HEADER HYDROLASE, IMMUNE SYSTEM 01-FEB-02 1KXV
TITLE CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC
TITLE 2 ALPHA-AMYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-AMYLASE, PANCREATIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND 5 EC: 3.2.1.1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CAMELID VHH DOMAIN CAB10;
COMPND 8 CHAIN: C, D;
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: PANCEATIC 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: WK;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PHEN6
KEYWDS BETA 8 ALPHA 8, BETA BARREL, HYDROLASE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DESMYTER,S.SPINELLI,F.PAYAN,M.LAUWEREYS,L.WYNS,
AUTHOR 2 S.MUYLDERMANS,C.CAMBILLAU
REVDAT 4 24-FEB-09 1KXV 1 VERSN
REVDAT 3 01-APR-03 1KXV 1 JRNL
REVDAT 2 14-AUG-02 1KXV 1 JRNL
REVDAT 1 19-JUN-02 1KXV 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
JRNL TITL 2 PANCREATIC ALPHA-AMYLASE. INHIBITION AND
JRNL TITL 3 VERSATILITY OF BINDING 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,
REMARK 1 AUTH 2 W.HOLZER,E.DE GENST,L.WYNS,S.MUYLDERMANS
REMARK 1 TITL POTENT ENZYME INHIBITORS DERIVED FROM DROMEDARY
REMARK 1 TITL 2 HEAVY-CHAIN 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
REMARK 1 TITL 2 PANCREATIC 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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1228117.080
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 168160
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) : 0.205
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3337
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) (%) : 85.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 15241
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 165
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9574
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1377
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.65000
REMARK 3 B22 (A**2) : -2.76000
REMARK 3 B33 (A**2) : -3.89000
REMARK 3 B12 (A**2) : -0.47000
REMARK 3 B13 (A**2) : -1.99000
REMARK 3 B23 (A**2) : -3.06000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.07
REMARK 3 LOW RESOLUTION CUTOFF (A) : 10.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 2.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.53
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 : 0.36
REMARK 3 BSOL : 53.06
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 1KXV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-02.
REMARK 100 THE RCSB ID CODE IS RCSB015449.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
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 : DIAMOND
REMARK 200 OPTICS : DIAMOND
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 175069
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.13700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 1FJH, PDB ENTRY 1QD0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000 32%, NA CITRATE 0.1M &
REMARK 280 AMMONIUM ACETATE 0.2M, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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
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, C
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, D
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 GLN C 1
REMARK 465 SER C 121
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 LYS A 243 CG CD CE NZ
REMARK 470 ARG A 343 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 343 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 465 CG1 CG2 CD1
REMARK 470 TYR B 468 CG CD1 CD2 CE1 CE2 CZ OH
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 OE1 GLU B 282 O HOH B 626 1.66
REMARK 500 OD2 ASP D 61 O HOH D 159 1.87
REMARK 500 O HOH B 690 O HOH B 799 2.02
REMARK 500 N GLN A 1 O PRO A 228 2.03
REMARK 500 O HOH B 742 O HOH B 805 2.13
REMARK 500 ND2 ASN B 355 O HOH B 805 2.15
REMARK 500 O LEU B 170 CD ARG B 176 2.15
REMARK 500 O ASN B 355 O HOH B 826 2.15
REMARK 500 OD1 ASN A 347 O HOH A 838 2.16
REMARK 500 O HOH B 579 O HOH B 826 2.17
REMARK 500 OD1 ASP D 33 O HOH D 128 2.18
REMARK 500 O LEU A 170 CD ARG A 176 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLN D 1 C VAL D 2 N -0.154
REMARK 500 GLY D 8 C GLY D 9 N -0.434
REMARK 500 SER D 121 C SER D 121 OXT 0.634
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 ARG A 10 NE - CZ - NH1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 CYS A 70 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 72 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 ARG A 72 NE - CZ - NH2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG A 92 CB - CG - CD ANGL. DEV. = 18.7 DEGREES
REMARK 500 ARG A 92 CD - NE - CZ ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 176 CB - CG - CD ANGL. DEV. = 21.0 DEGREES
REMARK 500 ARG A 176 NE - CZ - NH1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG A 176 NE - CZ - NH2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG A 195 CD - NE - CZ ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 195 NE - CZ - NH1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 195 NE - CZ - NH2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLY A 225 C - N - CA ANGL. DEV. = -18.2 DEGREES
REMARK 500 ARG A 252 CB - CG - CD ANGL. DEV. = 20.4 DEGREES
REMARK 500 ARG A 252 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH1 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 LEU A 293 CA - CB - CG ANGL. DEV. = -21.1 DEGREES
REMARK 500 ARG A 389 CG - CD - NE ANGL. DEV. = -15.7 DEGREES
REMARK 500 ARG A 389 NE - CZ - NH1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG A 389 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 VAL A 395 CG1 - CB - CG2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 421 NE - CZ - NH1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 421 NE - CZ - NH2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 CYS B 70 CA - CB - SG ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG B 72 NE - CZ - NH2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG B 176 CB - CG - CD ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG B 176 CD - NE - CZ ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG B 176 NE - CZ - NH1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG B 176 NE - CZ - NH2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG B 195 NE - CZ - NH1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 195 NE - CZ - NH2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 252 CB - CG - CD ANGL. DEV. = 18.8 DEGREES
REMARK 500 ARG B 252 CD - NE - CZ ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP B 290 CB - CG - OD1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 ASP B 290 CB - CG - OD2 ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU B 293 CA - CB - CG ANGL. DEV. = -20.1 DEGREES
REMARK 500 ARG B 389 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 389 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG C 39 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 45 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 61 ANGLE DEVIATIONS.
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 -59.66 -143.57
REMARK 500 MET A 102 -150.89 -107.26
REMARK 500 ASP A 402 121.15 -39.33
REMARK 500 SER A 414 -106.91 -135.67
REMARK 500 ASP A 433 41.48 -91.55
REMARK 500 ASN A 460 40.87 -96.80
REMARK 500 PRO A 486 41.25 -82.01
REMARK 500 TYR B 31 -58.66 -143.60
REMARK 500 MET B 102 -148.28 -110.17
REMARK 500 VAL B 129 -60.86 -90.32
REMARK 500 ALA B 224 -104.28 -20.27
REMARK 500 SER B 414 -106.18 -134.36
REMARK 500 ASP B 433 42.48 -92.07
REMARK 500 ASN B 460 56.71 -101.29
REMARK 500 PRO B 486 38.32 -82.55
REMARK 500 ASN C 27 93.89 -161.40
REMARK 500 LYS C 75 151.53 -49.79
REMARK 500 ALA C 91 172.92 175.75
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 A 468 0.07 SIDE_CHAIN
REMARK 500 ARG C 39 0.11 SIDE_CHAIN
REMARK 500 ARG C 45 0.08 SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KXQ RELATED DB: PDB
REMARK 900 CAMELID VHH DOMAIN IN COMPLEX WITH PORCINE PANCREATIC ALPHA
REMARK 900 -AMYLASE
REMARK 900 RELATED ID: 1KXT RELATED DB: PDB
REMARK 900 CAMELID VHH DOMAINS IN COMPLEX WITH PORCINE PANCREATIC
REMARK 900 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
REMARK 999
REMARK 999 AN APPROPRIATE SEQUENCE DATABASE REFERENCE
REMARK 999 FOR THE ANTIBODY CAMELID VHH DOMAIN CAB10 , CHAINS
REMARK 999 C AND D, WAS NOT AVAILABLE AT THE TIME
REMARK 999 OF PROCESSING.
DBREF 1KXV A 1 496 UNP P00690 AMYP_PIG 1 496
DBREF 1KXV B 1 496 UNP P00690 AMYP_PIG 1 496
DBREF 1KXV C 1 121 PDB 1KXV 1KXV 1 121
DBREF 1KXV D 1 121 PDB 1KXV 1KXV 1 121
SEQADV 1KXV LYS A 243 UNP P00690 GLN 243 SEE REMARK 999
SEQADV 1KXV SER A 310 UNP P00690 ALA 310 SEE REMARK 999
SEQADV 1KXV ILE A 323 UNP P00690 VAL 323 SEE REMARK 999
SEQADV 1KXV GLN A 404 UNP P00690 GLU 404 SEE REMARK 999
SEQADV 1KXV LYS B 243 UNP P00690 GLN 243 SEE REMARK 999
SEQADV 1KXV SER B 310 UNP P00690 ALA 310 SEE REMARK 999
SEQADV 1KXV ILE B 323 UNP P00690 VAL 323 SEE REMARK 999
SEQADV 1KXV GLN B 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 121 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY THR VAL PRO
SEQRES 2 C 121 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 C 121 ASN THR LEU CYS THR TYR ASP MET SER TRP TYR ARG ARG
SEQRES 4 C 121 ALA PRO GLY LYS GLY ARG ASP PHE VAL SER GLY ILE ASP
SEQRES 5 C 121 ASN ASP GLY THR THR THR TYR VAL ASP SER VAL ALA GLY
SEQRES 6 C 121 ARG PHE THR ILE SER GLN GLY ASN ALA LYS ASN THR ALA
SEQRES 7 C 121 TYR LEU GLN MET ASP SER LEU LYS PRO ASP ASP THR ALA
SEQRES 8 C 121 MET TYR TYR CYS LYS PRO SER LEU ARG TYR GLY LEU PRO
SEQRES 9 C 121 GLY CYS PRO ILE ILE PRO TRP GLY GLN GLY THR GLN VAL
SEQRES 10 C 121 THR VAL SER SER
SEQRES 1 D 121 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY THR VAL PRO
SEQRES 2 D 121 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 D 121 ASN THR LEU CYS THR TYR ASP MET SER TRP TYR ARG ARG
SEQRES 4 D 121 ALA PRO GLY LYS GLY ARG ASP PHE VAL SER GLY ILE ASP
SEQRES 5 D 121 ASN ASP GLY THR THR THR TYR VAL ASP SER VAL ALA GLY
SEQRES 6 D 121 ARG PHE THR ILE SER GLN GLY ASN ALA LYS ASN THR ALA
SEQRES 7 D 121 TYR LEU GLN MET ASP SER LEU LYS PRO ASP ASP THR ALA
SEQRES 8 D 121 MET TYR TYR CYS LYS PRO SER LEU ARG TYR GLY LEU PRO
SEQRES 9 D 121 GLY CYS PRO ILE ILE PRO TRP GLY GLN GLY THR GLN VAL
SEQRES 10 D 121 THR VAL SER SER
FORMUL 5 HOH *1377(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 ASN A 88 1 14
HELIX 4 4 ASN A 120 ARG A 124 5 5
HELIX 5 5 SER A 132 PHE A 136 5 5
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 LYS A 268 1 13
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 GLU A 493 LYS A 495 5 3
HELIX 22 22 ARG B 20 TYR B 31 1 12
HELIX 23 23 PRO B 57 GLN B 63 5 7
HELIX 24 24 ASN B 75 VAL B 89 1 15
HELIX 25 25 ASN B 120 ARG B 124 5 5
HELIX 26 26 SER B 132 PHE B 136 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 LYS B 213 1 11
HELIX 31 31 LYS B 243 PHE B 248 5 6
HELIX 32 32 PHE B 256 LYS B 268 1 13
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 ASP B 402 1 15
HELIX 42 42 GLU B 493 LYS B 495 5 3
HELIX 43 43 ASP C 61 ALA C 64 5 4
HELIX 44 44 LYS C 86 THR C 90 5 5
HELIX 45 45 ASP D 61 ALA D 64 5 4
HELIX 46 46 LYS D 86 THR D 90 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 O ALA A 418 N 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 O VAL B 366 N 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 N VAL B 467 O TYR B 449
SHEET 1 P 4 GLN C 3 SER C 7 0
SHEET 2 P 4 LEU C 18 SER C 25 -1 N SER C 21 O SER C 7
SHEET 3 P 4 THR C 77 MET C 82 -1 O ALA C 78 N CYS C 22
SHEET 4 P 4 PHE C 67 GLN C 71 -1 O THR C 68 N GLN C 81
SHEET 1 Q 6 GLY C 10 VAL C 12 0
SHEET 2 Q 6 THR C 115 VAL C 119 1 O GLN C 116 N GLY C 10
SHEET 3 Q 6 ALA C 91 LEU C 99 -1 O ALA C 91 N VAL C 117
SHEET 4 Q 6 TYR C 32 ARG C 39 -1 N ASP C 33 O SER C 98
SHEET 5 Q 6 ARG C 45 ILE C 51 -1 N ASP C 46 O ARG C 38
SHEET 6 Q 6 THR C 57 TYR C 59 -1 O THR C 58 N GLY C 50
SHEET 1 R 4 GLN D 3 SER D 7 0
SHEET 2 R 4 LEU D 18 SER D 25 -1 N SER D 21 O SER D 7
SHEET 3 R 4 THR D 77 MET D 82 -1 N ALA D 78 O CYS D 22
SHEET 4 R 4 PHE D 67 GLN D 71 -1 O THR D 68 N GLN D 81
SHEET 1 S 6 GLY D 10 PRO D 13 0
SHEET 2 S 6 THR D 115 SER D 120 1 O GLN D 116 N GLY D 10
SHEET 3 S 6 ALA D 91 LEU D 99 -1 O ALA D 91 N VAL D 117
SHEET 4 S 6 TYR D 32 ARG D 39 -1 N ASP D 33 O SER D 98
SHEET 5 S 6 ARG D 45 ILE D 51 -1 N ASP D 46 O ARG D 38
SHEET 6 S 6 THR D 57 TYR D 59 -1 N THR D 58 O GLY D 50
SSBOND 1 CYS A 28 CYS A 86 1555 1555 2.08
SSBOND 2 CYS A 70 CYS A 115 1555 1555 2.08
SSBOND 3 CYS A 141 CYS A 160 1555 1555 2.07
SSBOND 4 CYS A 378 CYS A 384 1555 1555 2.06
SSBOND 5 CYS A 450 CYS A 462 1555 1555 2.03
SSBOND 6 CYS B 28 CYS B 86 1555 1555 2.07
SSBOND 7 CYS B 70 CYS B 115 1555 1555 2.07
SSBOND 8 CYS B 141 CYS B 160 1555 1555 2.08
SSBOND 9 CYS B 378 CYS B 384 1555 1555 2.05
SSBOND 10 CYS B 450 CYS B 462 1555 1555 2.05
SSBOND 11 CYS C 22 CYS C 95 1555 1555 2.03
SSBOND 12 CYS C 30 CYS C 106 1555 1555 2.07
SSBOND 13 CYS D 22 CYS D 95 1555 1555 2.03
SSBOND 14 CYS D 30 CYS D 106 1555 1555 2.07
CISPEP 1 ASN A 53 PRO A 54 0 0.00
CISPEP 2 VAL A 129 PRO A 130 0 -0.48
CISPEP 3 ASN B 53 PRO B 54 0 0.05
CISPEP 4 VAL B 129 PRO B 130 0 0.61
CRYST1 57.568 60.990 107.333 98.78 100.88 101.14 P 1 2
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 0.017371 0.003421 0.004090 0.00000
SCALE2 0.000000 0.016711 0.003345 0.00000
SCALE3 0.000000 0.000000 0.009676 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
