HEADER ENDOCYTOSIS 10-JUN-09 3HS9
TITLE INTERSECTIN 1-PEPTIDE-AP2 BETA EAR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AP-2 COMPLEX SUBUNIT BETA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 701-937;
COMPND 5 SYNONYM: ADAPTER-RELATED PROTEIN COMPLEX 2 BETA-1 SUBUNIT, BETA2-
COMPND 6 ADAPTIN, BETA-ADAPTIN, PLASMA MEMBRANE ADAPTOR HA2/AP2 ADAPTIN BETA
COMPND 7 SUBUNIT, CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 BETA LARGE CHAIN,
COMPND 8 AP105B;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: PEPTIDE FROM INTERSECTIN-1, RESIDUES 841-851;
COMPND 12 CHAIN: P;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: AP2B1, CLAPB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS CLATHRIN, ADAPTOR COMPLEX AP-2, ENDOCYTOSIS, ALTERNATIVE SPLICING,
KEYWDS 2 CELL MEMBRANE, COATED PIT, MEMBRANE, DISEASE MUTATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VAHEDI-FARIDI,A.PECHSTEIN,J.G.SCHAEFER,W.SAENGER,V.HAUCKE
REVDAT 3 01-NOV-23 3HS9 1 SEQADV
REVDAT 2 05-MAY-10 3HS9 1 JRNL
REVDAT 1 23-FEB-10 3HS9 0
JRNL AUTH A.PECHSTEIN,J.BACETIC,A.VAHEDI-FARIDI,K.GROMOVA,
JRNL AUTH 2 A.SUNDBORGER,N.TOMLIN,G.KRAINER,O.VORONTSOVA,J.G.SCHAFER,
JRNL AUTH 3 S.G.OWE,M.A.COUSIN,W.SAENGER,O.SHUPLIAKOV,V.HAUCKE
JRNL TITL REGULATION OF SYNAPTIC VESICLE RECYCLING BY COMPLEX
JRNL TITL 2 FORMATION BETWEEN INTERSECTIN 1 AND THE CLATHRIN ADAPTOR
JRNL TITL 3 COMPLEX AP2.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 4206 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20160082
JRNL DOI 10.1073/PNAS.0911073107
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 17529
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 + TEST SET) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.200
REMARK 3 FREE R VALUE TEST SET COUNT : 743
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1245
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.4090
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.4070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1952
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.95000
REMARK 3 B22 (A**2) : 8.20000
REMARK 3 B33 (A**2) : -3.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.275
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.221
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.259
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.424
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2000 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2722 ; 1.564 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 242 ; 7.926 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;42.845 ;25.699
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 341 ;18.483 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;11.833 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 304 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1518 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 919 ; 0.232 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1331 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 135 ; 0.188 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 43 ; 0.249 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.218 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1261 ; 0.812 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1992 ; 1.404 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 834 ; 1.650 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 730 ; 2.628 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3HS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053521.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.25
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23441
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 60.523
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1190
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.46600
REMARK 200 R SYM FOR SHELL (I) : 0.46600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2G30
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG8000, 100MM HEPES, 4MM DTT, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K
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 61.04400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.55150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.04400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.55150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 678
REMARK 465 GLY A 679
REMARK 465 SER A 680
REMARK 465 SER A 681
REMARK 465 HIS A 682
REMARK 465 HIS A 683
REMARK 465 HIS A 684
REMARK 465 HIS A 685
REMARK 465 HIS A 686
REMARK 465 HIS A 687
REMARK 465 SER A 688
REMARK 465 SER A 689
REMARK 465 GLY A 690
REMARK 465 LEU A 691
REMARK 465 VAL A 692
REMARK 465 PRO A 693
REMARK 465 ARG A 694
REMARK 465 GLY A 695
REMARK 465 SER A 696
REMARK 465 HIS A 697
REMARK 465 MET A 698
REMARK 465 ALA A 699
REMARK 465 SER A 700
REMARK 465 GLY A 701
REMARK 465 MET A 702
REMARK 465 ALA A 703
REMARK 465 PRO A 704
REMARK 465 PRO P 840
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 ALA A 720 44.42 -140.50
REMARK 500 HIS A 773 56.97 -100.55
REMARK 500 MET A 795 118.76 -165.50
REMARK 500 GLU A 828 -5.81 -57.39
REMARK 500 PRO A 845 135.81 -36.50
REMARK 500 GLU A 856 51.29 27.54
REMARK 500 GLU A 882 43.90 76.89
REMARK 500 ASN A 895 24.35 -78.60
REMARK 500 PRO A 910 42.40 -90.54
REMARK 500 ASP P 845 -95.53 -94.46
REMARK 500 PHE P 846 77.72 63.49
REMARK 500 TRP P 850 -13.76 -166.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HS8 RELATED DB: PDB
DBREF 3HS9 A 701 937 UNP P62944 AP2B1_RAT 701 937
DBREF 3HS9 P 840 851 UNP Q9Z0R4 ITSN1_MOUSE 840 851
SEQADV 3HS9 MET A 678 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 GLY A 679 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 SER A 680 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 SER A 681 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 682 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 683 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 684 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 685 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 686 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 687 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 SER A 688 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 SER A 689 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 GLY A 690 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 LEU A 691 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 VAL A 692 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 PRO A 693 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 ARG A 694 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 GLY A 695 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 SER A 696 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 HIS A 697 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 MET A 698 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 ALA A 699 UNP P62944 EXPRESSION TAG
SEQADV 3HS9 SER A 700 UNP P62944 EXPRESSION TAG
SEQRES 1 A 260 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 260 LEU VAL PRO ARG GLY SER HIS MET ALA SER GLY MET ALA
SEQRES 3 A 260 PRO GLY GLY TYR VAL ALA PRO LYS ALA VAL TRP LEU PRO
SEQRES 4 A 260 ALA VAL LYS ALA LYS GLY LEU GLU ILE SER GLY THR PHE
SEQRES 5 A 260 THR HIS ARG GLN GLY HIS ILE TYR MET GLU MET ASN PHE
SEQRES 6 A 260 THR ASN LYS ALA LEU GLN HIS MET THR ASP PHE ALA ILE
SEQRES 7 A 260 GLN PHE ASN LYS ASN SER PHE GLY VAL ILE PRO SER THR
SEQRES 8 A 260 PRO LEU ALA ILE HIS THR PRO LEU MET PRO ASN GLN SER
SEQRES 9 A 260 ILE ASP VAL SER LEU PRO LEU ASN THR LEU GLY PRO VAL
SEQRES 10 A 260 MET LYS MET GLU PRO LEU ASN ASN LEU GLN VAL ALA VAL
SEQRES 11 A 260 LYS ASN ASN ILE ASP VAL PHE TYR PHE SER CYS LEU ILE
SEQRES 12 A 260 PRO LEU ASN VAL LEU PHE VAL GLU ASP GLY LYS MET GLU
SEQRES 13 A 260 ARG GLN VAL PHE LEU ALA THR TRP LYS ASP ILE PRO ASN
SEQRES 14 A 260 GLU ASN GLU LEU GLN PHE GLN ILE LYS GLU CYS HIS LEU
SEQRES 15 A 260 ASN ALA ASP THR VAL SER SER LYS LEU GLN ASN ASN ASN
SEQRES 16 A 260 VAL TYR THR ILE ALA LYS ARG ASN VAL GLU GLY GLN ASP
SEQRES 17 A 260 MET LEU TYR GLN SER LEU LYS LEU THR ASN GLY ILE TRP
SEQRES 18 A 260 ILE LEU ALA GLU LEU ARG ILE GLN PRO GLY ASN PRO ASN
SEQRES 19 A 260 TYR THR LEU SER LEU LYS CYS ARG ALA PRO GLU VAL SER
SEQRES 20 A 260 GLN TYR ILE TYR GLN VAL TYR ASP SER ILE LEU LYS ASN
SEQRES 1 P 12 PRO ASN ASN TRP ALA ASP PHE SER SER THR TRP PRO
FORMUL 3 HOH *133(H2 O)
HELIX 1 1 PRO A 716 ALA A 720 5 5
HELIX 2 2 PRO A 821 PHE A 826 5 6
HELIX 3 3 GLU A 833 ILE A 844 1 12
HELIX 4 4 PRO A 845 GLU A 847 5 3
HELIX 5 5 ASN A 860 ASN A 871 1 12
HELIX 6 6 VAL A 923 LEU A 935 1 13
SHEET 1 A 5 ALA A 712 LEU A 715 0
SHEET 2 A 5 LEU A 723 HIS A 731 -1 O ILE A 725 N TRP A 714
SHEET 3 A 5 ILE A 736 ASN A 744 -1 O THR A 743 N GLU A 724
SHEET 4 A 5 SER A 781 ASN A 789 -1 O ILE A 782 N PHE A 742
SHEET 5 A 5 ILE A 765 PRO A 766 -1 N ILE A 765 O ASN A 789
SHEET 1 B 3 ALA A 754 PHE A 757 0
SHEET 2 B 3 ASN A 802 LYS A 808 -1 O LYS A 808 N ALA A 754
SHEET 3 B 3 VAL A 813 LEU A 819 -1 O PHE A 814 N VAL A 807
SHEET 1 C 5 GLU A 849 ILE A 854 0
SHEET 2 C 5 TYR A 912 CYS A 918 -1 O LEU A 914 N PHE A 852
SHEET 3 C 5 TRP A 898 ILE A 905 -1 N LEU A 900 O LYS A 917
SHEET 4 C 5 ASP A 885 LYS A 892 -1 N LEU A 891 O ILE A 899
SHEET 5 C 5 TYR A 874 ASN A 880 -1 N ILE A 876 O TYR A 888
CISPEP 1 GLU A 798 PRO A 799 0 5.08
CRYST1 122.088 47.103 58.945 90.00 97.66 90.00 C 1 2 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 0.008191 0.000000 0.001102 0.00000
SCALE2 0.000000 0.021230 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017118 0.00000
(ATOM LINES ARE NOT SHOWN.)
END