HEADER SIGNALING PROTEIN 31-MAY-11 3S8V
TITLE CRYSTAL STRUCTURE OF LRP6-DKK1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 6;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: E3E4, RESIDUES 629-1243;
COMPND 5 SYNONYM: LRP-6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DICKKOPF-RELATED PROTEIN 1;
COMPND 9 CHAIN: X;
COMPND 10 FRAGMENT: DKK1C, RESIDUES 184-266;
COMPND 11 SYNONYM: DICKKOPF-1, DKK-1, HDKK-1, SK;
COMPND 12 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: LRP6;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACGP67B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: DKK1, UNQ492/PRO1008;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET32M
KEYWDS WNT, RECEPTOR, LRP5, LRP6, LDL RECEPTOR-LIKE PROTEIN, DICKKOPF (DKK),
KEYWDS 2 YWTD B-PROPELLER, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.CHENG,W.XU
REVDAT 3 13-SEP-23 3S8V 1 SEQADV
REVDAT 2 23-NOV-11 3S8V 1 JRNL
REVDAT 1 26-OCT-11 3S8V 0
JRNL AUTH Z.CHENG,T.BIECHELE,Z.WEI,S.MORRONE,R.T.MOON,L.WANG,W.XU
JRNL TITL CRYSTAL STRUCTURES OF THE EXTRACELLULAR DOMAIN OF LRP6 AND
JRNL TITL 2 ITS COMPLEX WITH DKK1.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 18 1204 2011
JRNL REFN ISSN 1545-9993
JRNL PMID 21984209
JRNL DOI 10.1038/NSMB.2139
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 27740
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1485
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1880
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.3240
REMARK 3 BIN FREE R VALUE SET COUNT : 83
REMARK 3 BIN FREE R VALUE : 0.4080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10177
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) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.12
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.20000
REMARK 3 B22 (A**2) : -5.09000
REMARK 3 B33 (A**2) : 8.29000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.562
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.462
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.364
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10403 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14105 ; 1.082 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1268 ; 5.462 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 514 ;36.274 ;23.658
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1786 ;18.467 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;14.872 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1545 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7927 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 629 A 1243 5
REMARK 3 1 B 629 B 1243 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2388 ; 0.590 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 2382 ; 0.820 ; 5.000
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3S8V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065907.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-11; 10-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; ALS
REMARK 200 BEAMLINE : 8.2.2; 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999; 0.999
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30419
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1IJQ AND 3S8Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM CITRIC ACID, 80MM BIS-TRIS
REMARK 280 PROPANE PH 8.8, 19-20% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 47.19200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.61300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.52500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.61300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.19200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.52500
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
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: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 HIS A 621
REMARK 465 HIS A 622
REMARK 465 HIS A 623
REMARK 465 HIS A 624
REMARK 465 HIS A 625
REMARK 465 HIS A 626
REMARK 465 HIS A 627
REMARK 465 HIS A 628
REMARK 465 VAL A 909
REMARK 465 GLY A 910
REMARK 465 GLN A 953
REMARK 465 SER A 954
REMARK 465 SER A 1006
REMARK 465 VAL A 1007
REMARK 465 PRO A 1008
REMARK 465 SER A 1009
REMARK 465 GLN A 1010
REMARK 465 ASN A 1011
REMARK 465 LEU A 1012
REMARK 465 GLU A 1013
REMARK 465 THR A 1173
REMARK 465 GLY A 1174
REMARK 465 ARG A 1175
REMARK 465 HIS B 621
REMARK 465 HIS B 622
REMARK 465 HIS B 623
REMARK 465 HIS B 624
REMARK 465 HIS B 625
REMARK 465 HIS B 626
REMARK 465 HIS B 627
REMARK 465 HIS B 628
REMARK 465 VAL B 629
REMARK 465 PRO B 630
REMARK 465 SER B 1005
REMARK 465 SER B 1006
REMARK 465 VAL B 1007
REMARK 465 PRO B 1008
REMARK 465 SER B 1009
REMARK 465 GLN B 1010
REMARK 465 ASN B 1011
REMARK 465 LEU B 1012
REMARK 465 GLU B 1013
REMARK 465 GLY X 179
REMARK 465 PRO X 180
REMARK 465 GLY X 181
REMARK 465 SER X 182
REMARK 465 GLY X 183
REMARK 465 LYS X 249
REMARK 465 ASP X 250
REMARK 465 HIS X 251
REMARK 465 HIS X 252
REMARK 465 GLN X 253
REMARK 465 ALA X 254
REMARK 465 SER X 255
REMARK 465 ASN X 256
REMARK 465 SER X 257
REMARK 465 HIS X 266
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 ARG X 265 O
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 ARG A 639 -61.75 67.33
REMARK 500 ASN A 650 34.55 -162.05
REMARK 500 ASN A 651 -164.26 -66.61
REMARK 500 SER A 665 -78.47 -130.22
REMARK 500 ALA A 695 33.39 72.18
REMARK 500 ASP A 705 -88.33 -143.93
REMARK 500 MET A 710 130.67 -175.96
REMARK 500 TRP A 744 -23.16 -149.99
REMARK 500 ASP A 748 -86.69 -83.86
REMARK 500 ARG A 751 -85.34 -104.78
REMARK 500 TRP A 767 -115.97 -102.77
REMARK 500 MET A 778 10.02 -66.94
REMARK 500 ASN A 789 73.57 -112.03
REMARK 500 ASN A 794 -45.93 -133.54
REMARK 500 HIS A 834 71.59 -152.98
REMARK 500 PHE A 836 -74.70 -138.61
REMARK 500 TYR A 841 -90.67 -117.82
REMARK 500 GLN A 842 -100.05 -89.80
REMARK 500 TYR A 875 93.30 63.34
REMARK 500 ASP A 878 174.68 51.64
REMARK 500 ILE A 879 137.58 171.95
REMARK 500 ASN A 897 13.78 59.02
REMARK 500 HIS A 902 -82.15 -134.53
REMARK 500 HIS A 919 -20.81 86.06
REMARK 500 GLN A 940 -147.49 -101.88
REMARK 500 ILE A 949 76.00 -103.14
REMARK 500 ARG A 965 -71.47 -118.20
REMARK 500 ARG A 985 -45.82 70.59
REMARK 500 TYR A1017 -54.17 -126.75
REMARK 500 GLN A1056 -23.09 74.64
REMARK 500 ARG A1060 -79.82 -119.44
REMARK 500 ARG A1079 -6.71 58.57
REMARK 500 LEU A1088 -8.19 -58.75
REMARK 500 SER A1102 -48.13 -143.12
REMARK 500 LEU A1145 -50.36 -122.83
REMARK 500 PHE A1153 -70.04 -95.67
REMARK 500 GLU A1154 -74.19 -128.84
REMARK 500 GLN A1182 108.70 -161.42
REMARK 500 ALA A1186 -79.94 -57.08
REMARK 500 ASN A1211 19.60 48.08
REMARK 500 HIS A1216 -68.14 -128.63
REMARK 500 PRO A1231 178.95 -54.27
REMARK 500 LEU A1237 -165.72 -100.38
REMARK 500 ARG B 638 -163.27 -104.81
REMARK 500 ALA B 640 -2.41 68.31
REMARK 500 ASN B 650 -132.60 45.82
REMARK 500 ASN B 651 -47.69 70.84
REMARK 500 ASP B 705 -59.63 -135.05
REMARK 500 MET B 710 119.00 -169.44
REMARK 500 SER B 749 84.07 -158.34
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3S8Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LRP6-E3E4
REMARK 900 RELATED ID: 3S94 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF LRP6-E1E2
DBREF 3S8V A 629 1243 UNP O75581 LRP6_HUMAN 629 1243
DBREF 3S8V B 629 1243 UNP O75581 LRP6_HUMAN 629 1243
DBREF 3S8V X 183 266 UNP O94907 DKK1_HUMAN 183 266
SEQADV 3S8V HIS A 621 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 622 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 623 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 624 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 625 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 626 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 627 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS A 628 UNP O75581 EXPRESSION TAG
SEQADV 3S8V ILE A 1062 UNP O75581 VAL 1062 CONFLICT
SEQADV 3S8V HIS B 621 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 622 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 623 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 624 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 625 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 626 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 627 UNP O75581 EXPRESSION TAG
SEQADV 3S8V HIS B 628 UNP O75581 EXPRESSION TAG
SEQADV 3S8V ILE B 1062 UNP O75581 VAL 1062 CONFLICT
SEQADV 3S8V GLY X 179 UNP O94907 EXPRESSION TAG
SEQADV 3S8V PRO X 180 UNP O94907 EXPRESSION TAG
SEQADV 3S8V GLY X 181 UNP O94907 EXPRESSION TAG
SEQADV 3S8V SER X 182 UNP O94907 EXPRESSION TAG
SEQRES 1 A 623 HIS HIS HIS HIS HIS HIS HIS HIS VAL PRO GLU ALA PHE
SEQRES 2 A 623 LEU LEU PHE SER ARG ARG ALA ASP ILE ARG ARG ILE SER
SEQRES 3 A 623 LEU GLU THR ASN ASN ASN ASN VAL ALA ILE PRO LEU THR
SEQRES 4 A 623 GLY VAL LYS GLU ALA SER ALA LEU ASP PHE ASP VAL THR
SEQRES 5 A 623 ASP ASN ARG ILE TYR TRP THR ASP ILE SER LEU LYS THR
SEQRES 6 A 623 ILE SER ARG ALA PHE MET ASN GLY SER ALA LEU GLU HIS
SEQRES 7 A 623 VAL VAL GLU PHE GLY LEU ASP TYR PRO GLU GLY MET ALA
SEQRES 8 A 623 VAL ASP TRP LEU GLY LYS ASN LEU TYR TRP ALA ASP THR
SEQRES 9 A 623 GLY THR ASN ARG ILE GLU VAL SER LYS LEU ASP GLY GLN
SEQRES 10 A 623 HIS ARG GLN VAL LEU VAL TRP LYS ASP LEU ASP SER PRO
SEQRES 11 A 623 ARG ALA LEU ALA LEU ASP PRO ALA GLU GLY PHE MET TYR
SEQRES 12 A 623 TRP THR GLU TRP GLY GLY LYS PRO LYS ILE ASP ARG ALA
SEQRES 13 A 623 ALA MET ASP GLY SER GLU ARG THR THR LEU VAL PRO ASN
SEQRES 14 A 623 VAL GLY ARG ALA ASN GLY LEU THR ILE ASP TYR ALA LYS
SEQRES 15 A 623 ARG ARG LEU TYR TRP THR ASP LEU ASP THR ASN LEU ILE
SEQRES 16 A 623 GLU SER SER ASN MET LEU GLY LEU ASN ARG GLU VAL ILE
SEQRES 17 A 623 ALA ASP ASP LEU PRO HIS PRO PHE GLY LEU THR GLN TYR
SEQRES 18 A 623 GLN ASP TYR ILE TYR TRP THR ASP TRP SER ARG ARG SER
SEQRES 19 A 623 ILE GLU ARG ALA ASN LYS THR SER GLY GLN ASN ARG THR
SEQRES 20 A 623 ILE ILE GLN GLY HIS LEU ASP TYR VAL MET ASP ILE LEU
SEQRES 21 A 623 VAL PHE HIS SER SER ARG GLN SER GLY TRP ASN GLU CYS
SEQRES 22 A 623 ALA SER SER ASN GLY HIS CYS SER HIS LEU CYS LEU ALA
SEQRES 23 A 623 VAL PRO VAL GLY GLY PHE VAL CYS GLY CYS PRO ALA HIS
SEQRES 24 A 623 TYR SER LEU ASN ALA ASP ASN ARG THR CYS SER ALA PRO
SEQRES 25 A 623 THR THR PHE LEU LEU PHE SER GLN LYS SER ALA ILE ASN
SEQRES 26 A 623 ARG MET VAL ILE ASP GLU GLN GLN SER PRO ASP ILE ILE
SEQRES 27 A 623 LEU PRO ILE HIS SER LEU ARG ASN VAL ARG ALA ILE ASP
SEQRES 28 A 623 TYR ASP PRO LEU ASP LYS GLN LEU TYR TRP ILE ASP SER
SEQRES 29 A 623 ARG GLN ASN MET ILE ARG LYS ALA GLN GLU ASP GLY SER
SEQRES 30 A 623 GLN GLY PHE THR VAL VAL VAL SER SER VAL PRO SER GLN
SEQRES 31 A 623 ASN LEU GLU ILE GLN PRO TYR ASP LEU SER ILE ASP ILE
SEQRES 32 A 623 TYR SER ARG TYR ILE TYR TRP THR CYS GLU ALA THR ASN
SEQRES 33 A 623 VAL ILE ASN VAL THR ARG LEU ASP GLY ARG SER VAL GLY
SEQRES 34 A 623 VAL VAL LEU LYS GLY GLU GLN ASP ARG PRO ARG ALA ILE
SEQRES 35 A 623 VAL VAL ASN PRO GLU LYS GLY TYR MET TYR PHE THR ASN
SEQRES 36 A 623 LEU GLN GLU ARG SER PRO LYS ILE GLU ARG ALA ALA LEU
SEQRES 37 A 623 ASP GLY THR GLU ARG GLU VAL LEU PHE PHE SER GLY LEU
SEQRES 38 A 623 SER LYS PRO ILE ALA LEU ALA LEU ASP SER ARG LEU GLY
SEQRES 39 A 623 LYS LEU PHE TRP ALA ASP SER ASP LEU ARG ARG ILE GLU
SEQRES 40 A 623 SER SER ASP LEU SER GLY ALA ASN ARG ILE VAL LEU GLU
SEQRES 41 A 623 ASP SER ASN ILE LEU GLN PRO VAL GLY LEU THR VAL PHE
SEQRES 42 A 623 GLU ASN TRP LEU TYR TRP ILE ASP LYS GLN GLN GLN MET
SEQRES 43 A 623 ILE GLU LYS ILE ASP MET THR GLY ARG GLU GLY ARG THR
SEQRES 44 A 623 LYS VAL GLN ALA ARG ILE ALA GLN LEU SER ASP ILE HIS
SEQRES 45 A 623 ALA VAL LYS GLU LEU ASN LEU GLN GLU TYR ARG GLN HIS
SEQRES 46 A 623 PRO CYS ALA GLN ASP ASN GLY GLY CYS SER HIS ILE CYS
SEQRES 47 A 623 LEU VAL LYS GLY ASP GLY THR THR ARG CYS SER CYS PRO
SEQRES 48 A 623 MET HIS LEU VAL LEU LEU GLN ASP GLU LEU SER CYS
SEQRES 1 B 623 HIS HIS HIS HIS HIS HIS HIS HIS VAL PRO GLU ALA PHE
SEQRES 2 B 623 LEU LEU PHE SER ARG ARG ALA ASP ILE ARG ARG ILE SER
SEQRES 3 B 623 LEU GLU THR ASN ASN ASN ASN VAL ALA ILE PRO LEU THR
SEQRES 4 B 623 GLY VAL LYS GLU ALA SER ALA LEU ASP PHE ASP VAL THR
SEQRES 5 B 623 ASP ASN ARG ILE TYR TRP THR ASP ILE SER LEU LYS THR
SEQRES 6 B 623 ILE SER ARG ALA PHE MET ASN GLY SER ALA LEU GLU HIS
SEQRES 7 B 623 VAL VAL GLU PHE GLY LEU ASP TYR PRO GLU GLY MET ALA
SEQRES 8 B 623 VAL ASP TRP LEU GLY LYS ASN LEU TYR TRP ALA ASP THR
SEQRES 9 B 623 GLY THR ASN ARG ILE GLU VAL SER LYS LEU ASP GLY GLN
SEQRES 10 B 623 HIS ARG GLN VAL LEU VAL TRP LYS ASP LEU ASP SER PRO
SEQRES 11 B 623 ARG ALA LEU ALA LEU ASP PRO ALA GLU GLY PHE MET TYR
SEQRES 12 B 623 TRP THR GLU TRP GLY GLY LYS PRO LYS ILE ASP ARG ALA
SEQRES 13 B 623 ALA MET ASP GLY SER GLU ARG THR THR LEU VAL PRO ASN
SEQRES 14 B 623 VAL GLY ARG ALA ASN GLY LEU THR ILE ASP TYR ALA LYS
SEQRES 15 B 623 ARG ARG LEU TYR TRP THR ASP LEU ASP THR ASN LEU ILE
SEQRES 16 B 623 GLU SER SER ASN MET LEU GLY LEU ASN ARG GLU VAL ILE
SEQRES 17 B 623 ALA ASP ASP LEU PRO HIS PRO PHE GLY LEU THR GLN TYR
SEQRES 18 B 623 GLN ASP TYR ILE TYR TRP THR ASP TRP SER ARG ARG SER
SEQRES 19 B 623 ILE GLU ARG ALA ASN LYS THR SER GLY GLN ASN ARG THR
SEQRES 20 B 623 ILE ILE GLN GLY HIS LEU ASP TYR VAL MET ASP ILE LEU
SEQRES 21 B 623 VAL PHE HIS SER SER ARG GLN SER GLY TRP ASN GLU CYS
SEQRES 22 B 623 ALA SER SER ASN GLY HIS CYS SER HIS LEU CYS LEU ALA
SEQRES 23 B 623 VAL PRO VAL GLY GLY PHE VAL CYS GLY CYS PRO ALA HIS
SEQRES 24 B 623 TYR SER LEU ASN ALA ASP ASN ARG THR CYS SER ALA PRO
SEQRES 25 B 623 THR THR PHE LEU LEU PHE SER GLN LYS SER ALA ILE ASN
SEQRES 26 B 623 ARG MET VAL ILE ASP GLU GLN GLN SER PRO ASP ILE ILE
SEQRES 27 B 623 LEU PRO ILE HIS SER LEU ARG ASN VAL ARG ALA ILE ASP
SEQRES 28 B 623 TYR ASP PRO LEU ASP LYS GLN LEU TYR TRP ILE ASP SER
SEQRES 29 B 623 ARG GLN ASN MET ILE ARG LYS ALA GLN GLU ASP GLY SER
SEQRES 30 B 623 GLN GLY PHE THR VAL VAL VAL SER SER VAL PRO SER GLN
SEQRES 31 B 623 ASN LEU GLU ILE GLN PRO TYR ASP LEU SER ILE ASP ILE
SEQRES 32 B 623 TYR SER ARG TYR ILE TYR TRP THR CYS GLU ALA THR ASN
SEQRES 33 B 623 VAL ILE ASN VAL THR ARG LEU ASP GLY ARG SER VAL GLY
SEQRES 34 B 623 VAL VAL LEU LYS GLY GLU GLN ASP ARG PRO ARG ALA ILE
SEQRES 35 B 623 VAL VAL ASN PRO GLU LYS GLY TYR MET TYR PHE THR ASN
SEQRES 36 B 623 LEU GLN GLU ARG SER PRO LYS ILE GLU ARG ALA ALA LEU
SEQRES 37 B 623 ASP GLY THR GLU ARG GLU VAL LEU PHE PHE SER GLY LEU
SEQRES 38 B 623 SER LYS PRO ILE ALA LEU ALA LEU ASP SER ARG LEU GLY
SEQRES 39 B 623 LYS LEU PHE TRP ALA ASP SER ASP LEU ARG ARG ILE GLU
SEQRES 40 B 623 SER SER ASP LEU SER GLY ALA ASN ARG ILE VAL LEU GLU
SEQRES 41 B 623 ASP SER ASN ILE LEU GLN PRO VAL GLY LEU THR VAL PHE
SEQRES 42 B 623 GLU ASN TRP LEU TYR TRP ILE ASP LYS GLN GLN GLN MET
SEQRES 43 B 623 ILE GLU LYS ILE ASP MET THR GLY ARG GLU GLY ARG THR
SEQRES 44 B 623 LYS VAL GLN ALA ARG ILE ALA GLN LEU SER ASP ILE HIS
SEQRES 45 B 623 ALA VAL LYS GLU LEU ASN LEU GLN GLU TYR ARG GLN HIS
SEQRES 46 B 623 PRO CYS ALA GLN ASP ASN GLY GLY CYS SER HIS ILE CYS
SEQRES 47 B 623 LEU VAL LYS GLY ASP GLY THR THR ARG CYS SER CYS PRO
SEQRES 48 B 623 MET HIS LEU VAL LEU LEU GLN ASP GLU LEU SER CYS
SEQRES 1 X 88 GLY PRO GLY SER GLY GLN GLU GLY SER VAL CYS LEU ARG
SEQRES 2 X 88 SER SER ASP CYS ALA SER GLY LEU CYS CYS ALA ARG HIS
SEQRES 3 X 88 PHE TRP SER LYS ILE CYS LYS PRO VAL LEU LYS GLU GLY
SEQRES 4 X 88 GLN VAL CYS THR LYS HIS ARG ARG LYS GLY SER HIS GLY
SEQRES 5 X 88 LEU GLU ILE PHE GLN ARG CYS TYR CYS GLY GLU GLY LEU
SEQRES 6 X 88 SER CYS ARG ILE GLN LYS ASP HIS HIS GLN ALA SER ASN
SEQRES 7 X 88 SER SER ARG LEU HIS THR CYS GLN ARG HIS
HELIX 1 1 ASN A 891 CYS A 900 5 10
HELIX 2 2 ASN A 1198 GLN A 1204 1 7
HELIX 3 3 GLN A 1209 CYS A 1214 5 6
HELIX 4 4 ASN B 891 CYS B 900 5 10
HELIX 5 5 ASN B 1198 GLN B 1204 1 7
HELIX 6 6 GLN B 1209 CYS B 1214 5 6
HELIX 7 7 ARG X 191 CYS X 195 5 5
HELIX 8 8 GLY X 227 GLU X 232 1 6
SHEET 1 A 4 ASN A 653 ALA A 655 0
SHEET 2 A 4 ILE A 642 SER A 646 -1 N ARG A 644 O VAL A 654
SHEET 3 A 4 PHE A 633 SER A 637 -1 N LEU A 634 O ILE A 645
SHEET 4 A 4 MET A 877 PHE A 882 -1 O PHE A 882 N PHE A 633
SHEET 1 B 4 ALA A 664 ASP A 670 0
SHEET 2 B 4 ARG A 675 ASP A 680 -1 O TYR A 677 N ASP A 668
SHEET 3 B 4 THR A 685 PHE A 690 -1 O ALA A 689 N ILE A 676
SHEET 4 B 4 GLU A 697 VAL A 700 -1 O VAL A 699 N ILE A 686
SHEET 1 C 4 GLY A 709 ASP A 713 0
SHEET 2 C 4 ASN A 718 ASP A 723 -1 O ALA A 722 N GLY A 709
SHEET 3 C 4 ARG A 728 LYS A 733 -1 O SER A 732 N LEU A 719
SHEET 4 C 4 GLN A 740 VAL A 743 -1 O GLN A 740 N VAL A 731
SHEET 1 D 4 PRO A 750 ASP A 756 0
SHEET 2 D 4 PHE A 761 GLU A 766 -1 O TYR A 763 N ALA A 754
SHEET 3 D 4 LYS A 772 ALA A 777 -1 O ALA A 776 N MET A 762
SHEET 4 D 4 THR A 784 VAL A 787 -1 O THR A 784 N ARG A 775
SHEET 1 E 4 THR A 797 ASP A 799 0
SHEET 2 E 4 ARG A 804 ASP A 809 -1 O ARG A 804 N ASP A 799
SHEET 3 E 4 LEU A 814 ASN A 819 -1 O LEU A 814 N ASP A 809
SHEET 4 E 4 GLU A 826 ALA A 829 -1 O ILE A 828 N ILE A 815
SHEET 1 F 4 PRO A 835 GLN A 840 0
SHEET 2 F 4 TYR A 844 ASP A 849 -1 O TYR A 846 N THR A 839
SHEET 3 F 4 SER A 854 ASN A 859 -1 O ALA A 858 N ILE A 845
SHEET 4 F 4 THR A 867 GLN A 870 -1 O GLN A 870 N ILE A 855
SHEET 1 G 2 LEU A 903 ALA A 906 0
SHEET 2 G 2 PHE A 912 GLY A 915 -1 O GLY A 915 N LEU A 903
SHEET 1 H 2 SER A 921 LEU A 922 0
SHEET 2 H 2 CYS A 929 SER A 930 -1 O SER A 930 N SER A 921
SHEET 1 I 4 ILE A 957 ILE A 958 0
SHEET 2 I 4 ILE A 944 VAL A 948 -1 N ARG A 946 O ILE A 957
SHEET 3 I 4 PHE A 935 SER A 939 -1 N LEU A 936 O MET A 947
SHEET 4 I 4 ASP A1190 VAL A1194 -1 O HIS A1192 N LEU A 937
SHEET 1 J 4 ASN A 966 ASP A 973 0
SHEET 2 J 4 GLN A 978 SER A 984 -1 O SER A 984 N ASN A 966
SHEET 3 J 4 MET A 988 ALA A 992 -1 O ARG A 990 N TRP A 981
SHEET 4 J 4 PHE A1000 VAL A1003 -1 O PHE A1000 N LYS A 991
SHEET 1 K 4 PRO A1016 ASP A1022 0
SHEET 2 K 4 TYR A1027 CYS A1032 -1 O TYR A1029 N SER A1020
SHEET 3 K 4 VAL A1037 ARG A1042 -1 O THR A1041 N ILE A1028
SHEET 4 K 4 SER A1047 LEU A1052 -1 O GLY A1049 N VAL A1040
SHEET 1 L 4 PRO A1059 ASN A1065 0
SHEET 2 L 4 TYR A1070 ASN A1075 -1 O THR A1074 N ARG A1060
SHEET 3 L 4 LYS A1082 ALA A1087 -1 O ALA A1086 N MET A1071
SHEET 4 L 4 GLU A1094 PHE A1097 -1 O GLU A1094 N ARG A1085
SHEET 1 M 4 PRO A1104 ASP A1110 0
SHEET 2 M 4 LYS A1115 ASP A1120 -1 O PHE A1117 N ALA A1108
SHEET 3 M 4 ARG A1125 ASP A1130 -1 O SER A1129 N LEU A1116
SHEET 4 M 4 ILE A1137 GLU A1140 -1 O LEU A1139 N ILE A1126
SHEET 1 N 4 PRO A1147 VAL A1152 0
SHEET 2 N 4 TRP A1156 ASP A1161 -1 O TYR A1158 N THR A1151
SHEET 3 N 4 MET A1166 ASP A1171 -1 O GLU A1168 N TRP A1159
SHEET 4 N 4 THR A1179 GLN A1182 -1 O VAL A1181 N ILE A1167
SHEET 1 O 2 ILE A1217 CYS A1218 0
SHEET 2 O 2 CYS A1228 SER A1229 -1 O SER A1229 N ILE A1217
SHEET 1 P 4 ASN B 653 ALA B 655 0
SHEET 2 P 4 ILE B 642 SER B 646 -1 N ARG B 644 O VAL B 654
SHEET 3 P 4 PHE B 633 SER B 637 -1 N PHE B 636 O ARG B 643
SHEET 4 P 4 ILE B 879 PHE B 882 -1 O PHE B 882 N PHE B 633
SHEET 1 Q 4 ALA B 664 ASP B 670 0
SHEET 2 Q 4 ARG B 675 ASP B 680 -1 O TYR B 677 N ASP B 668
SHEET 3 Q 4 THR B 685 PHE B 690 -1 O ALA B 689 N ILE B 676
SHEET 4 Q 4 GLU B 697 VAL B 700 -1 O GLU B 697 N ARG B 688
SHEET 1 R 4 GLY B 709 ASP B 713 0
SHEET 2 R 4 ASN B 718 ASP B 723 -1 O ALA B 722 N GLY B 709
SHEET 3 R 4 ARG B 728 LYS B 733 -1 O SER B 732 N LEU B 719
SHEET 4 R 4 GLN B 740 VAL B 743 -1 O GLN B 740 N VAL B 731
SHEET 1 S 4 PRO B 750 ASP B 756 0
SHEET 2 S 4 PHE B 761 GLU B 766 -1 O THR B 765 N ARG B 751
SHEET 3 S 4 LYS B 772 ALA B 777 -1 O ALA B 776 N MET B 762
SHEET 4 S 4 THR B 784 VAL B 787 -1 O THR B 784 N ARG B 775
SHEET 1 T 4 THR B 797 ASP B 799 0
SHEET 2 T 4 ARG B 804 ASP B 809 -1 O ARG B 804 N ASP B 799
SHEET 3 T 4 LEU B 814 ASN B 819 -1 O SER B 818 N LEU B 805
SHEET 4 T 4 GLU B 826 ALA B 829 -1 O ILE B 828 N ILE B 815
SHEET 1 U 4 PRO B 835 GLN B 840 0
SHEET 2 U 4 TYR B 844 ASP B 849 -1 O TYR B 846 N THR B 839
SHEET 3 U 4 SER B 854 ASN B 859 -1 O GLU B 856 N TRP B 847
SHEET 4 U 4 THR B 867 GLN B 870 -1 O ILE B 869 N ILE B 855
SHEET 1 V 2 LEU B 903 ALA B 906 0
SHEET 2 V 2 PHE B 912 GLY B 915 -1 O GLY B 915 N LEU B 903
SHEET 1 W 2 SER B 921 LEU B 922 0
SHEET 2 W 2 CYS B 929 SER B 930 -1 O SER B 930 N SER B 921
SHEET 1 X 4 ILE B 957 ILE B 958 0
SHEET 2 X 4 ALA B 943 MET B 947 -1 N ARG B 946 O ILE B 957
SHEET 3 X 4 PHE B 935 GLN B 940 -1 N LEU B 936 O MET B 947
SHEET 4 X 4 LEU B1188 VAL B1194 -1 O SER B1189 N SER B 939
SHEET 1 Y 4 VAL B 967 ASP B 973 0
SHEET 2 Y 4 GLN B 978 ASP B 983 -1 O ILE B 982 N ARG B 968
SHEET 3 Y 4 MET B 988 ALA B 992 -1 O ALA B 992 N LEU B 979
SHEET 4 Y 4 PHE B1000 VAL B1003 -1 O PHE B1000 N LYS B 991
SHEET 1 Z 4 PRO B1016 ASP B1022 0
SHEET 2 Z 4 TYR B1027 CYS B1032 -1 O TYR B1029 N SER B1020
SHEET 3 Z 4 VAL B1037 ARG B1042 -1 O VAL B1037 N CYS B1032
SHEET 4 Z 4 SER B1047 LYS B1053 -1 O GLY B1049 N VAL B1040
SHEET 1 AA 4 PRO B1059 ASN B1065 0
SHEET 2 AA 4 TYR B1070 GLN B1077 -1 O TYR B1072 N VAL B1063
SHEET 3 AA 4 SER B1080 ALA B1087 -1 O GLU B1084 N PHE B1073
SHEET 4 AA 4 GLU B1094 PHE B1097 -1 O LEU B1096 N ILE B1083
SHEET 1 AB 4 PRO B1104 ASP B1110 0
SHEET 2 AB 4 LYS B1115 ASP B1120 -1 O PHE B1117 N ALA B1108
SHEET 3 AB 4 ARG B1125 ASP B1130 -1 O SER B1129 N LEU B1116
SHEET 4 AB 4 ILE B1137 GLU B1140 -1 O LEU B1139 N ILE B1126
SHEET 1 AC 4 PRO B1147 VAL B1152 0
SHEET 2 AC 4 TRP B1156 ASP B1161 -1 O ILE B1160 N VAL B1148
SHEET 3 AC 4 MET B1166 ASP B1171 -1 O MET B1166 N ASP B1161
SHEET 4 AC 4 THR B1179 GLN B1182 -1 O VAL B1181 N ILE B1167
SHEET 1 AD 2 ILE B1217 VAL B1220 0
SHEET 2 AD 2 THR B1226 SER B1229 -1 O SER B1229 N ILE B1217
SHEET 1 AE 2 LEU X 199 HIS X 204 0
SHEET 2 AE 2 SER X 207 PRO X 212 -1 O SER X 207 N HIS X 204
SHEET 1 AF 2 SER X 244 ILE X 247 0
SHEET 2 AF 2 HIS X 261 GLN X 264 -1 O GLN X 264 N SER X 244
SSBOND 1 CYS A 893 CYS A 904 1555 1555 2.04
SSBOND 2 CYS A 900 CYS A 914 1555 1555 2.02
SSBOND 3 CYS A 916 CYS A 929 1555 1555 2.05
SSBOND 4 CYS A 1207 CYS A 1218 1555 1555 2.05
SSBOND 5 CYS A 1214 CYS A 1228 1555 1555 2.03
SSBOND 6 CYS A 1230 CYS A 1243 1555 1555 2.03
SSBOND 7 CYS B 893 CYS B 904 1555 1555 2.03
SSBOND 8 CYS B 900 CYS B 914 1555 1555 2.03
SSBOND 9 CYS B 916 CYS B 929 1555 1555 2.04
SSBOND 10 CYS B 1207 CYS B 1218 1555 1555 2.04
SSBOND 11 CYS B 1214 CYS B 1228 1555 1555 2.03
SSBOND 12 CYS B 1230 CYS B 1243 1555 1555 2.04
SSBOND 13 CYS X 189 CYS X 201 1555 1555 2.05
SSBOND 14 CYS X 195 CYS X 210 1555 1555 2.05
SSBOND 15 CYS X 200 CYS X 237 1555 1555 2.04
SSBOND 16 CYS X 220 CYS X 245 1555 1555 2.05
SSBOND 17 CYS X 239 CYS X 263 1555 1555 2.04
CRYST1 94.384 105.050 161.226 90.00 90.00 90.00 P 21 21 21 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 0.010595 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009519 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
