HEADER LYASE/IMMUNE SYSTEM 08-NOV-00 1G6V
TITLE COMPLEX OF THE CAMELID HEAVY-CHAIN ANTIBODY FRAGMENT CAB-CA05 WITH
TITLE 2 BOVINE CARBONIC ANHYDRASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.2.1.1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ANTIBODY HEAVY CHAIN;
COMPND 7 CHAIN: K;
COMPND 8 FRAGMENT: CAB-CA05, VARIABLE DOMAIN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS;
SOURCE 7 ORGANISM_COMMON: ARABIAN CAMEL;
SOURCE 8 ORGANISM_TAXID: 9838;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANTIBODY, ANTIGEN, COMPLEX, IMMUNOGLOBULIN, LYASE-IMMUNE SYSTEM
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DESMYTER,K.DECANNIERE,S.MUYLDERMANS,L.WYNS
REVDAT 4 09-AUG-23 1G6V 1 REMARK LINK
REVDAT 3 24-FEB-09 1G6V 1 VERSN
REVDAT 2 05-APR-05 1G6V 1 JRNL
REVDAT 1 22-NOV-00 1G6V 0
JRNL AUTH A.DESMYTER,K.DECANNIERE,S.MUYLDERMANS,L.WYNS
JRNL TITL ANTIGEN SPECIFICITY AND HIGH AFFINITY BINDING PROVIDED BY
JRNL TITL 2 ONE SINGLE LOOP OF A CAMEL SINGLE-DOMAIN ANTIBODY.
JRNL REF J.BIOL.CHEM. V. 276 26285 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11342547
JRNL DOI 10.1074/JBC.M102107200
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER BASED CNS LIBRARIES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.50
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 10533
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) : 0.210
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 502
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 : 2988
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 0
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.359
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUPED ISOTROPIC
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 1G6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-98
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10533
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 26.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.34500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 1F2X, 1CA2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM CITRATE, PH 5.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 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+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
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 112.02500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.93000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.93000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.01250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.93000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.93000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 168.03750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.93000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.93000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.01250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.93000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.93000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 168.03750
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 112.02500
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 APPLY THE FOLLOWING TO CHAINS: A, K
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 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 LYS A 261
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 HIS A 17 -4.95 -54.69
REMARK 500 ALA A 23 1.33 -68.48
REMARK 500 PRO A 30 -168.68 -75.96
REMARK 500 PRO A 42 3.14 -65.16
REMARK 500 TYR A 51 30.97 -87.40
REMARK 500 HIS A 64 3.51 -150.17
REMARK 500 ALA A 65 -172.88 174.79
REMARK 500 LYS A 80 -155.53 -137.50
REMARK 500 LYS A 111 16.77 56.81
REMARK 500 VAL A 135 23.75 -78.66
REMARK 500 PRO A 138 -3.82 -57.97
REMARK 500 ASP A 139 -2.55 -141.50
REMARK 500 VAL A 150 150.85 -44.73
REMARK 500 VAL A 160 -70.14 -101.64
REMARK 500 ILE A 167 41.47 -142.96
REMARK 500 ASN A 178 91.88 57.19
REMARK 500 THR A 199 36.49 -88.97
REMARK 500 THR A 200 147.77 -173.18
REMARK 500 PRO A 201 138.47 -39.64
REMARK 500 CYS A 206 -10.47 -145.44
REMARK 500 THR A 208 65.09 -106.62
REMARK 500 TRP A 209 139.66 -33.81
REMARK 500 VAL A 223 -15.20 -48.94
REMARK 500 ARG A 227 33.22 -76.03
REMARK 500 ASN A 244 34.34 -150.51
REMARK 500 LYS A 252 -109.89 38.37
REMARK 500 ASN A 253 -83.74 -90.44
REMARK 500 ARG A 254 -151.54 22.99
REMARK 500 GLN A 255 139.07 163.96
REMARK 500 SER K 817 140.33 -177.40
REMARK 500 VAL K 829 -7.65 -49.46
REMARK 500 VAL K 848 -65.69 -95.67
REMARK 500 ASP K 860 -30.71 -37.63
REMARK 500 ASN K 872 -22.58 -35.86
REMARK 500 ASN K 875 67.16 39.93
REMARK 500 ALA K 890 -175.24 -179.98
REMARK 500 LEU K 908 64.91 68.47
REMARK 500 ARG K 909 54.50 -140.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 105.4
REMARK 620 3 HIS A 119 ND1 122.7 84.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F2X RELATED DB: PDB
REMARK 900 STRUCTURE OF THE UNCOMPLEXED ANTIBODY
DBREF 1G6V A 1 261 UNP P00921 CAH2_BOVIN 0 260
DBREF 1G6V K 801 926 PDB 1G6V 1G6V 801 926
SEQRES 1 A 260 MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES 2 A 260 GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES 3 A 260 ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES 4 A 260 TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES 5 A 260 GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES 6 A 260 PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES 7 A 260 LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES 8 A 260 GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES 9 A 260 SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES 10 A 260 LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES 11 A 260 GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES 12 A 260 GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES 13 A 260 GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES 14 A 260 GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES 15 A 260 LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES 16 A 260 SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES 17 A 260 ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES 18 A 260 VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES 19 A 260 GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES 20 A 260 GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
SEQRES 1 K 126 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES 2 K 126 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 K 126 TYR THR VAL SER THR TYR CYS MET GLY TRP PHE ARG GLN
SEQRES 4 K 126 ALA PRO GLY LYS GLU ARG GLU GLY VAL ALA THR ILE LEU
SEQRES 5 K 126 GLY GLY SER THR TYR TYR GLY ASP SER VAL LYS GLY ARG
SEQRES 6 K 126 PHE THR ILE SER GLN ASP ASN ALA LYS ASN THR VAL TYR
SEQRES 7 K 126 LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA ILE
SEQRES 8 K 126 TYR TYR CYS ALA GLY SER THR VAL ALA SER THR GLY TRP
SEQRES 9 K 126 CYS SER ARG LEU ARG PRO TYR ASP TYR HIS TYR ARG GLY
SEQRES 10 K 126 GLN GLY THR GLN VAL THR VAL SER SER
HET ZN A1001 1
HETNAM ZN ZINC ION
FORMUL 3 ZN ZN 2+
HELIX 1 1 HIS A 15 PHE A 20 1 6
HELIX 2 2 PRO A 21 GLY A 25 5 5
HELIX 3 3 LYS A 127 GLY A 129 5 3
HELIX 4 4 ASP A 130 VAL A 135 1 6
HELIX 5 5 LYS A 154 ASP A 162 1 9
HELIX 6 6 VAL A 163 LYS A 168 5 6
HELIX 7 7 ASP A 180 LEU A 185 5 6
HELIX 8 8 GLN A 222 ARG A 227 1 6
HELIX 9 9 LYS K 885 THR K 889 5 5
HELIX 10 10 SER K 901 SER K 906 1 6
HELIX 11 11 ARG K 909 TYR K 913 5 5
SHEET 1 A 2 ASP A 32 ILE A 33 0
SHEET 2 A 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 B16 LYS A 39 TYR A 40 0
SHEET 2 B16 LYS A 257 ALA A 258 1 N ALA A 258 O LYS A 39
SHEET 3 B16 TYR A 191 THR A 193 -1 O THR A 193 N LYS A 257
SHEET 4 B16 ILE A 210 LEU A 212 -1 O VAL A 211 N TRP A 192
SHEET 5 B16 LEU A 141 GLY A 151 1 O VAL A 143 N ILE A 210
SHEET 6 B16 ILE A 216 SER A 219 1 N ILE A 216 O PHE A 147
SHEET 7 B16 LEU A 141 GLY A 151 1 O PHE A 147 N ILE A 216
SHEET 8 B16 ALA A 116 ASN A 124 -1 O ALA A 116 N LEU A 148
SHEET 9 B16 TYR A 88 TRP A 97 -1 N ARG A 89 O TRP A 123
SHEET 10 B16 VAL A 78 GLY A 81 -1 N LEU A 79 O TYR A 88
SHEET 11 B16 LEU A 47 SER A 50 -1 O SER A 48 N LYS A 80
SHEET 12 B16 VAL A 78 GLY A 81 -1 N VAL A 78 O SER A 50
SHEET 13 B16 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 14 B16 PHE A 66 PHE A 70 -1 O PHE A 66 N PHE A 95
SHEET 15 B16 SER A 56 ASN A 61 -1 N LEU A 57 O GLU A 69
SHEET 16 B16 SER A 173 ALA A 174 -1 O ALA A 174 N ILE A 59
SHEET 1 C 4 GLN K 803 SER K 807 0
SHEET 2 C 4 SER K 817 SER K 825 -1 N SER K 821 O SER K 807
SHEET 3 C 4 VAL K 877 ASN K 882 -1 N VAL K 877 O CYS K 822
SHEET 4 C 4 PHE K 866 GLN K 870 -1 O THR K 867 N GLN K 880
SHEET 1 D 8 GLY K 810 GLN K 813 0
SHEET 2 D 8 THR K 920 SER K 925 1 O GLN K 921 N GLY K 810
SHEET 3 D 8 ALA K 890 GLY K 896 -1 O ALA K 890 N VAL K 922
SHEET 4 D 8 TYR K 915 ARG K 916 -1 O TYR K 915 N GLY K 896
SHEET 5 D 8 ALA K 890 GLY K 896 -1 N GLY K 896 O TYR K 915
SHEET 6 D 8 MET K 834 GLN K 839 -1 O GLY K 835 N ALA K 895
SHEET 7 D 8 GLU K 846 LEU K 852 -1 O GLU K 846 N ARG K 838
SHEET 8 D 8 SER K 855 TYR K 858 -1 O SER K 855 N LEU K 852
SSBOND 1 CYS K 822 CYS K 894 1555 1555 2.03
SSBOND 2 CYS K 833 CYS K 905 1555 1555 2.03
LINK NE2 HIS A 94 ZN ZN A1001 1555 1555 2.67
LINK NE2 HIS A 96 ZN ZN A1001 1555 1555 2.23
LINK ND1 HIS A 119 ZN ZN A1001 1555 1555 2.39
CISPEP 1 SER A 29 PRO A 30 0 -0.19
CISPEP 2 PRO A 201 PRO A 202 0 0.26
SITE 1 AC1 4 HIS A 94 HIS A 96 HIS A 119 THR A 199
CRYST1 83.860 83.860 224.050 90.00 90.00 90.00 P 41 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 0.011925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011925 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004463 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
