HEADER HYDROLASE, IMMUNE SYSTEM 01-FEB-02 1KXQ
TITLE CAMELID VHH DOMAIN IN COMPLEX WITH PORCINE PANCREATIC ALPHA-AMYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND 5 EC: 3.2.1.1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ANTIBODY VHH FRAGMENT CABAMD9;
COMPND 8 CHAIN: E, F, G, H;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 OTHER_DETAILS: PANCREATIC ENZYME;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: CAMELUS DROMEDARIUS;
SOURCE 8 ORGANISM_COMMON: ARABIAN CAMEL;
SOURCE 9 ORGANISM_TAXID: 9838;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: WK6;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA 8 BETA 8, BETA BARREL, HYDROLASE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DESMYTER,S.SPINELLI,F.PAYAN,M.LAUWEREYS,L.WYNS,S.MUYLDERMANS,
AUTHOR 2 C.CAMBILLAU
REVDAT 6 16-AUG-23 1KXQ 1 REMARK LINK
REVDAT 5 24-JAN-18 1KXQ 1 JRNL
REVDAT 4 24-FEB-09 1KXQ 1 VERSN
REVDAT 3 01-APR-03 1KXQ 1 JRNL
REVDAT 2 14-AUG-02 1KXQ 1 JRNL
REVDAT 1 19-JUN-02 1KXQ 0
JRNL AUTH A.DESMYTER,S.SPINELLI,F.PAYAN,M.LAUWEREYS,L.WYNS,
JRNL AUTH 2 S.MUYLDERMANS,C.CAMBILLAU
JRNL TITL THREE CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC
JRNL TITL 2 ALPHA-AMYLASE. INHIBITION AND VERSATILITY OF BINDING
JRNL TITL 3 TOPOLOGY.
JRNL REF J.BIOL.CHEM. V. 277 23645 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11960990
JRNL DOI 10.1074/JBC.M202327200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.LAUWEREYS,M.ARBABI GHAHROUDI,A.DESMYTER,J.KINNE,W.HOLZER,
REMARK 1 AUTH 2 E.DE GENST,L.WYNS,S.MUYLDERMANS
REMARK 1 TITL POTENT ENZYME INHIBITORS DERIVED FROM DROMEDARY HEAVY-CHAIN
REMARK 1 TITL 2 ANTIBODIES.
REMARK 1 REF EMBO J. V. 17 3512 1998
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/17.13.3512
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.QIAN,R.HASER,F.PAYAN
REMARK 1 TITL STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG PANCREATIC
REMARK 1 TITL 2 ALPHA-AMYLASE AT 2.1 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 231 785 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1993.1326
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1735909.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 317086
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) : 0.197
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9426
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 29934
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 913
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 2807
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.49000
REMARK 3 B22 (A**2) : -1.66000
REMARK 3 B33 (A**2) : -1.83000
REMARK 3 B12 (A**2) : -2.22000
REMARK 3 B13 (A**2) : -2.35000
REMARK 3 B23 (A**2) : 0.85000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.16
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.920
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) : 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 : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 48.68
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KXQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000015445.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID09
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
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 : 383526
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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: PDB ENTRY 1JFH, PDB ENTRY 1QD0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE BUFFER 0.8 M, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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, 2, 3, 4
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, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 350
REMARK 350 BIOMOLECULE: 4
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: 2360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E
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 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 SER E 120 OG
REMARK 470 SER F 120 OG
REMARK 470 SER G 120 OG
REMARK 470 SER H 120 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 352 OD1 ASN H 97 1.75
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 CYS A 70 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU A 293 CA - CB - CG ANGL. DEV. = -16.2 DEGREES
REMARK 500 CYS B 70 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG C 72 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 CYS D 70 CA - CB - SG ANGL. DEV. = 7.4 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 A 31 -57.52 -146.04
REMARK 500 MET A 102 -153.47 -108.19
REMARK 500 VAL A 163 51.50 36.61
REMARK 500 ASP A 317 58.98 -118.55
REMARK 500 SER A 414 -105.59 -132.25
REMARK 500 ASP A 433 32.51 -87.52
REMARK 500 ASN A 460 49.88 -97.21
REMARK 500 PRO A 486 47.01 -76.66
REMARK 500 TYR B 31 -57.24 -149.75
REMARK 500 SER B 66 -179.57 -172.60
REMARK 500 MET B 102 -156.98 -109.77
REMARK 500 VAL B 163 47.48 37.66
REMARK 500 SER B 414 -109.71 -132.91
REMARK 500 ASP B 433 35.49 -90.50
REMARK 500 ASN B 460 40.35 -105.43
REMARK 500 PRO B 486 38.83 -74.71
REMARK 500 TYR C 31 -56.42 -142.82
REMARK 500 MET C 102 -155.88 -109.34
REMARK 500 VAL C 163 49.12 37.50
REMARK 500 ASP C 317 59.65 -115.43
REMARK 500 THR C 376 4.74 82.03
REMARK 500 SER C 414 -110.38 -133.91
REMARK 500 ASP C 433 32.79 -88.13
REMARK 500 PRO C 486 45.43 -79.12
REMARK 500 TYR D 31 -57.48 -141.20
REMARK 500 MET D 102 -145.14 -107.70
REMARK 500 VAL D 163 47.82 37.12
REMARK 500 SER D 414 -109.61 -129.54
REMARK 500 ASP D 433 37.26 -93.16
REMARK 500 PRO D 486 41.14 -77.99
REMARK 500 ASN E 97 16.76 -146.64
REMARK 500 ARG E 100 72.84 -104.91
REMARK 500 VAL F 2 99.90 -179.95
REMARK 500 PRO F 38 107.21 -35.30
REMARK 500 ASN F 97 21.73 -145.81
REMARK 500 ARG F 100 72.43 -119.49
REMARK 500 VAL G 2 103.05 -168.87
REMARK 500 ASN G 97 20.90 -144.42
REMARK 500 ARG G 100 74.15 -105.28
REMARK 500 ASN H 97 19.37 -146.62
REMARK 500 ARG H 100 72.62 -111.15
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 CA A4001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 100 OD1
REMARK 620 2 ARG A 158 O 157.4
REMARK 620 3 ASP A 167 OD1 79.4 120.5
REMARK 620 4 ASP A 167 OD2 126.7 75.8 52.6
REMARK 620 5 HIS A 201 O 74.9 82.7 138.4 157.0
REMARK 620 6 HOH A4014 O 71.5 120.9 76.2 75.4 123.8
REMARK 620 7 HOH A4094 O 102.1 76.3 73.5 86.5 80.6 149.6
REMARK 620 8 HOH A4125 O 103.1 70.3 137.2 98.9 81.0 64.8 143.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B4003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 100 OD1
REMARK 620 2 ARG B 158 O 154.6
REMARK 620 3 ASP B 167 OD1 82.4 120.5
REMARK 620 4 ASP B 167 OD2 128.4 77.0 53.0
REMARK 620 5 HIS B 201 O 73.7 81.1 139.9 157.6
REMARK 620 6 HOH B4012 O 98.6 74.2 133.5 95.9 82.5
REMARK 620 7 HOH B4030 O 100.2 79.2 71.4 89.7 81.5 150.7
REMARK 620 8 HOH B4307 O 72.2 121.8 74.6 71.9 125.1 62.0 145.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C4005 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 100 OD1
REMARK 620 2 ARG C 158 O 155.9
REMARK 620 3 ASP C 167 OD1 80.9 121.5
REMARK 620 4 ASP C 167 OD2 127.6 76.4 52.6
REMARK 620 5 HIS C 201 O 73.8 82.5 139.2 157.8
REMARK 620 6 HOH C4022 O 70.6 121.1 74.5 74.5 123.6
REMARK 620 7 HOH C4047 O 103.1 77.7 73.3 86.7 81.9 147.8
REMARK 620 8 HOH C4060 O 99.8 71.0 136.0 99.1 80.4 64.8 145.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D4007 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN D 100 OD1
REMARK 620 2 ARG D 158 O 156.5
REMARK 620 3 ASP D 167 OD2 126.7 76.8
REMARK 620 4 ASP D 167 OD1 80.8 119.6 52.5
REMARK 620 5 HIS D 201 O 75.9 80.7 156.9 140.4
REMARK 620 6 HOH D4016 O 72.4 121.2 73.1 76.7 124.1
REMARK 620 7 HOH D4038 O 101.6 72.3 97.9 136.9 79.7 63.6
REMARK 620 8 HOH D4041 O 99.8 78.4 88.4 70.5 82.3 147.2 147.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 4005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 4007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4008
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KXT RELATED DB: PDB
REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC ALPHA-AMYLASE
REMARK 900 RELATED ID: 1KXV RELATED DB: PDB
REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC ALPHA-AMYLASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DISCREPANCY BETWEEN THE SEQUENCE OF THIS
REMARK 999 ENTRY AND THE DATABASE REFERENCE IS EXPLAINED
REMARK 999 IN REFERENCE 2 GIVEN ABOVE.
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE
REMARK 999 FOR THE ANTIBODY VHH FRAGMENT CABAMD9, CHAINS
REMARK 999 E, F, G, AND H, WAS NOT AVAILABLE AT THE TIME
REMARK 999 OF PROCESSING.
DBREF 1KXQ A 1 496 UNP P00690 AMYP_PIG 1 496
DBREF 1KXQ B 1 496 UNP P00690 AMYP_PIG 1 496
DBREF 1KXQ C 1 496 UNP P00690 AMYP_PIG 1 496
DBREF 1KXQ D 1 496 UNP P00690 AMYP_PIG 1 496
DBREF 1KXQ E 1 120 PDB 1KXQ 1KXQ 1 120
DBREF 1KXQ F 1 120 PDB 1KXQ 1KXQ 1 120
DBREF 1KXQ G 1 120 PDB 1KXQ 1KXQ 1 120
DBREF 1KXQ H 1 120 PDB 1KXQ 1KXQ 1 120
SEQADV 1KXQ LYS A 243 UNP P00690 GLN 243 SEE REMARK 999
SEQADV 1KXQ SER A 310 UNP P00690 ALA 310 SEE REMARK 999
SEQADV 1KXQ ILE A 323 UNP P00690 VAL 323 SEE REMARK 999
SEQADV 1KXQ GLN A 404 UNP P00690 GLU 404 SEE REMARK 999
SEQADV 1KXQ LYS B 243 UNP P00690 GLN 243 SEE REMARK 999
SEQADV 1KXQ SER B 310 UNP P00690 ALA 310 SEE REMARK 999
SEQADV 1KXQ ILE B 323 UNP P00690 VAL 323 SEE REMARK 999
SEQADV 1KXQ GLN B 404 UNP P00690 GLU 404 SEE REMARK 999
SEQADV 1KXQ LYS C 243 UNP P00690 GLN 243 SEE REMARK 999
SEQADV 1KXQ SER C 310 UNP P00690 ALA 310 SEE REMARK 999
SEQADV 1KXQ ILE C 323 UNP P00690 VAL 323 SEE REMARK 999
SEQADV 1KXQ GLN C 404 UNP P00690 GLU 404 SEE REMARK 999
SEQADV 1KXQ LYS D 243 UNP P00690 GLN 243 SEE REMARK 999
SEQADV 1KXQ SER D 310 UNP P00690 ALA 310 SEE REMARK 999
SEQADV 1KXQ ILE D 323 UNP P00690 VAL 323 SEE REMARK 999
SEQADV 1KXQ GLN D 404 UNP P00690 GLU 404 SEE REMARK 999
SEQRES 1 A 496 GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES 2 A 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 A 496 GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES 4 A 496 VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR
SEQRES 5 A 496 ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 A 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES 7 A 496 PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 A 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 A 496 SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES 10 A 496 TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO
SEQRES 11 A 496 TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 A 496 ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES 13 A 496 VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES 14 A 496 LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES 15 A 496 LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 A 496 ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 A 496 ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES 18 A 496 PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES 19 A 496 ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR
SEQRES 20 A 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 A 496 LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES 22 A 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 A 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 A 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE
SEQRES 25 A 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL
SEQRES 26 A 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 A 496 MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES 28 A 496 GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES 29 A 496 GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES 30 A 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES 31 A 496 ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 A 496 GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES 33 A 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 A 496 ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES 35 A 496 GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 A 496 ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES 37 A 496 VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES 38 A 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 A 496 LYS LEU
SEQRES 1 B 496 GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES 2 B 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 B 496 GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES 4 B 496 VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR
SEQRES 5 B 496 ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 B 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES 7 B 496 PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 B 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 B 496 SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES 10 B 496 TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO
SEQRES 11 B 496 TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 B 496 ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES 13 B 496 VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES 14 B 496 LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES 15 B 496 LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 B 496 ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 B 496 ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES 18 B 496 PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES 19 B 496 ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR
SEQRES 20 B 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 B 496 LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES 22 B 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 B 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 B 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE
SEQRES 25 B 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL
SEQRES 26 B 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 B 496 MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES 28 B 496 GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES 29 B 496 GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES 30 B 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES 31 B 496 ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 B 496 GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES 33 B 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 B 496 ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES 35 B 496 GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 B 496 ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES 37 B 496 VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES 38 B 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 B 496 LYS LEU
SEQRES 1 C 496 GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES 2 C 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 C 496 GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES 4 C 496 VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR
SEQRES 5 C 496 ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 C 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES 7 C 496 PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 C 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 C 496 SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES 10 C 496 TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO
SEQRES 11 C 496 TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 C 496 ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES 13 C 496 VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES 14 C 496 LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES 15 C 496 LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 C 496 ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 C 496 ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES 18 C 496 PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES 19 C 496 ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR
SEQRES 20 C 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 C 496 LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES 22 C 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 C 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 C 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE
SEQRES 25 C 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL
SEQRES 26 C 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 C 496 MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES 28 C 496 GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES 29 C 496 GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES 30 C 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES 31 C 496 ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 C 496 GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES 33 C 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 C 496 ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES 35 C 496 GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 C 496 ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES 37 C 496 VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES 38 C 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 C 496 LYS LEU
SEQRES 1 D 496 GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES 2 D 496 VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES 3 D 496 GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES 4 D 496 VAL GLN VAL SER PRO PRO ASN GLU ASN ILE VAL VAL THR
SEQRES 5 D 496 ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES 6 D 496 SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES 7 D 496 PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES 8 D 496 ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES 9 D 496 SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES 10 D 496 TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO
SEQRES 11 D 496 TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES 12 D 496 ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES 13 D 496 VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES 14 D 496 LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES 15 D 496 LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES 16 D 496 ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES 17 D 496 ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES 18 D 496 PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES 19 D 496 ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR
SEQRES 20 D 496 PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES 21 D 496 LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES 22 D 496 MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES 23 D 496 MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES 24 D 496 ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE
SEQRES 25 D 496 LEU THR PHE TRP ASP ALA ARG LEU TYR LYS ILE ALA VAL
SEQRES 26 D 496 GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES 27 D 496 MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES 28 D 496 GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES 29 D 496 GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES 30 D 496 CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES 31 D 496 ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES 32 D 496 GLN PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES 33 D 496 VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES 34 D 496 ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES 35 D 496 GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES 36 D 496 ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES 37 D 496 VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES 38 D 496 SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES 39 D 496 LYS LEU
SEQRES 1 E 120 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES 2 E 120 ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR
SEQRES 3 E 120 TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY
SEQRES 4 E 120 LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR
SEQRES 5 E 120 GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE
SEQRES 6 E 120 THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU
SEQRES 7 E 120 GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR
SEQRES 8 E 120 TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP
SEQRES 9 E 120 GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR
SEQRES 10 E 120 VAL SER SER
SEQRES 1 F 120 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES 2 F 120 ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR
SEQRES 3 F 120 TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY
SEQRES 4 F 120 LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR
SEQRES 5 F 120 GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE
SEQRES 6 F 120 THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU
SEQRES 7 F 120 GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR
SEQRES 8 F 120 TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP
SEQRES 9 F 120 GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR
SEQRES 10 F 120 VAL SER SER
SEQRES 1 G 120 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES 2 G 120 ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR
SEQRES 3 G 120 TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY
SEQRES 4 G 120 LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR
SEQRES 5 G 120 GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE
SEQRES 6 G 120 THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU
SEQRES 7 G 120 GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR
SEQRES 8 G 120 TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP
SEQRES 9 G 120 GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR
SEQRES 10 G 120 VAL SER SER
SEQRES 1 H 120 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN
SEQRES 2 H 120 ALA GLY GLY SER LEU SER LEU SER CYS ALA ALA SER THR
SEQRES 3 H 120 TYR THR ASP THR VAL GLY TRP PHE ARG GLN ALA PRO GLY
SEQRES 4 H 120 LYS GLU ARG GLU GLY VAL ALA ALA ILE TYR ARG ARG THR
SEQRES 5 H 120 GLY TYR THR TYR SER ALA ASP SER VAL LYS GLY ARG PHE
SEQRES 6 H 120 THR LEU SER GLN ASP ASN ASN LYS ASN THR VAL TYR LEU
SEQRES 7 H 120 GLN MET ASN SER LEU LYS PRO GLU ASP THR GLY ILE TYR
SEQRES 8 H 120 TYR CYS ALA THR GLY ASN SER VAL ARG LEU ALA SER TRP
SEQRES 9 H 120 GLU GLY TYR PHE TYR TRP GLY GLN GLY THR GLN VAL THR
SEQRES 10 H 120 VAL SER SER
HET CA A4001 1
HET CL A4002 1
HET CA B4003 1
HET CL B4004 1
HET CA C4005 1
HET CL C4006 1
HET CA D4007 1
HET CL D4008 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 9 CA 4(CA 2+)
FORMUL 10 CL 4(CL 1-)
FORMUL 17 HOH *2807(H2 O)
HELIX 1 1 ARG A 20 TYR A 31 1 12
HELIX 2 2 PRO A 57 GLN A 63 5 7
HELIX 3 3 ASN A 75 VAL A 89 1 15
HELIX 4 4 ASN A 120 ARG A 124 5 5
HELIX 5 5 SER A 132 LYS A 140 5 9
HELIX 6 6 ASP A 153 CYS A 160 1 8
HELIX 7 7 LYS A 172 GLY A 190 1 19
HELIX 8 8 ALA A 198 MET A 202 5 5
HELIX 9 9 TRP A 203 ASP A 212 1 10
HELIX 10 10 LYS A 243 PHE A 248 5 6
HELIX 11 11 PHE A 256 ARG A 267 1 12
HELIX 12 12 LYS A 273 TRP A 280 5 8
HELIX 13 13 GLY A 281 GLY A 285 5 5
HELIX 14 14 PRO A 288 ASP A 290 5 3
HELIX 15 15 ASP A 300 GLY A 304 5 5
HELIX 16 16 GLY A 308 ILE A 312 5 5
HELIX 17 17 THR A 314 TRP A 316 5 3
HELIX 18 18 ASP A 317 HIS A 331 1 15
HELIX 19 19 CYS A 384 ARG A 387 5 4
HELIX 20 20 TRP A 388 ASP A 402 1 15
HELIX 21 21 ARG B 20 TYR B 31 1 12
HELIX 22 22 PRO B 57 GLN B 63 5 7
HELIX 23 23 ASN B 75 ASN B 88 1 14
HELIX 24 24 ASN B 120 ARG B 124 5 5
HELIX 25 25 SER B 132 PHE B 136 5 5
HELIX 26 26 ASN B 137 CYS B 141 5 5
HELIX 27 27 ASP B 153 CYS B 160 1 8
HELIX 28 28 LYS B 172 GLY B 190 1 19
HELIX 29 29 ALA B 198 MET B 202 5 5
HELIX 30 30 TRP B 203 ASP B 212 1 10
HELIX 31 31 LYS B 243 PHE B 248 5 6
HELIX 32 32 PHE B 256 ARG B 267 1 12
HELIX 33 33 LYS B 273 TRP B 280 5 8
HELIX 34 34 GLY B 281 GLY B 285 5 5
HELIX 35 35 PRO B 288 ASP B 290 5 3
HELIX 36 36 ASP B 300 GLY B 304 5 5
HELIX 37 37 GLY B 308 ILE B 312 5 5
HELIX 38 38 THR B 314 TRP B 316 5 3
HELIX 39 39 ASP B 317 HIS B 331 1 15
HELIX 40 40 CYS B 384 ARG B 387 5 4
HELIX 41 41 TRP B 388 VAL B 401 1 14
HELIX 42 42 GLU B 493 LYS B 495 5 3
HELIX 43 43 ARG C 20 TYR C 31 1 12
HELIX 44 44 PRO C 57 GLN C 63 5 7
HELIX 45 45 ASN C 75 VAL C 89 1 15
HELIX 46 46 ASN C 120 ARG C 124 5 5
HELIX 47 47 SER C 132 LYS C 140 5 9
HELIX 48 48 ASP C 153 CYS C 160 1 8
HELIX 49 49 LYS C 172 GLY C 190 1 19
HELIX 50 50 ALA C 198 MET C 202 5 5
HELIX 51 51 TRP C 203 ASP C 212 1 10
HELIX 52 52 LYS C 243 PHE C 248 5 6
HELIX 53 53 PHE C 256 LYS C 268 1 13
HELIX 54 54 LYS C 273 TRP C 280 5 8
HELIX 55 55 GLY C 281 GLY C 285 5 5
HELIX 56 56 PRO C 288 ASP C 290 5 3
HELIX 57 57 ASP C 300 GLY C 304 5 5
HELIX 58 58 GLY C 308 ILE C 312 5 5
HELIX 59 59 THR C 314 TRP C 316 5 3
HELIX 60 60 ASP C 317 HIS C 331 1 15
HELIX 61 61 CYS C 384 ARG C 387 5 4
HELIX 62 62 TRP C 388 VAL C 401 1 14
HELIX 63 63 GLU C 493 LYS C 495 5 3
HELIX 64 64 ARG D 20 TYR D 31 1 12
HELIX 65 65 PRO D 57 GLN D 63 5 7
HELIX 66 66 ASN D 75 VAL D 89 1 15
HELIX 67 67 ASN D 120 ARG D 124 5 5
HELIX 68 68 SER D 132 PHE D 136 5 5
HELIX 69 69 ASP D 153 CYS D 160 1 8
HELIX 70 70 LYS D 172 GLY D 190 1 19
HELIX 71 71 ALA D 198 MET D 202 5 5
HELIX 72 72 TRP D 203 ASP D 212 1 10
HELIX 73 73 LYS D 243 PHE D 248 5 6
HELIX 74 74 PHE D 256 ARG D 267 1 12
HELIX 75 75 LYS D 273 TRP D 280 5 8
HELIX 76 76 GLY D 281 GLY D 285 5 5
HELIX 77 77 PRO D 288 ASP D 290 5 3
HELIX 78 78 ASP D 300 GLY D 304 5 5
HELIX 79 79 GLY D 308 ILE D 312 5 5
HELIX 80 80 THR D 314 TRP D 316 5 3
HELIX 81 81 ASP D 317 HIS D 331 1 15
HELIX 82 82 CYS D 384 ARG D 387 5 4
HELIX 83 83 TRP D 388 VAL D 401 1 14
HELIX 84 84 GLU D 493 LYS D 495 5 3
HELIX 85 85 LYS E 84 THR E 88 5 5
HELIX 86 86 ARG E 100 TRP E 104 5 5
HELIX 87 87 LYS F 84 THR F 88 5 5
HELIX 88 88 ARG F 100 TRP F 104 5 5
HELIX 89 89 LYS G 84 THR G 88 5 5
HELIX 90 90 ARG G 100 TRP G 104 5 5
HELIX 91 91 ASP H 59 LYS H 62 5 4
HELIX 92 92 LYS H 84 THR H 88 5 5
HELIX 93 93 ARG H 100 TRP H 104 5 5
SHEET 1 A 9 SER A 12 LEU A 16 0
SHEET 2 A 9 GLY A 39 VAL A 42 1 O GLY A 39 N VAL A 14
SHEET 3 A 9 ARG A 92 ALA A 97 1 O ARG A 92 N VAL A 40
SHEET 4 A 9 GLY A 193 ILE A 196 1 O GLY A 193 N VAL A 95
SHEET 5 A 9 PHE A 229 GLN A 232 1 O PHE A 229 N PHE A 194
SHEET 6 A 9 ARG A 252 THR A 254 1 O ARG A 252 N GLN A 232
SHEET 7 A 9 ALA A 292 VAL A 294 1 N LEU A 293 O VAL A 253
SHEET 8 A 9 PHE A 335 SER A 340 1 O PHE A 335 N VAL A 294
SHEET 9 A 9 SER A 12 LEU A 16 1 O ILE A 13 N VAL A 338
SHEET 1 B 2 HIS A 101 GLY A 104 0
SHEET 2 B 2 LEU A 165 ASP A 167 -1 N LEU A 166 O CYS A 103
SHEET 1 C 2 PHE A 348 VAL A 349 0
SHEET 2 C 2 GLU A 352 ASP A 353 -1 O GLU A 352 N VAL A 349
SHEET 1 D 2 ASN A 362 ASN A 363 0
SHEET 2 D 2 VAL A 366 ILE A 367 -1 O VAL A 366 N ASN A 363
SHEET 1 E 4 PHE A 406 ASP A 411 0
SHEET 2 E 4 GLN A 416 ARG A 421 -1 N ALA A 418 O TRP A 410
SHEET 3 E 4 GLY A 425 ASN A 430 -1 O GLY A 425 N ARG A 421
SHEET 4 E 4 PHE A 487 HIS A 491 -1 O ILE A 488 N VAL A 428
SHEET 1 F 2 LEU A 436 GLN A 441 0
SHEET 2 F 2 THR A 474 ILE A 479 -1 O ALA A 475 N LEU A 440
SHEET 1 G 2 GLY A 447 CYS A 450 0
SHEET 2 G 2 LYS A 466 VAL A 469 -1 N VAL A 467 O TYR A 449
SHEET 1 H 2 LYS A 457 VAL A 458 0
SHEET 2 H 2 SER A 461 CYS A 462 -1 O SER A 461 N VAL A 458
SHEET 1 I 9 SER B 12 LEU B 16 0
SHEET 2 I 9 GLY B 39 VAL B 42 1 O GLY B 39 N VAL B 14
SHEET 3 I 9 ARG B 92 ALA B 97 1 O ARG B 92 N VAL B 40
SHEET 4 I 9 GLY B 193 ILE B 196 1 O GLY B 193 N VAL B 95
SHEET 5 I 9 PHE B 229 GLN B 232 1 O PHE B 229 N PHE B 194
SHEET 6 I 9 ARG B 252 THR B 254 1 O ARG B 252 N GLN B 232
SHEET 7 I 9 ALA B 292 VAL B 294 1 N LEU B 293 O VAL B 253
SHEET 8 I 9 PHE B 335 SER B 340 1 O PHE B 335 N VAL B 294
SHEET 9 I 9 SER B 12 LEU B 16 1 O ILE B 13 N VAL B 338
SHEET 1 J 2 HIS B 101 GLY B 104 0
SHEET 2 J 2 LEU B 165 ASP B 167 -1 N LEU B 166 O CYS B 103
SHEET 1 K 2 PHE B 348 VAL B 349 0
SHEET 2 K 2 GLU B 352 ASP B 353 -1 O GLU B 352 N VAL B 349
SHEET 1 L 2 ASN B 362 ASN B 363 0
SHEET 2 L 2 VAL B 366 ILE B 367 -1 N VAL B 366 O ASN B 363
SHEET 1 M 4 PHE B 406 ASP B 411 0
SHEET 2 M 4 GLN B 416 ARG B 421 -1 O ALA B 418 N TRP B 410
SHEET 3 M 4 GLY B 425 ASN B 430 -1 O GLY B 425 N ARG B 421
SHEET 4 M 4 PHE B 487 HIS B 491 -1 O ILE B 488 N VAL B 428
SHEET 1 N 2 LEU B 436 GLN B 441 0
SHEET 2 N 2 THR B 474 ILE B 479 -1 O ALA B 475 N LEU B 440
SHEET 1 O 2 GLY B 447 CYS B 450 0
SHEET 2 O 2 LYS B 466 VAL B 469 -1 O VAL B 467 N TYR B 449
SHEET 1 P 2 LYS B 457 VAL B 458 0
SHEET 2 P 2 SER B 461 CYS B 462 -1 O SER B 461 N VAL B 458
SHEET 1 Q 9 SER C 12 LEU C 16 0
SHEET 2 Q 9 GLY C 39 VAL C 42 1 O GLY C 39 N VAL C 14
SHEET 3 Q 9 ARG C 92 ALA C 97 1 O ARG C 92 N VAL C 40
SHEET 4 Q 9 GLY C 193 ILE C 196 1 O GLY C 193 N VAL C 95
SHEET 5 Q 9 PHE C 229 GLN C 232 1 O PHE C 229 N PHE C 194
SHEET 6 Q 9 ARG C 252 THR C 254 1 O ARG C 252 N GLN C 232
SHEET 7 Q 9 ALA C 292 VAL C 294 1 N LEU C 293 O VAL C 253
SHEET 8 Q 9 PHE C 335 SER C 340 1 O PHE C 335 N VAL C 294
SHEET 9 Q 9 SER C 12 LEU C 16 1 O ILE C 13 N VAL C 338
SHEET 1 R 2 HIS C 101 GLY C 104 0
SHEET 2 R 2 LEU C 165 ASP C 167 -1 N LEU C 166 O CYS C 103
SHEET 1 S 2 PHE C 348 VAL C 349 0
SHEET 2 S 2 GLU C 352 ASP C 353 -1 N GLU C 352 O VAL C 349
SHEET 1 T 2 ASN C 362 ASN C 363 0
SHEET 2 T 2 VAL C 366 ILE C 367 -1 O VAL C 366 N ASN C 363
SHEET 1 U 4 PHE C 406 ASP C 411 0
SHEET 2 U 4 GLN C 416 ARG C 421 -1 O ALA C 418 N TRP C 410
SHEET 3 U 4 GLY C 425 ASN C 430 -1 O GLY C 425 N ARG C 421
SHEET 4 U 4 PHE C 487 HIS C 491 -1 O ILE C 488 N VAL C 428
SHEET 1 V 2 LEU C 436 GLN C 441 0
SHEET 2 V 2 THR C 474 ILE C 479 -1 O ALA C 475 N LEU C 440
SHEET 1 W 2 GLY C 447 CYS C 450 0
SHEET 2 W 2 LYS C 466 VAL C 469 -1 N VAL C 467 O TYR C 449
SHEET 1 X 2 LYS C 457 VAL C 458 0
SHEET 2 X 2 SER C 461 CYS C 462 -1 O SER C 461 N VAL C 458
SHEET 1 Y 9 SER D 12 LEU D 16 0
SHEET 2 Y 9 GLY D 39 VAL D 42 1 O GLY D 39 N VAL D 14
SHEET 3 Y 9 ARG D 92 ALA D 97 1 O ARG D 92 N VAL D 40
SHEET 4 Y 9 GLY D 193 ILE D 196 1 O GLY D 193 N VAL D 95
SHEET 5 Y 9 PHE D 229 GLN D 232 1 O PHE D 229 N PHE D 194
SHEET 6 Y 9 ARG D 252 THR D 254 1 O ARG D 252 N GLN D 232
SHEET 7 Y 9 ALA D 292 VAL D 294 1 N LEU D 293 O VAL D 253
SHEET 8 Y 9 PHE D 335 SER D 340 1 O PHE D 335 N VAL D 294
SHEET 9 Y 9 SER D 12 LEU D 16 1 O ILE D 13 N VAL D 338
SHEET 1 Z 2 HIS D 101 GLY D 104 0
SHEET 2 Z 2 LEU D 165 ASP D 167 -1 N LEU D 166 O CYS D 103
SHEET 1 AA 2 PHE D 348 VAL D 349 0
SHEET 2 AA 2 GLU D 352 ASP D 353 -1 N GLU D 352 O VAL D 349
SHEET 1 AB 2 ASN D 362 ASN D 363 0
SHEET 2 AB 2 VAL D 366 ILE D 367 -1 O VAL D 366 N ASN D 363
SHEET 1 AC 4 PHE D 406 ASP D 411 0
SHEET 2 AC 4 GLN D 416 ARG D 421 -1 O ALA D 418 N TRP D 410
SHEET 3 AC 4 PHE D 348 VAL D 349 0
SHEET 4 AC 4 PHE D 487 HIS D 491 0
SHEET 1 AD 2 LEU D 436 GLN D 441 0
SHEET 2 AD 2 THR D 474 ILE D 479 -1 O ALA D 475 N LEU D 440
SHEET 1 AE 2 GLY D 447 CYS D 450 0
SHEET 2 AE 2 LYS D 466 VAL D 469 -1 O VAL D 467 N TYR D 449
SHEET 1 AF 2 LYS D 457 VAL D 458 0
SHEET 2 AF 2 SER D 461 CYS D 462 -1 O SER D 461 N VAL D 458
SHEET 1 AG 4 LEU E 4 SER E 7 0
SHEET 2 AG 4 LEU E 18 ALA E 24 -1 N SER E 21 O SER E 7
SHEET 3 AG 4 THR E 75 MET E 80 -1 O VAL E 76 N CYS E 22
SHEET 4 AG 4 PHE E 65 GLN E 69 -1 O THR E 66 N GLN E 79
SHEET 1 AH 8 SER E 11 VAL E 12 0
SHEET 2 AH 8 THR E 114 VAL E 118 1 O THR E 117 N VAL E 12
SHEET 3 AH 8 GLY E 89 GLY E 96 -1 N GLY E 89 O VAL E 116
SHEET 4 AH 8 TYR E 107 TRP E 110 -1 N PHE E 108 O THR E 95
SHEET 5 AH 8 GLY E 89 GLY E 96 -1 O THR E 95 N PHE E 108
SHEET 6 AH 8 THR E 30 GLN E 36 -1 O THR E 30 N GLY E 96
SHEET 7 AH 8 GLU E 43 TYR E 49 -1 N GLU E 43 O ARG E 35
SHEET 8 AH 8 THR E 55 SER E 57 -1 O TYR E 56 N ALA E 47
SHEET 1 AI 4 LEU F 4 GLY F 8 0
SHEET 2 AI 4 LEU F 18 ALA F 24 -1 N SER F 21 O SER F 7
SHEET 3 AI 4 THR F 75 MET F 80 -1 O VAL F 76 N CYS F 22
SHEET 4 AI 4 PHE F 65 GLN F 69 -1 O THR F 66 N GLN F 79
SHEET 1 AJ 8 GLY F 10 GLN F 13 0
SHEET 2 AJ 8 THR F 114 SER F 119 1 O GLN F 115 N GLY F 10
SHEET 3 AJ 8 GLY F 89 GLY F 96 -1 N GLY F 89 O VAL F 116
SHEET 4 AJ 8 TYR F 107 TRP F 110 -1 N PHE F 108 O THR F 95
SHEET 5 AJ 8 GLY F 89 GLY F 96 -1 O THR F 95 N PHE F 108
SHEET 6 AJ 8 THR F 30 GLN F 36 -1 O THR F 30 N GLY F 96
SHEET 7 AJ 8 GLU F 43 TYR F 49 -1 O GLU F 43 N ARG F 35
SHEET 8 AJ 8 THR F 55 SER F 57 -1 O TYR F 56 N ALA F 47
SHEET 1 AK 4 LEU G 4 SER G 7 0
SHEET 2 AK 4 LEU G 18 ALA G 24 -1 N SER G 21 O SER G 7
SHEET 3 AK 4 THR G 75 MET G 80 -1 N VAL G 76 O CYS G 22
SHEET 4 AK 4 PHE G 65 GLN G 69 -1 O THR G 66 N GLN G 79
SHEET 1 AL 8 GLY G 10 GLN G 13 0
SHEET 2 AL 8 THR G 114 SER G 119 1 O GLN G 115 N GLY G 10
SHEET 3 AL 8 GLY G 89 GLY G 96 -1 N GLY G 89 O VAL G 116
SHEET 4 AL 8 TYR G 107 TRP G 110 -1 N PHE G 108 O THR G 95
SHEET 5 AL 8 GLY G 89 GLY G 96 -1 O THR G 95 N PHE G 108
SHEET 6 AL 8 THR G 30 GLN G 36 -1 O THR G 30 N GLY G 96
SHEET 7 AL 8 GLU G 43 TYR G 49 -1 N GLU G 43 O ARG G 35
SHEET 8 AL 8 THR G 55 SER G 57 -1 O TYR G 56 N ALA G 47
SHEET 1 AM 4 LEU H 4 SER H 7 0
SHEET 2 AM 4 LEU H 18 ALA H 24 -1 N SER H 21 O SER H 7
SHEET 3 AM 4 THR H 75 MET H 80 -1 O VAL H 76 N CYS H 22
SHEET 4 AM 4 PHE H 65 GLN H 69 -1 O THR H 66 N GLN H 79
SHEET 1 AN 8 GLY H 10 GLN H 13 0
SHEET 2 AN 8 THR H 114 SER H 119 1 O GLN H 115 N GLY H 10
SHEET 3 AN 8 GLY H 89 GLY H 96 -1 N GLY H 89 O VAL H 116
SHEET 4 AN 8 TYR H 107 TRP H 110 -1 N PHE H 108 O THR H 95
SHEET 5 AN 8 GLY H 89 GLY H 96 -1 O THR H 95 N PHE H 108
SHEET 6 AN 8 THR H 30 GLN H 36 -1 O THR H 30 N GLY H 96
SHEET 7 AN 8 GLU H 43 TYR H 49 -1 N GLU H 43 O ARG H 35
SHEET 8 AN 8 THR H 55 SER H 57 -1 N TYR H 56 O ALA H 47
SSBOND 1 CYS A 28 CYS A 86 1555 1555 2.04
SSBOND 2 CYS A 70 CYS A 115 1555 1555 2.05
SSBOND 3 CYS A 141 CYS A 160 1555 1555 2.04
SSBOND 4 CYS A 378 CYS A 384 1555 1555 2.05
SSBOND 5 CYS A 450 CYS A 462 1555 1555 2.03
SSBOND 6 CYS B 28 CYS B 86 1555 1555 2.04
SSBOND 7 CYS B 70 CYS B 115 1555 1555 2.05
SSBOND 8 CYS B 141 CYS B 160 1555 1555 2.07
SSBOND 9 CYS B 378 CYS B 384 1555 1555 2.04
SSBOND 10 CYS B 450 CYS B 462 1555 1555 2.03
SSBOND 11 CYS C 28 CYS C 86 1555 1555 2.04
SSBOND 12 CYS C 70 CYS C 115 1555 1555 2.05
SSBOND 13 CYS C 141 CYS C 160 1555 1555 2.07
SSBOND 14 CYS C 378 CYS C 384 1555 1555 2.04
SSBOND 15 CYS C 450 CYS C 462 1555 1555 2.03
SSBOND 16 CYS D 28 CYS D 86 1555 1555 2.04
SSBOND 17 CYS D 70 CYS D 115 1555 1555 2.05
SSBOND 18 CYS D 141 CYS D 160 1555 1555 2.07
SSBOND 19 CYS D 378 CYS D 384 1555 1555 2.03
SSBOND 20 CYS D 450 CYS D 462 1555 1555 2.03
SSBOND 21 CYS E 22 CYS E 93 1555 1555 2.02
SSBOND 22 CYS F 22 CYS F 93 1555 1555 2.03
SSBOND 23 CYS G 22 CYS G 93 1555 1555 2.03
SSBOND 24 CYS H 22 CYS H 93 1555 1555 2.02
LINK OD1 ASN A 100 CA CA A4001 1555 1555 2.42
LINK O ARG A 158 CA CA A4001 1555 1555 2.42
LINK OD1 ASP A 167 CA CA A4001 1555 1555 2.50
LINK OD2 ASP A 167 CA CA A4001 1555 1555 2.49
LINK O HIS A 201 CA CA A4001 1555 1555 2.41
LINK CA CA A4001 O HOH A4014 1555 1555 2.49
LINK CA CA A4001 O HOH A4094 1555 1555 2.45
LINK CA CA A4001 O HOH A4125 1555 1555 2.58
LINK OD1 ASN B 100 CA CA B4003 1555 1555 2.42
LINK O ARG B 158 CA CA B4003 1555 1555 2.40
LINK OD1 ASP B 167 CA CA B4003 1555 1555 2.48
LINK OD2 ASP B 167 CA CA B4003 1555 1555 2.47
LINK O HIS B 201 CA CA B4003 1555 1555 2.42
LINK CA CA B4003 O HOH B4012 1555 1555 2.55
LINK CA CA B4003 O HOH B4030 1555 1555 2.42
LINK CA CA B4003 O HOH B4307 1555 1555 2.50
LINK OD1 ASN C 100 CA CA C4005 1555 1555 2.40
LINK O ARG C 158 CA CA C4005 1555 1555 2.41
LINK OD1 ASP C 167 CA CA C4005 1555 1555 2.50
LINK OD2 ASP C 167 CA CA C4005 1555 1555 2.47
LINK O HIS C 201 CA CA C4005 1555 1555 2.39
LINK CA CA C4005 O HOH C4022 1555 1555 2.53
LINK CA CA C4005 O HOH C4047 1555 1555 2.44
LINK CA CA C4005 O HOH C4060 1555 1555 2.53
LINK OD1 ASN D 100 CA CA D4007 1555 1555 2.41
LINK O ARG D 158 CA CA D4007 1555 1555 2.40
LINK OD2 ASP D 167 CA CA D4007 1555 1555 2.51
LINK OD1 ASP D 167 CA CA D4007 1555 1555 2.46
LINK O HIS D 201 CA CA D4007 1555 1555 2.41
LINK CA CA D4007 O HOH D4016 1555 1555 2.52
LINK CA CA D4007 O HOH D4038 1555 1555 2.56
LINK CA CA D4007 O HOH D4041 1555 1555 2.51
CISPEP 1 ASN A 53 PRO A 54 0 0.25
CISPEP 2 VAL A 129 PRO A 130 0 0.00
CISPEP 3 ASN B 53 PRO B 54 0 0.31
CISPEP 4 VAL B 129 PRO B 130 0 -0.24
CISPEP 5 ASN C 53 PRO C 54 0 0.31
CISPEP 6 VAL C 129 PRO C 130 0 -0.31
CISPEP 7 ASN D 53 PRO D 54 0 -0.07
CISPEP 8 VAL D 129 PRO D 130 0 0.45
SITE 1 AC1 7 ASN A 100 ARG A 158 ASP A 167 HIS A 201
SITE 2 AC1 7 HOH A4014 HOH A4094 HOH A4125
SITE 1 AC2 3 ARG A 195 ASN A 298 ARG A 337
SITE 1 AC3 7 ASN B 100 ARG B 158 ASP B 167 HIS B 201
SITE 2 AC3 7 HOH B4012 HOH B4030 HOH B4307
SITE 1 AC4 3 ARG B 195 ASN B 298 ARG B 337
SITE 1 AC5 7 ASN C 100 ARG C 158 ASP C 167 HIS C 201
SITE 2 AC5 7 HOH C4022 HOH C4047 HOH C4060
SITE 1 AC6 3 ARG C 195 ASN C 298 ARG C 337
SITE 1 AC7 7 ASN D 100 ARG D 158 ASP D 167 HIS D 201
SITE 2 AC7 7 HOH D4016 HOH D4038 HOH D4041
SITE 1 AC8 3 ARG D 195 ASN D 298 ARG D 337
CRYST1 65.170 100.920 103.740 79.31 72.63 86.11 P 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 0.015344 -0.001043 -0.004690 0.00000
SCALE2 0.000000 0.009932 -0.001750 0.00000
SCALE3 0.000000 0.000000 0.010256 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
