HEADER PROTEIN BINDING 19-SEP-17 6B27
TITLE CRYSTAL STRUCTURE OF HUMAN STAC2 TANDEM SH3 DOMAINS (296-411) IN
TITLE 2 COMPLEX WITH A CAV1.1 II-III LOOP PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SH3 AND CYSTEINE-RICH DOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 296-411;
COMPND 5 SYNONYM: 24B2/STAC2,SRC HOMOLOGY 3 AND CYSTEINE-RICH DOMAIN-
COMPND 6 CONTAINING PROTEIN 2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1S;
COMPND 10 CHAIN: G, H, I, J, K, L;
COMPND 11 FRAGMENT: RESIDUES 747-760;
COMPND 12 SYNONYM: CALCIUM CHANNEL,L TYPE,ALPHA-1 POLYPEPTIDE,ISOFORM 3,
COMPND 13 SKELETAL MUSCLE,VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV1.1;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: STAC2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS EXCITATION-CONTRACTION COUPLING, ION CHANNEL ADAPTOR PROTEIN, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.WONG KING YUEN,F.VAN PETEGEM
REVDAT 6 13-MAR-24 6B27 1 REMARK
REVDAT 5 08-JAN-20 6B27 1 REMARK
REVDAT 4 06-DEC-17 6B27 1 REMARK
REVDAT 3 22-NOV-17 6B27 1 JRNL
REVDAT 2 08-NOV-17 6B27 1 JRNL
REVDAT 1 25-OCT-17 6B27 0
JRNL AUTH S.M.WONG KING YUEN,M.CAMPIGLIO,C.C.TUNG,B.E.FLUCHER,
JRNL AUTH 2 F.VAN PETEGEM
JRNL TITL STRUCTURAL INSIGHTS INTO BINDING OF STAC PROTEINS TO
JRNL TITL 2 VOLTAGE-GATED CALCIUM CHANNELS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 E9520 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29078335
JRNL DOI 10.1073/PNAS.1708852114
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 79187
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4075
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) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5842
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5797
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.86000
REMARK 3 B22 (A**2) : -0.92000
REMARK 3 B33 (A**2) : 0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.111
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.358
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6135 ; 0.021 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5567 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8352 ; 1.935 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12970 ; 1.045 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 779 ; 6.009 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 300 ;36.998 ;24.300
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1000 ;13.237 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;18.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 870 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6914 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1259 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6B27 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000230119.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83341
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.49300
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.24M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 5.5, VAPOR DIFFUSION, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.96000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.33900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.32500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.33900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.96000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.32500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
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: 1120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: 3
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: 1150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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: 1210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J
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: 5
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: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, K
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
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: 1050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, L
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 SER A 292
REMARK 465 ASN A 293
REMARK 465 SER B 292
REMARK 465 ASN B 293
REMARK 465 SER B 385
REMARK 465 LYS B 386
REMARK 465 ASP B 387
REMARK 465 ALA B 388
REMARK 465 SER C 292
REMARK 465 ASN C 293
REMARK 465 SER C 385
REMARK 465 LYS C 386
REMARK 465 ASP C 387
REMARK 465 ALA C 388
REMARK 465 ASP C 389
REMARK 465 SER D 292
REMARK 465 ASN D 293
REMARK 465 SER E 292
REMARK 465 ASN E 293
REMARK 465 ALA E 294
REMARK 465 ASN E 295
REMARK 465 GLY E 383
REMARK 465 ARG E 384
REMARK 465 SER E 385
REMARK 465 LYS E 386
REMARK 465 ASP E 387
REMARK 465 ALA E 388
REMARK 465 GLU E 410
REMARK 465 ILE E 411
REMARK 465 SER F 292
REMARK 465 ASN F 293
REMARK 465 ALA F 294
REMARK 465 SER F 385
REMARK 465 LYS F 386
REMARK 465 ASP F 387
REMARK 465 ALA F 388
REMARK 465 ASP F 389
REMARK 465 GLU G 747
REMARK 465 ASP G 748
REMARK 465 ARG G 759
REMARK 465 PRO G 760
REMARK 465 GLU H 747
REMARK 465 ASP H 748
REMARK 465 GLU H 749
REMARK 465 GLU I 747
REMARK 465 ASP I 748
REMARK 465 PRO I 760
REMARK 465 GLU J 747
REMARK 465 ASP J 748
REMARK 465 ARG J 759
REMARK 465 PRO J 760
REMARK 465 GLU K 747
REMARK 465 ASP K 748
REMARK 465 ARG K 759
REMARK 465 PRO K 760
REMARK 465 GLU L 747
REMARK 465 ASP L 748
REMARK 465 GLU L 749
REMARK 465 ARG L 759
REMARK 465 PRO L 760
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 GLU A 327 CG CD OE1 OE2
REMARK 470 LYS A 386 CG CD CE NZ
REMARK 470 ASP A 387 CG OD1 OD2
REMARK 470 ARG A 393 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 398 CG CD CE NZ
REMARK 470 ARG A 400 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 393 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 398 CG CD CE NZ
REMARK 470 ARG B 400 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 384 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 384 CG CD NE CZ NH1 NH2
REMARK 470 SER D 385 OG
REMARK 470 LYS D 386 CG CD CE NZ
REMARK 470 ASP D 387 CG OD1 OD2
REMARK 470 ARG D 400 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 302 CG CD CE NZ
REMARK 470 LYS E 374 CG CD CE NZ
REMARK 470 ARG E 393 CG CD NE CZ NH1 NH2
REMARK 470 ARG E 400 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 399 CG CD CE NZ
REMARK 470 ARG F 400 CG CD NE CZ NH1 NH2
REMARK 470 GLU I 749 CG CD OE1 OE2
REMARK 470 GLU J 749 CG CD OE1 OE2
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 NH2 ARG D 348 O1 SO4 A 501 2.06
REMARK 500 OE2 GLU G 749 O HOH G 801 2.11
REMARK 500 NE ARG D 350 O2 SO4 A 501 2.19
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 318 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 MET A 320 CG - SD - CE ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 348 CG - CD - NE ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG A 348 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 348 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 384 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 337 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 357 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 357 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG C 318 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 318 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 337 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG C 337 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 348 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG C 357 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG D 337 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG D 337 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG D 348 CG - CD - NE ANGL. DEV. = -13.5 DEGREES
REMARK 500 ARG D 348 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP D 406 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG E 318 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG E 348 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG E 348 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG E 350 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG F 337 CG - CD - NE ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG F 384 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG G 757 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG G 757 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG I 757 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG I 757 NE - CZ - NH2 ANGL. DEV. = -3.9 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 ASP E 323 117.82 -163.85
REMARK 500 ASN F 365 115.24 -161.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 501
DBREF 6B27 A 296 411 UNP Q6ZMT1 STAC2_HUMAN 296 411
DBREF 6B27 B 296 411 UNP Q6ZMT1 STAC2_HUMAN 296 411
DBREF 6B27 C 296 411 UNP Q6ZMT1 STAC2_HUMAN 296 411
DBREF 6B27 D 296 411 UNP Q6ZMT1 STAC2_HUMAN 296 411
DBREF 6B27 E 296 411 UNP Q6ZMT1 STAC2_HUMAN 296 411
DBREF 6B27 F 296 411 UNP Q6ZMT1 STAC2_HUMAN 296 411
DBREF 6B27 G 747 760 UNP Q13698 CAC1S_HUMAN 747 760
DBREF 6B27 H 747 760 UNP Q13698 CAC1S_HUMAN 747 760
DBREF 6B27 I 747 760 UNP Q13698 CAC1S_HUMAN 747 760
DBREF 6B27 J 747 760 UNP Q13698 CAC1S_HUMAN 747 760
DBREF 6B27 K 747 760 UNP Q13698 CAC1S_HUMAN 747 760
DBREF 6B27 L 747 760 UNP Q13698 CAC1S_HUMAN 747 760
SEQADV 6B27 SER A 292 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN A 293 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ALA A 294 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN A 295 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 SER B 292 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN B 293 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ALA B 294 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN B 295 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 SER C 292 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN C 293 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ALA C 294 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN C 295 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 SER D 292 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN D 293 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ALA D 294 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN D 295 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 SER E 292 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN E 293 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ALA E 294 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN E 295 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 SER F 292 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN F 293 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ALA F 294 UNP Q6ZMT1 EXPRESSION TAG
SEQADV 6B27 ASN F 295 UNP Q6ZMT1 EXPRESSION TAG
SEQRES 1 A 120 SER ASN ALA ASN SER TYR VAL ALA LEU TYR LYS PHE LEU
SEQRES 2 A 120 PRO GLN GLU ASN ASN ASP LEU ALA LEU GLN PRO GLY ASP
SEQRES 3 A 120 ARG ILE MET LEU VAL ASP ASP SER ASN GLU ASP TRP TRP
SEQRES 4 A 120 LYS GLY LYS ILE GLY ASP ARG VAL GLY PHE PHE PRO ALA
SEQRES 5 A 120 ASN PHE VAL GLN ARG VAL ARG PRO GLY GLU ASN VAL TRP
SEQRES 6 A 120 ARG CYS CYS GLN PRO PHE SER GLY ASN LYS GLU GLN GLY
SEQRES 7 A 120 TYR MET SER LEU LYS GLU ASN GLN ILE CYS VAL GLY VAL
SEQRES 8 A 120 GLY ARG SER LYS ASP ALA ASP GLY PHE ILE ARG VAL SER
SEQRES 9 A 120 SER GLY LYS LYS ARG GLY LEU VAL PRO VAL ASP ALA LEU
SEQRES 10 A 120 THR GLU ILE
SEQRES 1 B 120 SER ASN ALA ASN SER TYR VAL ALA LEU TYR LYS PHE LEU
SEQRES 2 B 120 PRO GLN GLU ASN ASN ASP LEU ALA LEU GLN PRO GLY ASP
SEQRES 3 B 120 ARG ILE MET LEU VAL ASP ASP SER ASN GLU ASP TRP TRP
SEQRES 4 B 120 LYS GLY LYS ILE GLY ASP ARG VAL GLY PHE PHE PRO ALA
SEQRES 5 B 120 ASN PHE VAL GLN ARG VAL ARG PRO GLY GLU ASN VAL TRP
SEQRES 6 B 120 ARG CYS CYS GLN PRO PHE SER GLY ASN LYS GLU GLN GLY
SEQRES 7 B 120 TYR MET SER LEU LYS GLU ASN GLN ILE CYS VAL GLY VAL
SEQRES 8 B 120 GLY ARG SER LYS ASP ALA ASP GLY PHE ILE ARG VAL SER
SEQRES 9 B 120 SER GLY LYS LYS ARG GLY LEU VAL PRO VAL ASP ALA LEU
SEQRES 10 B 120 THR GLU ILE
SEQRES 1 C 120 SER ASN ALA ASN SER TYR VAL ALA LEU TYR LYS PHE LEU
SEQRES 2 C 120 PRO GLN GLU ASN ASN ASP LEU ALA LEU GLN PRO GLY ASP
SEQRES 3 C 120 ARG ILE MET LEU VAL ASP ASP SER ASN GLU ASP TRP TRP
SEQRES 4 C 120 LYS GLY LYS ILE GLY ASP ARG VAL GLY PHE PHE PRO ALA
SEQRES 5 C 120 ASN PHE VAL GLN ARG VAL ARG PRO GLY GLU ASN VAL TRP
SEQRES 6 C 120 ARG CYS CYS GLN PRO PHE SER GLY ASN LYS GLU GLN GLY
SEQRES 7 C 120 TYR MET SER LEU LYS GLU ASN GLN ILE CYS VAL GLY VAL
SEQRES 8 C 120 GLY ARG SER LYS ASP ALA ASP GLY PHE ILE ARG VAL SER
SEQRES 9 C 120 SER GLY LYS LYS ARG GLY LEU VAL PRO VAL ASP ALA LEU
SEQRES 10 C 120 THR GLU ILE
SEQRES 1 D 120 SER ASN ALA ASN SER TYR VAL ALA LEU TYR LYS PHE LEU
SEQRES 2 D 120 PRO GLN GLU ASN ASN ASP LEU ALA LEU GLN PRO GLY ASP
SEQRES 3 D 120 ARG ILE MET LEU VAL ASP ASP SER ASN GLU ASP TRP TRP
SEQRES 4 D 120 LYS GLY LYS ILE GLY ASP ARG VAL GLY PHE PHE PRO ALA
SEQRES 5 D 120 ASN PHE VAL GLN ARG VAL ARG PRO GLY GLU ASN VAL TRP
SEQRES 6 D 120 ARG CYS CYS GLN PRO PHE SER GLY ASN LYS GLU GLN GLY
SEQRES 7 D 120 TYR MET SER LEU LYS GLU ASN GLN ILE CYS VAL GLY VAL
SEQRES 8 D 120 GLY ARG SER LYS ASP ALA ASP GLY PHE ILE ARG VAL SER
SEQRES 9 D 120 SER GLY LYS LYS ARG GLY LEU VAL PRO VAL ASP ALA LEU
SEQRES 10 D 120 THR GLU ILE
SEQRES 1 E 120 SER ASN ALA ASN SER TYR VAL ALA LEU TYR LYS PHE LEU
SEQRES 2 E 120 PRO GLN GLU ASN ASN ASP LEU ALA LEU GLN PRO GLY ASP
SEQRES 3 E 120 ARG ILE MET LEU VAL ASP ASP SER ASN GLU ASP TRP TRP
SEQRES 4 E 120 LYS GLY LYS ILE GLY ASP ARG VAL GLY PHE PHE PRO ALA
SEQRES 5 E 120 ASN PHE VAL GLN ARG VAL ARG PRO GLY GLU ASN VAL TRP
SEQRES 6 E 120 ARG CYS CYS GLN PRO PHE SER GLY ASN LYS GLU GLN GLY
SEQRES 7 E 120 TYR MET SER LEU LYS GLU ASN GLN ILE CYS VAL GLY VAL
SEQRES 8 E 120 GLY ARG SER LYS ASP ALA ASP GLY PHE ILE ARG VAL SER
SEQRES 9 E 120 SER GLY LYS LYS ARG GLY LEU VAL PRO VAL ASP ALA LEU
SEQRES 10 E 120 THR GLU ILE
SEQRES 1 F 120 SER ASN ALA ASN SER TYR VAL ALA LEU TYR LYS PHE LEU
SEQRES 2 F 120 PRO GLN GLU ASN ASN ASP LEU ALA LEU GLN PRO GLY ASP
SEQRES 3 F 120 ARG ILE MET LEU VAL ASP ASP SER ASN GLU ASP TRP TRP
SEQRES 4 F 120 LYS GLY LYS ILE GLY ASP ARG VAL GLY PHE PHE PRO ALA
SEQRES 5 F 120 ASN PHE VAL GLN ARG VAL ARG PRO GLY GLU ASN VAL TRP
SEQRES 6 F 120 ARG CYS CYS GLN PRO PHE SER GLY ASN LYS GLU GLN GLY
SEQRES 7 F 120 TYR MET SER LEU LYS GLU ASN GLN ILE CYS VAL GLY VAL
SEQRES 8 F 120 GLY ARG SER LYS ASP ALA ASP GLY PHE ILE ARG VAL SER
SEQRES 9 F 120 SER GLY LYS LYS ARG GLY LEU VAL PRO VAL ASP ALA LEU
SEQRES 10 F 120 THR GLU ILE
SEQRES 1 G 14 GLU ASP GLU PRO GLU ILE PRO LEU SER PRO ARG PRO ARG
SEQRES 2 G 14 PRO
SEQRES 1 H 14 GLU ASP GLU PRO GLU ILE PRO LEU SER PRO ARG PRO ARG
SEQRES 2 H 14 PRO
SEQRES 1 I 14 GLU ASP GLU PRO GLU ILE PRO LEU SER PRO ARG PRO ARG
SEQRES 2 I 14 PRO
SEQRES 1 J 14 GLU ASP GLU PRO GLU ILE PRO LEU SER PRO ARG PRO ARG
SEQRES 2 J 14 PRO
SEQRES 1 K 14 GLU ASP GLU PRO GLU ILE PRO LEU SER PRO ARG PRO ARG
SEQRES 2 K 14 PRO
SEQRES 1 L 14 GLU ASP GLU PRO GLU ILE PRO LEU SER PRO ARG PRO ARG
SEQRES 2 L 14 PRO
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 B 501 5
HET SO4 C 501 5
HET SO4 D 501 5
HET CL E 501 1
HET CL E 502 1
HET SO4 E 503 5
HET SO4 F 501 5
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 13 SO4 8(O4 S 2-)
FORMUL 19 CL 2(CL 1-)
FORMUL 23 HOH *620(H2 O)
HELIX 1 AA1 PRO A 404 ASP A 406 5 3
HELIX 2 AA2 ASN C 365 GLY C 369 5 5
HELIX 3 AA3 PRO D 404 ASP D 406 5 3
HELIX 4 AA4 PRO E 404 ASP E 406 5 3
HELIX 5 AA5 PRO F 404 ASP F 406 5 3
SHEET 1 AA1 5 ARG A 337 PRO A 342 0
SHEET 2 AA1 5 TRP A 329 ILE A 334 -1 N ILE A 334 O ARG A 337
SHEET 3 AA1 5 ARG A 318 ASP A 323 -1 N VAL A 322 O LYS A 331
SHEET 4 AA1 5 SER A 296 ALA A 299 -1 N TYR A 297 O ILE A 319
SHEET 5 AA1 5 VAL A 346 ARG A 348 -1 O GLN A 347 N VAL A 298
SHEET 1 AA2 3 ILE A 378 GLY A 381 0
SHEET 2 AA2 3 ASN A 354 CYS A 358 -1 N TRP A 356 O CYS A 379
SHEET 3 AA2 3 LEU A 408 ILE A 411 -1 O THR A 409 N ARG A 357
SHEET 1 AA3 2 ILE A 392 SER A 396 0
SHEET 2 AA3 2 LYS A 399 VAL A 403 -1 O LYS A 399 N SER A 396
SHEET 1 AA4 5 ARG B 337 PRO B 342 0
SHEET 2 AA4 5 TRP B 329 ILE B 334 -1 N ILE B 334 O ARG B 337
SHEET 3 AA4 5 ARG B 318 ASP B 323 -1 N VAL B 322 O LYS B 331
SHEET 4 AA4 5 SER B 296 ALA B 299 -1 N TYR B 297 O ILE B 319
SHEET 5 AA4 5 VAL B 346 ARG B 348 -1 O GLN B 347 N VAL B 298
SHEET 1 AA5 3 ILE B 378 GLY B 381 0
SHEET 2 AA5 3 ASN B 354 CYS B 358 -1 N TRP B 356 O CYS B 379
SHEET 3 AA5 3 LEU B 408 GLU B 410 -1 O THR B 409 N ARG B 357
SHEET 1 AA6 2 PHE B 391 SER B 396 0
SHEET 2 AA6 2 LYS B 399 PRO B 404 -1 O LYS B 399 N SER B 396
SHEET 1 AA7 5 ARG C 337 PRO C 342 0
SHEET 2 AA7 5 TRP C 329 ILE C 334 -1 N ILE C 334 O ARG C 337
SHEET 3 AA7 5 ARG C 318 ASP C 323 -1 N VAL C 322 O LYS C 331
SHEET 4 AA7 5 SER C 296 ALA C 299 -1 N TYR C 297 O ILE C 319
SHEET 5 AA7 5 VAL C 346 ARG C 348 -1 O GLN C 347 N VAL C 298
SHEET 1 AA8 3 ILE C 378 GLY C 381 0
SHEET 2 AA8 3 ASN C 354 CYS C 358 -1 N TRP C 356 O CYS C 379
SHEET 3 AA8 3 LEU C 408 ILE C 411 -1 O THR C 409 N ARG C 357
SHEET 1 AA9 2 PHE C 391 SER C 396 0
SHEET 2 AA9 2 LYS C 399 PRO C 404 -1 O LYS C 399 N SER C 396
SHEET 1 AB1 5 ARG D 337 PRO D 342 0
SHEET 2 AB1 5 TRP D 329 ILE D 334 -1 N ILE D 334 O ARG D 337
SHEET 3 AB1 5 ARG D 318 ASP D 323 -1 N VAL D 322 O LYS D 331
SHEET 4 AB1 5 SER D 296 ALA D 299 -1 N TYR D 297 O ILE D 319
SHEET 5 AB1 5 VAL D 346 ARG D 348 -1 O GLN D 347 N VAL D 298
SHEET 1 AB2 3 ILE D 378 GLY D 381 0
SHEET 2 AB2 3 ASN D 354 CYS D 358 -1 N TRP D 356 O CYS D 379
SHEET 3 AB2 3 LEU D 408 GLU D 410 -1 O THR D 409 N ARG D 357
SHEET 1 AB3 2 ILE D 392 SER D 396 0
SHEET 2 AB3 2 LYS D 399 VAL D 403 -1 O LYS D 399 N SER D 396
SHEET 1 AB4 5 ARG E 337 PRO E 342 0
SHEET 2 AB4 5 TRP E 329 ILE E 334 -1 N ILE E 334 O ARG E 337
SHEET 3 AB4 5 ARG E 318 ASP E 323 -1 N VAL E 322 O LYS E 331
SHEET 4 AB4 5 TYR E 297 ALA E 299 -1 N TYR E 297 O ILE E 319
SHEET 5 AB4 5 VAL E 346 ARG E 348 -1 O GLN E 347 N VAL E 298
SHEET 1 AB5 3 ILE E 378 GLY E 381 0
SHEET 2 AB5 3 ASN E 354 CYS E 358 -1 N ASN E 354 O GLY E 381
SHEET 3 AB5 3 LEU E 408 THR E 409 -1 O THR E 409 N ARG E 357
SHEET 1 AB6 2 ILE E 392 SER E 396 0
SHEET 2 AB6 2 LYS E 399 VAL E 403 -1 O GLY E 401 N VAL E 394
SHEET 1 AB7 5 ARG F 337 PRO F 342 0
SHEET 2 AB7 5 TRP F 329 ILE F 334 -1 N ILE F 334 O ARG F 337
SHEET 3 AB7 5 ARG F 318 ASP F 323 -1 N VAL F 322 O LYS F 331
SHEET 4 AB7 5 SER F 296 ALA F 299 -1 N TYR F 297 O ILE F 319
SHEET 5 AB7 5 VAL F 346 VAL F 349 -1 O VAL F 349 N SER F 296
SHEET 1 AB8 3 ILE F 378 GLY F 381 0
SHEET 2 AB8 3 ASN F 354 CYS F 358 -1 N TRP F 356 O CYS F 379
SHEET 3 AB8 3 LEU F 408 GLU F 410 -1 O THR F 409 N ARG F 357
SHEET 1 AB9 2 ILE F 392 SER F 396 0
SHEET 2 AB9 2 LYS F 399 VAL F 403 -1 O LYS F 399 N SER F 396
SITE 1 AC1 5 ARG A 348 ARG A 350 HOH A 695 ARG D 348
SITE 2 AC1 5 ARG D 350
SITE 1 AC2 6 ALA A 294 ASN A 295 SER A 296 ARG A 348
SITE 2 AC2 6 PRO A 351 HOH A 685
SITE 1 AC3 5 GLN A 347 ARG A 348 ARG A 350 HOH A 613
SITE 2 AC3 5 HOH A 618
SITE 1 AC4 6 GLN B 347 ARG B 350 HOH B 602 HOH B 604
SITE 2 AC4 6 HOH B 611 ARG E 350
SITE 1 AC5 7 GLN C 347 ARG C 350 ARG C 400 HOH C 608
SITE 2 AC5 7 HOH C 611 HOH C 633 ARG F 350
SITE 1 AC6 7 ALA D 294 ASN D 295 SER D 296 ARG D 348
SITE 2 AC6 7 PRO D 351 HOH D 639 HOH D 675
SITE 1 AC7 3 ALA E 312 ARG E 337 HOH E 679
SITE 1 AC8 2 HOH C 612 GLU E 375
SITE 1 AC9 2 ARG B 400 ARG E 350
SITE 1 AD1 5 ARG C 393 ARG C 400 ARG F 348 ARG F 350
SITE 2 AD1 5 HOH F 605
CRYST1 47.920 114.650 144.678 90.00 90.00 90.00 P 21 21 21 24
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 0.020868 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008722 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006912 0.00000
(ATOM LINES ARE NOT SHOWN.)
END