HEADER ENDOCYTOSIS/EXOCYTOSIS 02-AUG-99 1C9L
TITLE PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER
TITLE 2 OF CLATHRIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLATHRIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: B-ADAPTIN 3;
COMPND 8 CHAIN: C, D;
COMPND 9 FRAGMENT: CLATHRIN-BOX PEPTIDE;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBAT4;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYTHESIZED.THE SEQUENCE
SOURCE 12 OF THIS PEPTIDE NATURALLY OCCURS IN HUMANS (HOMO SAPIENS).
KEYWDS BETA-PROPELLER, HELICAL HAIRPIN, ENDOCYTOSIS-EXOCYTOSIS COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.TER HAAR,S.C.HARRISON,T.KIRCHHAUSEN
REVDAT 4 07-FEB-24 1C9L 1 REMARK
REVDAT 3 04-OCT-17 1C9L 1 REMARK
REVDAT 2 24-FEB-09 1C9L 1 VERSN
REVDAT 1 07-FEB-00 1C9L 0
JRNL AUTH E.TER HAAR,S.C.HARRISON,T.KIRCHHAUSEN
JRNL TITL PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE
JRNL TITL 2 BETA-PROPELLER OF CLATHRIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 1096 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10655490
JRNL DOI 10.1073/PNAS.97.3.1096
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.5
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1585264.690
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 25725
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) : 0.221
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1282
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3882
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 201
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5716
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 220.3
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.76000
REMARK 3 B22 (A**2) : 1.05000
REMARK 3 B33 (A**2) : -5.82000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 12.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.40
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : 0.37
REMARK 3 BSOL : 35.79
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.PA
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009462.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ELLIOTT GX-13
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27854
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 92.5
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.14600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, KOAC, DTT, TRIS, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-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 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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 68.81000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.39350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.81000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 65.39350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 NE2 GLN B 89 O THR D 371 2.06
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 GLY A 359 C GLY A 359 OXT 1.007
REMARK 500 GLY B 359 C GLY B 359 OXT 1.007
REMARK 500 PHE C 376 C GLU C 377 N -0.143
REMARK 500 GLU C 377 N GLU C 377 CA -0.130
REMARK 500 GLU C 377 C GLU C 377 OXT 0.189
REMARK 500 GLU D 377 C GLU D 377 OXT 0.185
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 ILE A 4 C - N - CA ANGL. DEV. = -20.8 DEGREES
REMARK 500 ILE B 4 C - N - CA ANGL. DEV. = -16.5 DEGREES
REMARK 500 PRO B 6 CA - C - N ANGL. DEV. = -18.4 DEGREES
REMARK 500 ARG B 64 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 GLU C 377 N - CA - C ANGL. DEV. = 17.3 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 LEU A 15 -33.06 -39.90
REMARK 500 ASP A 57 71.19 -154.87
REMARK 500 SER A 67 37.01 -149.88
REMARK 500 GLU A 135 79.68 -102.83
REMARK 500 LYS A 189 51.75 37.12
REMARK 500 GLN B 10 137.06 -170.81
REMARK 500 SER B 34 -178.46 -177.01
REMARK 500 VAL B 44 95.91 -47.98
REMARK 500 ASP B 57 71.10 -169.69
REMARK 500 ASN B 60 50.17 -114.69
REMARK 500 SER B 67 31.72 -143.67
REMARK 500 TRP B 111 139.56 -175.04
REMARK 500 GLU B 135 -2.09 -48.39
REMARK 500 SER B 136 169.90 -43.53
REMARK 500 GLN B 162 45.25 38.89
REMARK 500 ARG B 176 148.82 -176.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C9I RELATED DB: PDB
DBREF 1C9L A 3 359 UNP P11442 CLH_RAT 3 359
DBREF 1C9L B 3 359 UNP P11442 CLH_RAT 3 359
DBREF 1C9L C 370 377 PDB 1C9L 1C9L 370 377
DBREF 1C9L D 370 377 PDB 1C9L 1C9L 370 377
SEQRES 1 A 357 GLN ILE LEU PRO ILE ARG PHE GLN GLU HIS LEU GLN LEU
SEQRES 2 A 357 GLN ASN LEU GLY ILE ASN PRO ALA ASN ILE GLY PHE SER
SEQRES 3 A 357 THR LEU THR MET GLU SER ASP LYS PHE ILE CYS ILE ARG
SEQRES 4 A 357 GLU LYS VAL GLY GLU GLN ALA GLN VAL VAL ILE ILE ASP
SEQRES 5 A 357 MET ASN ASP PRO SER ASN PRO ILE ARG ARG PRO ILE SER
SEQRES 6 A 357 ALA ASP SER ALA ILE MET ASN PRO ALA SER LYS VAL ILE
SEQRES 7 A 357 ALA LEU LYS ALA GLY LYS THR LEU GLN ILE PHE ASN ILE
SEQRES 8 A 357 GLU MET LYS SER LYS MET LYS ALA HIS THR MET THR ASP
SEQRES 9 A 357 ASP VAL THR PHE TRP LYS TRP ILE SER LEU ASN THR VAL
SEQRES 10 A 357 ALA LEU VAL THR ASP ASN ALA VAL TYR HIS TRP SER MET
SEQRES 11 A 357 GLU GLY GLU SER GLN PRO VAL LYS MET PHE ASP ARG HIS
SEQRES 12 A 357 SER SER LEU ALA GLY CYS GLN ILE ILE ASN TYR ARG THR
SEQRES 13 A 357 ASP ALA LYS GLN LYS TRP LEU LEU LEU THR GLY ILE SER
SEQRES 14 A 357 ALA GLN GLN ASN ARG VAL VAL GLY ALA MET GLN LEU TYR
SEQRES 15 A 357 SER VAL ASP ARG LYS VAL SER GLN PRO ILE GLU GLY HIS
SEQRES 16 A 357 ALA ALA SER PHE ALA GLN PHE LYS MET GLU GLY ASN ALA
SEQRES 17 A 357 GLU GLU SER THR LEU PHE CYS PHE ALA VAL ARG GLY GLN
SEQRES 18 A 357 ALA GLY GLY LYS LEU HIS ILE ILE GLU VAL GLY THR PRO
SEQRES 19 A 357 PRO THR GLY ASN GLN PRO PHE PRO LYS LYS ALA VAL ASP
SEQRES 20 A 357 VAL PHE PHE PRO PRO GLU ALA GLN ASN ASP PHE PRO VAL
SEQRES 21 A 357 ALA MET GLN ILE SER GLU LYS HIS ASP VAL VAL PHE LEU
SEQRES 22 A 357 ILE THR LYS TYR GLY TYR ILE HIS LEU TYR ASP LEU GLU
SEQRES 23 A 357 THR GLY THR CYS ILE TYR MET ASN ARG ILE SER GLY GLU
SEQRES 24 A 357 THR ILE PHE VAL THR ALA PRO HIS GLU ALA THR ALA GLY
SEQRES 25 A 357 ILE ILE GLY VAL ASN ARG LYS GLY GLN VAL LEU SER VAL
SEQRES 26 A 357 CYS VAL GLU GLU GLU ASN ILE ILE PRO TYR ILE THR ASN
SEQRES 27 A 357 VAL LEU GLN ASN PRO ASP LEU ALA LEU ARG MET ALA VAL
SEQRES 28 A 357 ARG ASN ASN LEU ALA GLY
SEQRES 1 B 357 GLN ILE LEU PRO ILE ARG PHE GLN GLU HIS LEU GLN LEU
SEQRES 2 B 357 GLN ASN LEU GLY ILE ASN PRO ALA ASN ILE GLY PHE SER
SEQRES 3 B 357 THR LEU THR MET GLU SER ASP LYS PHE ILE CYS ILE ARG
SEQRES 4 B 357 GLU LYS VAL GLY GLU GLN ALA GLN VAL VAL ILE ILE ASP
SEQRES 5 B 357 MET ASN ASP PRO SER ASN PRO ILE ARG ARG PRO ILE SER
SEQRES 6 B 357 ALA ASP SER ALA ILE MET ASN PRO ALA SER LYS VAL ILE
SEQRES 7 B 357 ALA LEU LYS ALA GLY LYS THR LEU GLN ILE PHE ASN ILE
SEQRES 8 B 357 GLU MET LYS SER LYS MET LYS ALA HIS THR MET THR ASP
SEQRES 9 B 357 ASP VAL THR PHE TRP LYS TRP ILE SER LEU ASN THR VAL
SEQRES 10 B 357 ALA LEU VAL THR ASP ASN ALA VAL TYR HIS TRP SER MET
SEQRES 11 B 357 GLU GLY GLU SER GLN PRO VAL LYS MET PHE ASP ARG HIS
SEQRES 12 B 357 SER SER LEU ALA GLY CYS GLN ILE ILE ASN TYR ARG THR
SEQRES 13 B 357 ASP ALA LYS GLN LYS TRP LEU LEU LEU THR GLY ILE SER
SEQRES 14 B 357 ALA GLN GLN ASN ARG VAL VAL GLY ALA MET GLN LEU TYR
SEQRES 15 B 357 SER VAL ASP ARG LYS VAL SER GLN PRO ILE GLU GLY HIS
SEQRES 16 B 357 ALA ALA SER PHE ALA GLN PHE LYS MET GLU GLY ASN ALA
SEQRES 17 B 357 GLU GLU SER THR LEU PHE CYS PHE ALA VAL ARG GLY GLN
SEQRES 18 B 357 ALA GLY GLY LYS LEU HIS ILE ILE GLU VAL GLY THR PRO
SEQRES 19 B 357 PRO THR GLY ASN GLN PRO PHE PRO LYS LYS ALA VAL ASP
SEQRES 20 B 357 VAL PHE PHE PRO PRO GLU ALA GLN ASN ASP PHE PRO VAL
SEQRES 21 B 357 ALA MET GLN ILE SER GLU LYS HIS ASP VAL VAL PHE LEU
SEQRES 22 B 357 ILE THR LYS TYR GLY TYR ILE HIS LEU TYR ASP LEU GLU
SEQRES 23 B 357 THR GLY THR CYS ILE TYR MET ASN ARG ILE SER GLY GLU
SEQRES 24 B 357 THR ILE PHE VAL THR ALA PRO HIS GLU ALA THR ALA GLY
SEQRES 25 B 357 ILE ILE GLY VAL ASN ARG LYS GLY GLN VAL LEU SER VAL
SEQRES 26 B 357 CYS VAL GLU GLU GLU ASN ILE ILE PRO TYR ILE THR ASN
SEQRES 27 B 357 VAL LEU GLN ASN PRO ASP LEU ALA LEU ARG MET ALA VAL
SEQRES 28 B 357 ARG ASN ASN LEU ALA GLY
SEQRES 1 C 8 ASP THR ASN LEU ILE GLU PHE GLU
SEQRES 1 D 8 ASP THR ASN LEU ILE GLU PHE GLU
HELIX 1 1 GLN A 16 GLY A 19 5 4
HELIX 2 2 ASN A 21 ILE A 25 5 5
HELIX 3 3 HIS A 145 ALA A 149 5 5
HELIX 4 4 ASN A 333 ASN A 340 1 8
HELIX 5 5 ASN A 344 ASN A 355 1 12
HELIX 6 6 GLN B 16 GLY B 19 5 4
HELIX 7 7 ASN B 21 ILE B 25 5 5
HELIX 8 8 HIS B 145 ALA B 149 5 5
HELIX 9 9 ASN B 333 VAL B 341 1 9
HELIX 10 10 ASN B 344 ASN B 356 1 13
SHEET 1 A 4 ILE A 7 GLN A 14 0
SHEET 2 A 4 GLN A 323 VAL A 329 -1 O VAL A 324 N HIS A 12
SHEET 3 A 4 GLY A 314 ASN A 319 -1 O ILE A 315 N VAL A 327
SHEET 4 A 4 ILE A 303 HIS A 309 -1 N PHE A 304 O VAL A 318
SHEET 1 B 4 LEU A 30 THR A 31 0
SHEET 2 B 4 PHE A 37 VAL A 44 -1 O CYS A 39 N THR A 31
SHEET 3 B 4 GLN A 47 ASP A 54 -1 N GLN A 47 O VAL A 44
SHEET 4 B 4 ASP A 57 PRO A 65 -1 N ASP A 57 O ASP A 54
SHEET 1 C 4 SER A 70 MET A 73 0
SHEET 2 C 4 VAL A 79 ALA A 84 -1 O ALA A 81 N ILE A 72
SHEET 3 C 4 THR A 87 ASN A 92 -1 O THR A 87 N ALA A 84
SHEET 4 C 4 SER A 97 THR A 103 -1 O SER A 97 N ASN A 92
SHEET 1 D 4 VAL A 108 TRP A 113 0
SHEET 2 D 4 THR A 118 THR A 123 -1 N ALA A 120 O LYS A 112
SHEET 3 D 4 ALA A 126 SER A 131 -1 O ALA A 126 N THR A 123
SHEET 4 D 4 VAL A 139 ASP A 143 -1 O VAL A 139 N HIS A 129
SHEET 1 E 4 GLN A 152 THR A 158 0
SHEET 2 E 4 TRP A 164 GLN A 173 -1 N LEU A 166 O ARG A 157
SHEET 3 E 4 ARG A 176 SER A 185 -1 N ARG A 176 O GLN A 173
SHEET 4 E 4 VAL A 190 GLU A 195 -1 O VAL A 190 N SER A 185
SHEET 1 F 4 ALA A 198 PHE A 204 0
SHEET 2 F 4 SER A 213 GLY A 222 -1 O SER A 213 N PHE A 204
SHEET 3 F 4 GLY A 225 GLU A 232 -1 O GLY A 225 N GLY A 222
SHEET 4 F 4 LYS A 246 VAL A 248 -1 N LYS A 246 O ILE A 230
SHEET 1 G 4 PRO A 261 SER A 267 0
SHEET 2 G 4 VAL A 272 THR A 277 -1 O VAL A 272 N SER A 267
SHEET 3 G 4 TYR A 281 ASP A 286 -1 O TYR A 281 N THR A 277
SHEET 4 G 4 CYS A 292 ARG A 297 -1 N ILE A 293 O LEU A 284
SHEET 1 H 4 ILE B 7 GLN B 14 0
SHEET 2 H 4 GLN B 323 VAL B 329 -1 O VAL B 324 N HIS B 12
SHEET 3 H 4 GLY B 314 ASN B 319 -1 N ILE B 315 O VAL B 327
SHEET 4 H 4 ILE B 303 VAL B 305 -1 N PHE B 304 O VAL B 318
SHEET 1 H1 4 ILE B 7 GLN B 14 0
SHEET 2 H1 4 GLN B 323 VAL B 329 -1 O VAL B 324 N HIS B 12
SHEET 3 H1 4 GLY B 314 ASN B 319 -1 N ILE B 315 O VAL B 327
SHEET 4 H1 4 PRO B 308 HIS B 309 -1 N HIS B 309 O GLY B 314
SHEET 1 I 4 LEU B 30 THR B 31 0
SHEET 2 I 4 PHE B 37 GLU B 42 -1 N CYS B 39 O THR B 31
SHEET 3 I 4 GLN B 49 ASP B 54 -1 O GLN B 49 N GLU B 42
SHEET 4 I 4 ASP B 57 PRO B 65 -1 N ASP B 57 O ASP B 54
SHEET 1 J 4 SER B 70 MET B 73 0
SHEET 2 J 4 VAL B 79 ALA B 84 -1 N ALA B 81 O ILE B 72
SHEET 3 J 4 THR B 87 ASN B 92 -1 O THR B 87 N ALA B 84
SHEET 4 J 4 SER B 97 THR B 103 -1 O SER B 97 N ASN B 92
SHEET 1 K 4 PHE B 110 TRP B 113 0
SHEET 2 K 4 THR B 118 THR B 123 -1 N ALA B 120 O LYS B 112
SHEET 3 K 4 ALA B 126 SER B 131 -1 O ALA B 126 N THR B 123
SHEET 4 K 4 VAL B 139 ASP B 143 -1 N VAL B 139 O HIS B 129
SHEET 1 L 4 GLN B 152 THR B 158 0
SHEET 2 L 4 TRP B 164 ALA B 172 -1 N LEU B 166 O ARG B 157
SHEET 3 L 4 VAL B 177 SER B 185 -1 N VAL B 178 O SER B 171
SHEET 4 L 4 VAL B 190 GLU B 195 -1 O VAL B 190 N SER B 185
SHEET 1 M 4 ALA B 198 PHE B 204 0
SHEET 2 M 4 SER B 213 GLY B 222 -1 N SER B 213 O PHE B 204
SHEET 3 M 4 GLY B 225 GLU B 232 -1 O GLY B 225 N GLY B 222
SHEET 4 M 4 LYS B 246 ASP B 249 -1 N LYS B 246 O ILE B 230
SHEET 1 N 4 PRO B 261 SER B 267 0
SHEET 2 N 4 VAL B 272 THR B 277 -1 O VAL B 272 N SER B 267
SHEET 3 N 4 TYR B 281 ASP B 286 -1 O TYR B 281 N THR B 277
SHEET 4 N 4 CYS B 292 ARG B 297 -1 N ILE B 293 O LEU B 284
CRYST1 137.620 130.787 78.468 90.00 115.47 90.00 C 1 2 1 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 0.007266 0.000000 0.003460 0.00000
SCALE2 0.000000 0.007646 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014115 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
