN: L;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 4-4-20 (IG*G2A=KAPPA=) FAB FRAGMENT;
COMPND 6 CHAIN: H
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 STRAIN: BALB/C;
SOURCE 6 VARIANT: BALB/CV;
SOURCE 7 CELL_LINE: 4-4-20 MURINE-MURINE HYBRIDOMA;
SOURCE 8 ORGAN: SPLEEN;
SOURCE 9 CELL: LYMPHOCYTE-PLASMA CELL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 STRAIN: BALB/C;
SOURCE 15 VARIANT: BALB/CV;
SOURCE 16 CELL_LINE: 4-4-20 MURINE-MURINE HYBRIDOMA;
SOURCE 17 ORGAN: SPLEEN;
SOURCE 18 CELL: LYMPHOCYTE-PLASMA CELL
KEYWDS IMMUNOGLOBULIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WHITLOW
REVDAT 4 13-JUL-11 1FLR 1 VERSN
REVDAT 3 24-FEB-09 1FLR 1 VERSN
REVDAT 2 01-APR-03 1FLR 1 JRNL
REVDAT 1 15-SEP-95 1FLR 0
JRNL AUTH M.WHITLOW,A.J.HOWARD,J.F.WOOD,E.W.VOSS JR.,K.D.HARDMAN
JRNL TITL 1.85 A STRUCTURE OF ANTI-FLUORESCEIN 4-4-20 FAB.
JRNL REF PROTEIN ENG. V. 8 749 1995
JRNL REFN ISSN 0269-2139
JRNL PMID 8637844
JRNL DOI 10.1093/PROTEIN/8.8.749
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.N.HERRON,X.HE,M.L.MASON,E.W.VOSS JUNIOR,A.B.EDMUNDSON
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF A FLUORESCEIN-FAB COMPLEX
REMARK 1 TITL 2 CRYSTALLIZED IN 2-METHYL-2,4-PENTANEDIOL
REMARK 1 REF PROTEINS V. 5 271 1989
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.L.GIBSON,J.N.HERRON,X.-M.HE,V.A.PATRICK,M.L.MASON,
REMARK 1 AUTH 2 J.-N.LIN,D.M.KRANZ,E.W.VOSS JUNIOR,A.B.EDMUNDSON
REMARK 1 TITL DIFFERENCES IN CRYSTAL PROPERTIES AND LIGAND AFFINITIES OF
REMARK 1 TITL 2 AN ANTIFLUORESCYL FAB (4-4-20) IN TWO SOLVENT SYSTEMS
REMARK 1 REF PROTEINS V. 3 155 1988
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.D.BEDZYK,L.S.JOHNSON,G.S.RIORDON,E.W.VOSS
REMARK 1 TITL COMPARISON OF VARIABLE REGION PRIMARY STRUCTURES WITHIN AN
REMARK 1 TITL 2 ANTI-FLUORESCEIN IDIOTYPE FAMILY
REMARK 1 REF J.BIOL.CHEM. V. 264 1565 1989
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26328
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 + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : NULL
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
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
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) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3350
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 290
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.017 ; 0.015
REMARK 3 ANGLE DISTANCE (A) : 0.037 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.047 ; 0.040
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.015 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.191 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.191 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.271 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.305 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 2.600 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 21.400; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 16.871; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 17.107; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 19.144; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 20.506; 2.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 RESIDUES CYS H 133 TO GLY H 138 ARE IN WEAK ELECTRON
REMARK 3 DENSITY. THERE IS A DISCONTINUITY IN THE ELECTION DENSITY
REMARK 3 MAP BETWEEN RESIDUES VAL H 132 AND CYS H 133. THE
REMARK 3 RESULTING COORDINATES, AS PRESENTED IN THIS ENTRY, CONTAIN
REMARK 3 TWO POSITIONS FOR N CYS H 133, ONE OF WHICH IS PROPERLY
REMARK 3 CONNECTED TO C VAL H 132 BUT QUITE DISTANT (5.58 ANGSTROMS)
REMARK 3 FROM CA CYS H 133. THE OTHER POSITION FOR N CYS H 133 IS
REMARK 3 PROPERLY CONNECTED TO CA H 133 BUT QUITE DISTANT (4.51
REMARK 3 ANGSTROMS) FROM C VAL H 132.
REMARK 4
REMARK 4 1FLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-88
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS-NICOLET X100
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XENGEN
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29963
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 70.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: 4580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 SER H 77
REMARK 465 LYS H 78
REMARK 465 GLY H 219
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 ARG L 24 CZ NH1 NH2
REMARK 470 ASP H 135 CG OD1 OD2
REMARK 470 THR H 136 OG1 CG2
REMARK 470 THR H 137 OG1 CG2
REMARK 470 GLY H 138 O
REMARK 470 GLU H 153 OE1 OE2
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 682 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH H 736 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH H 737 DISTANCE = 7.50 ANGSTROMS
REMARK 525 HOH H 774 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH H 775 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH H 776 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH H 784 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH H 790 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH H 792 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH H 793 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH H 794 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH H 804 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH H 805 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH H 806 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH H 808 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH H 815 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH H 820 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH H 825 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH H 837 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH H 856 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH L 623 DISTANCE = 5.58 ANGSTROMS
REMARK 525 HOH L 712 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH L 721 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH L 747 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH L 748 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH L 770 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH L 773 DISTANCE = 5.13 ANGSTROMS
REMARK 525 HOH L 841 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH L 842 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH L 863 DISTANCE = 9.36 ANGSTROMS
REMARK 525 HOH L 882 DISTANCE = 13.72 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLU L 600
DBREF 1FLR L 1 219 GB 1589925 AAB09710 1 219
DBREF 1FLR H 119 219 UNP P01865 GCAM_MOUSE 1 101
SEQADV 1FLR VAL L 2 GB 1589925 ILE 2 CONFLICT
SEQADV 1FLR THR L 7 GB 1589925 SER 7 CONFLICT
SEQADV 1FLR LEU L 29 GB 1589925 VAL 29 CONFLICT
SEQADV 1FLR ARG L 39 GB 1589925 GLU 39 CONFLICT
SEQADV 1FLR TYR L 41 GB 1589925 PHE 41 CONFLICT
SEQADV 1FLR VAL L 51 GB 1589925 LEU 51 CONFLICT
SEQADV 1FLR PHE L 92 GB 1589925 TYR 92 CONFLICT
SEQADV 1FLR SER L 94 GB 1589925 PHE 94 CONFLICT
SEQADV 1FLR SER L 96 GB 1589925 ALA 96 CONFLICT
SEQADV 1FLR THR L 97 GB 1589925 SER 97 CONFLICT
SEQADV 1FLR ASN L 217 GB 1589925 GLY 217 CONFLICT
SEQRES 1 L 219 ASP VAL VAL MET THR GLN THR PRO LEU SER LEU PRO VAL
SEQRES 2 L 219 SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER
SEQRES 3 L 219 GLN SER LEU VAL HIS SER ASN GLY ASN THR TYR LEU ARG
SEQRES 4 L 219 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO LYS VAL LEU
SEQRES 5 L 219 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP
SEQRES 6 L 219 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU
SEQRES 7 L 219 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR
SEQRES 8 L 219 PHE CYS SER GLN SER THR HIS VAL PRO TRP THR PHE GLY
SEQRES 9 L 219 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA
SEQRES 10 L 219 PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU
SEQRES 11 L 219 THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN
SEQRES 12 L 219 PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP
SEQRES 13 L 219 GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR
SEQRES 14 L 219 ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER
SEQRES 15 L 219 THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN
SEQRES 16 L 219 SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER
SEQRES 17 L 219 PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS
SEQRES 1 H 219 GLU VAL LYS LEU ASP GLU THR GLY GLY GLY LEU VAL GLN
SEQRES 2 H 219 PRO GLY ARG PRO MET LYS LEU SER CYS VAL ALA SER GLY
SEQRES 3 H 219 PHE THR PHE SER ASP TYR TRP MET ASN TRP VAL ARG GLN
SEQRES 4 H 219 SER PRO GLU LYS GLY LEU GLU TRP VAL ALA GLN ILE ARG
SEQRES 5 H 219 ASN LYS PRO TYR ASN TYR GLU THR TYR TYR SER ASP SER
SEQRES 6 H 219 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS
SEQRES 7 H 219 SER SER VAL TYR LEU GLN MET ASN ASN LEU ARG VAL GLU
SEQRES 8 H 219 ASP MET GLY ILE TYR TYR CYS THR GLY SER TYR TYR GLY
SEQRES 9 H 219 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER
SEQRES 10 H 219 SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU ALA
SEQRES 11 H 219 PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR LEU
SEQRES 12 H 219 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR
SEQRES 13 H 219 LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS
SEQRES 14 H 219 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU
SEQRES 15 H 219 SER SER SER VAL THR VAL THR SER SER THR TRP PRO SER
SEQRES 16 H 219 GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SER
SEQRES 17 H 219 THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY
HET FLU L 600 25
HETNAM FLU 2-(6-HYDROXY-3-OXO-3H-XANTHEN-9-YL)-BENZOIC ACID
HETSYN FLU FLUORESCEIN
FORMUL 3 FLU C20 H12 O5
FORMUL 4 HOH *290(H2 O)
HELIX 1 1 ALA L 85 ASP L 87 5 3
HELIX 2 2 SER L 127 SER L 132 1 6
HELIX 3 3 LYS L 188 ARG L 193 1 6
HELIX 4 4 PHE H 29 ASP H 31 5 3
HELIX 5 5 LYS H 54 TYR H 56 5 3
HELIX 6 6 ASP H 64 VAL H 66 5 3
HELIX 7 7 VAL H 90 ASP H 92 5 3
HELIX 8 8 ASN H 160 GLY H 162 5 3
HELIX 9 9 PRO H 205 SER H 207 5 3
SHEET 1 A 4 THR L 5 THR L 7 0
SHEET 2 A 4 ALA L 19 ARG L 24 -1 N ARG L 24 O THR L 5
SHEET 3 A 4 ASP L 75 ILE L 80 -1 N ILE L 80 O ALA L 19
SHEET 4 A 4 PHE L 67 SER L 72 -1 N SER L 72 O ASP L 75
SHEET 1 B 5 SER L 10 VAL L 13 0
SHEET 2 B 5 THR L 107 ILE L 111 1 N LYS L 108 O LEU L 11
SHEET 3 B 5 GLY L 89 GLN L 95 -1 N TYR L 91 O THR L 107
SHEET 4 B 5 LEU L 38 GLN L 43 -1 N GLN L 43 O VAL L 90
SHEET 5 B 5 LYS L 50 ILE L 53 -1 N ILE L 53 O TRP L 40
SHEET 1 C 4 THR L 119 PHE L 123 0
SHEET 2 C 4 GLY L 134 ASN L 142 -1 N ASN L 142 O THR L 119
SHEET 3 C 4 MET L 180 THR L 187 -1 N LEU L 186 O ALA L 135
SHEET 4 C 4 VAL L 164 TRP L 168 -1 N SER L 167 O SER L 181
SHEET 1 D 3 ASN L 150 ILE L 155 0
SHEET 2 D 3 SER L 196 THR L 202 -1 N THR L 202 O ASN L 150
SHEET 3 D 3 ILE L 210 ASN L 215 -1 N PHE L 214 O TYR L 197
SHEET 1 E 3 MET H 18 VAL H 23 0
SHEET 2 E 3 SER H 80 MET H 85 -1 N MET H 85 O MET H 18
SHEET 3 E 3 PHE H 70 ASP H 75 -1 N ASP H 75 O SER H 80
SHEET 1 F 5 THR H 112 VAL H 114 0
SHEET 2 F 5 GLY H 94 SER H 101 -1 N TYR H 96 O THR H 112
SHEET 3 F 5 TRP H 33 GLN H 39 -1 N GLN H 39 O ILE H 95
SHEET 4 F 5 LEU H 45 ILE H 51 -1 N ILE H 51 O MET H 34
SHEET 5 F 5 THR H 60 TYR H 62 -1 N TYR H 61 O GLN H 50
SHEET 1 G 2 THR H 99 TYR H 102 0
SHEET 2 G 2 MET H 105 TRP H 108 -1 N TYR H 107 O GLY H 100
SHEET 1 H 4 SER H 125 LEU H 129 0
SHEET 2 H 4 THR H 142 LYS H 148 -1 N LYS H 148 O SER H 125
SHEET 3 H 4 LEU H 182 THR H 187 -1 N VAL H 186 O LEU H 143
SHEET 4 H 4 VAL H 168 PHE H 171 -1 N PHE H 171 O SER H 183
SHEET 1 I 3 THR H 156 TRP H 159 0
SHEET 2 I 3 ILE H 198 HIS H 204 -1 N ALA H 203 O THR H 156
SHEET 3 I 3 THR H 209 ILE H 215 -1 N ILE H 215 O ILE H 198
SHEET 1 J 2 VAL H 174 GLN H 176 0
SHEET 2 J 2 LEU H 179 THR H 181 -1 N THR H 181 O VAL H 174
SSBOND 1 CYS L 23 CYS L 93 1555 1555 1.96
SSBOND 2 CYS L 139 CYS L 199 1555 1555 1.95
SSBOND 3 CYS L 219 CYS H 133 1555 1555 2.07
SSBOND 4 CYS H 22 CYS H 98 1555 1555 2.02
SSBOND 5 CYS H 145 CYS H 200 1555 1555 2.02
CISPEP 1 THR L 7 PRO L 8 0 -1.93
CISPEP 2 VAL L 99 PRO L 100 0 0.90
CISPEP 3 TYR L 145 PRO L 146 0 2.36
CISPEP 4 PHE H 151 PRO H 152 0 1.20
CISPEP 5 TRP H 193 PRO H 194 0 0.57
SITE 1 AC1 11 TRP H 33 TYR H 56 TYR H 102 TYR H 103
SITE 2 AC1 11 GLY H 104 HOH H 677 HIS L 31 TYR L 37
SITE 3 AC1 11 ARG L 39 SER L 96 TRP L 101
CRYST1 42.750 43.870 58.170 95.15 86.85 98.01 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 0.023392 0.003292 -0.001018 0.00000
SCALE2 0.000000 0.023019 0.001918 0.00000
SCALE3 0.000000 0.000000 0.017277 0.00000
(ATOM LINES ARE NOT SHOWN.)
END