HEADER CELL ADHESION 09-JUL-07 2V5R
TITLE STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DSCAM;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL FOUR DOMAINS (D1, D2, D3 AND D4), RESIDUES 36-
COMPND 5 423;
COMPND 6 SYNONYM: DOWN SYNDROME CELL ADHESION MOLECULE DSCAM;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: ISOFORM 4.9/6.9
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 VARIANT: SPLICING VARIANT 4.9/6.9;
SOURCE 6 ORGAN: BRAIN;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BACNBLUE
KEYWDS DOWN SYNDROME CELL ADHESION MOLECULE DSCAM NEUROBIOLOGY SPL
KEYWDS 2 IMMUNOGLOBULIN DOMAIN, MEMBRANE, CELL ADHESION, DEVELOPMENTAL
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MEIJERS,R.PUETTMANN-HOLGADO,G.SKINIOTIS,J.-H.LIU,T.WALZ,
AUTHOR 2 D.SCHMUCKER,J.-H.WANG
REVDAT 6 13-DEC-23 2V5R 1 HETSYN
REVDAT 5 29-JUL-20 2V5R 1 COMPND REMARK HETNAM SITE
REVDAT 4 23-OCT-19 2V5R 1 SEQADV
REVDAT 3 24-FEB-09 2V5R 1 VERSN
REVDAT 2 02-OCT-07 2V5R 1 JRNL
REVDAT 1 11-SEP-07 2V5R 0
JRNL AUTH R.MEIJERS,R.PUETTMANN-HOLGADO,G.SKINIOTIS,J.-H.LIU,T.WALZ,
JRNL AUTH 2 J.-H.WANG,D.SCHMUCKER
JRNL TITL STRUCTURAL BASIS OF DSCAM ISOFORM SPECIFICITY
JRNL REF NATURE V. 449 487 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17721508
JRNL DOI 10.1038/NATURE06147
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 3 NUMBER OF REFLECTIONS : 22250
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.271
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: B GROUP REFINEMENT NCS REFINEMENT
REMARK 3 DOMAIN D4 (RESIDUES 309-391) IS LESS WELL DEFINED
REMARK 4
REMARK 4 2V5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1290033141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53580
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: PDB ENTRY 2V5M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % PEG 8000, 1MM SPERMIDINE, 0.1 M
REMARK 280 TRISHCL PH 8.5
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 138.89050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.27400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 138.89050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.27400
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 300 REMARK: THE DIMERIC STATE DESCRIBED IN REMARK 350
REMARK 300 BELOW HASHAS BEEN EXPERIMENTALLY VALIDATED USIING
REMARK 300 BEAD AGGREGATIONASSAYS.
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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 O GLU A 126 N ILE A 127 0.98
REMARK 500 O CYS A 125 N GLU A 126 1.24
REMARK 500 O VAL B 212 N ARG B 213 1.32
REMARK 500 O VAL A 212 N ARG A 213 1.38
REMARK 500 C CYS A 125 CA GLU A 126 1.57
REMARK 500 O CYS A 125 CA GLU A 126 1.62
REMARK 500 O ARG A 213 N PRO A 214 1.66
REMARK 500 CA CYS A 125 N GLU A 126 1.69
REMARK 500 O ARG B 213 N PRO B 214 1.79
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 CYS A 125 C GLU A 126 N -1.039
REMARK 500 GLU A 126 C ILE A 127 N -0.717
REMARK 500 VAL A 212 C ARG A 213 N -0.334
REMARK 500 ARG A 213 C PRO A 214 N -0.465
REMARK 500 VAL B 212 C ARG B 213 N -0.374
REMARK 500 ARG B 213 C PRO B 214 N -0.385
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 PRO A 34 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 CYS A 125 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 CYS A 125 O - C - N ANGL. DEV. = -36.8 DEGREES
REMARK 500 GLU A 126 CA - C - N ANGL. DEV. = 51.7 DEGREES
REMARK 500 GLU A 126 O - C - N ANGL. DEV. = -70.7 DEGREES
REMARK 500 ILE A 127 C - N - CA ANGL. DEV. = 39.2 DEGREES
REMARK 500 VAL A 212 CA - C - N ANGL. DEV. = 21.4 DEGREES
REMARK 500 VAL A 212 O - C - N ANGL. DEV. = -47.4 DEGREES
REMARK 500 ARG A 213 CA - C - N ANGL. DEV. = 17.0 DEGREES
REMARK 500 ARG A 213 O - C - N ANGL. DEV. = -16.9 DEGREES
REMARK 500 PRO A 245 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO B 34 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 CYS B 125 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 VAL B 212 CA - C - N ANGL. DEV. = 21.2 DEGREES
REMARK 500 VAL B 212 O - C - N ANGL. DEV. = -50.0 DEGREES
REMARK 500 PRO B 245 C - N - CA ANGL. DEV. = 9.0 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 PRO A 4 -163.00 -62.76
REMARK 500 VAL A 5 145.60 147.73
REMARK 500 LEU A 7 -69.24 -97.99
REMARK 500 ASN A 12 -82.19 -41.38
REMARK 500 PHE A 16 -170.64 178.87
REMARK 500 ASN A 18 156.14 -43.42
REMARK 500 THR A 20 -40.63 -168.38
REMARK 500 ALA A 22 -168.57 -163.76
REMARK 500 GLU A 23 146.81 -175.34
REMARK 500 PRO A 32 -89.91 -78.42
REMARK 500 MET A 33 104.09 167.19
REMARK 500 ASP A 42 43.11 -93.90
REMARK 500 LEU A 52 -106.85 -147.73
REMARK 500 SER A 56 -150.68 -68.25
REMARK 500 SER A 57 -73.87 -126.29
REMARK 500 ASP A 58 68.05 -57.67
REMARK 500 ALA A 68 -8.07 -55.87
REMARK 500 ASN A 86 -147.11 -130.02
REMARK 500 SER A 105 99.75 -61.46
REMARK 500 GLU A 107 134.45 -171.80
REMARK 500 ARG A 117 124.14 -29.06
REMARK 500 CYS A 125 -135.62 -108.37
REMARK 500 GLU A 126 -77.14 -159.85
REMARK 500 ILE A 127 95.99 80.05
REMARK 500 ALA A 153 47.14 77.32
REMARK 500 THR A 156 -43.22 -137.82
REMARK 500 PRO A 164 -35.60 -35.48
REMARK 500 GLU A 176 19.20 -56.42
REMARK 500 LYS A 180 131.41 155.20
REMARK 500 LEU A 190 -73.04 -106.15
REMARK 500 LEU A 196 -169.37 -68.08
REMARK 500 VAL A 212 -150.50 -172.48
REMARK 500 ARG A 213 145.87 -171.55
REMARK 500 ALA A 230 -1.85 62.51
REMARK 500 SER A 241 135.11 164.02
REMARK 500 ASN A 265 -156.77 -160.69
REMARK 500 ASP A 279 34.49 71.47
REMARK 500 ALA A 280 78.01 -40.61
REMARK 500 GLU A 299 170.31 177.17
REMARK 500 VAL A 322 -156.03 -91.40
REMARK 500 PHE A 324 74.04 -63.52
REMARK 500 PRO A 327 -163.27 -66.29
REMARK 500 ALA A 328 94.74 -160.99
REMARK 500 ASN A 337 134.40 170.81
REMARK 500 THR A 341 130.43 163.86
REMARK 500 ILE A 351 -66.48 -97.06
REMARK 500 ARG A 376 -156.84 -70.46
REMARK 500 ASN A 377 -172.28 158.52
REMARK 500 GLU A 380 -166.33 175.58
REMARK 500 SER A 381 137.96 170.54
REMARK 500
REMARK 500 THIS ENTRY HAS 100 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 31 PRO A 32 132.26
REMARK 500 VAL A 212 ARG A 213 -136.27
REMARK 500 ASN B 31 PRO B 32 132.68
REMARK 500 VAL B 212 ARG B 213 -138.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CYS A 125 -59.54
REMARK 500 GLU A 126 125.70
REMARK 500 VAL A 212 -49.22
REMARK 500 ARG A 213 10.33
REMARK 500 VAL B 212 -52.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG A 1392
REMARK 610 NAG A 1393
REMARK 610 NAG A 1394
REMARK 610 NAG A 1395
REMARK 610 NAG B 1393
REMARK 610 NAG B 1394
REMARK 610 NAG B 1395
REMARK 610 NAG B 1396
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V5M RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY
REMARK 900 RELATED ID: 2V5S RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICTS GIVEN IN THE SEQADV RECORDS BELOW ARE AS A
REMARK 999 RESULT OF A SPLICE VARIANT FORM OF THE PROTEIN WHERE EXON 4
REMARK 999 COVERING RESIDUES 102 TO 156 CONSISTS OF ISOFORM 9 AND EXON 6
REMARK 999 COVERING RESIDUES 205 TO 245 CONSISTS OF ISOFORM 9.
DBREF 2V5R A 1 150 UNP Q9NBA1 Q9NBA1_DROME 36 185
DBREF 2V5R A 151 152 PDB 2V5R 2V5R 151 152
DBREF 2V5R A 153 225 UNP Q9NBA1 Q9NBA1_DROME 186 258
DBREF 2V5R A 226 226 PDB 2V5R 2V5R 226 226
DBREF 2V5R A 227 391 UNP Q9NBA1 Q9NBA1_DROME 259 423
DBREF 2V5R B 1 150 UNP Q9NBA1 Q9NBA1_DROME 36 185
DBREF 2V5R B 151 152 PDB 2V5R 2V5R 151 152
DBREF 2V5R B 153 225 UNP Q9NBA1 Q9NBA1_DROME 186 258
DBREF 2V5R B 226 226 PDB 2V5R 2V5R 226 226
DBREF 2V5R B 227 391 UNP Q9NBA1 Q9NBA1_DROME 259 423
SEQADV 2V5R ILE A 103 UNP Q9NBA1 ALA 138 VARIANT
SEQADV 2V5R SER A 105 UNP Q9NBA1 TYR 140 VARIANT
SEQADV 2V5R SER A 108 UNP Q9NBA1 ALA 143 VARIANT
SEQADV 2V5R GLU A 109 UNP Q9NBA1 ASP 144 VARIANT
SEQADV 2V5R ALA A 110 UNP Q9NBA1 VAL 145 VARIANT
SEQADV 2V5R ASP A 111 UNP Q9NBA1 ASN 146 VARIANT
SEQADV 2V5R ASN A 112 UNP Q9NBA1 LYS 147 VARIANT
SEQADV 2V5R TYR A 114 UNP Q9NBA1 HIS 149 VARIANT
SEQADV 2V5R VAL A 121 UNP Q9NBA1 ALA 156 VARIANT
SEQADV 2V5R MET A 123 UNP Q9NBA1 ILE 158 VARIANT
SEQADV 2V5R GLU A 126 UNP Q9NBA1 LEU 161 VARIANT
SEQADV 2V5R TYR A 130 UNP Q9NBA1 PHE 165 VARIANT
SEQADV 2V5R PHE A 136 UNP Q9NBA1 GLU 171 VARIANT
SEQADV 2V5R ASP A 138 UNP Q9NBA1 VAL 173 VARIANT
SEQADV 2V5R LEU A 139 UNP Q9NBA1 SER 174 VARIANT
SEQADV 2V5R LEU A 141 UNP Q9NBA1 HIS 176 VARIANT
SEQADV 2V5R ASP A 142 UNP Q9NBA1 THR 177 VARIANT
SEQADV 2V5R SER A 143 UNP Q9NBA1 ASP 178 VARIANT
SEQADV 2V5R GLY A 145 UNP Q9NBA1 GLU 180 VARIANT
SEQADV 2V5R ARG A 146 UNP Q9NBA1 GLU 181 VARIANT
SEQADV 2V5R TYR A 149 UNP Q9NBA1 PHE 184 VARIANT
SEQADV 2V5R ALA A 153 UNP Q9NBA1 GLY 186 VARIANT
SEQADV 2V5R THR A 156 UNP Q9NBA1 TYR 189 VARIANT
SEQADV 2V5R GLY A 210 UNP Q9NBA1 SER 243 VARIANT
SEQADV 2V5R VAL A 212 UNP Q9NBA1 SER 245 VARIANT
SEQADV 2V5R ARG A 213 UNP Q9NBA1 PRO 246 VARIANT
SEQADV 2V5R VAL A 216 UNP Q9NBA1 ILE 249 VARIANT
SEQADV 2V5R PRO A 218 UNP Q9NBA1 THR 251 VARIANT
SEQADV 2V5R GLN A 219 UNP Q9NBA1 LEU 252 VARIANT
SEQADV 2V5R ASP A 220 UNP Q9NBA1 THR 253 VARIANT
SEQADV 2V5R LYS A 221 UNP Q9NBA1 TYR 254 VARIANT
SEQADV 2V5R HIS A 222 UNP Q9NBA1 LYS 255 VARIANT
SEQADV 2V5R GLN A 223 UNP Q9NBA1 PRO 256 VARIANT
SEQADV 2V5R PHE A 224 UNP Q9NBA1 ASN 257 VARIANT
SEQADV 2V5R LEU A 229 UNP Q9NBA1 SER 261 VARIANT
SEQADV 2V5R ALA A 230 UNP Q9NBA1 MET 262 VARIANT
SEQADV 2V5R SER A 231 UNP Q9NBA1 ALA 263 VARIANT
SEQADV 2V5R TYR A 233 UNP Q9NBA1 THR 265 VARIANT
SEQADV 2V5R SER A 234 UNP Q9NBA1 ALA 266 VARIANT
SEQADV 2V5R LEU A 235 UNP Q9NBA1 ILE 267 VARIANT
SEQADV 2V5R MET A 238 UNP Q9NBA1 PRO 270 VARIANT
SEQADV 2V5R SER A 241 UNP Q9NBA1 GLY 273 VARIANT
SEQADV 2V5R THR A 244 UNP Q9NBA1 ALA 276 VARIANT
SEQADV 2V5R ILE B 103 UNP Q9NBA1 ALA 138 VARIANT
SEQADV 2V5R SER B 105 UNP Q9NBA1 TYR 140 VARIANT
SEQADV 2V5R SER B 108 UNP Q9NBA1 ALA 143 VARIANT
SEQADV 2V5R GLU B 109 UNP Q9NBA1 ASP 144 VARIANT
SEQADV 2V5R ALA B 110 UNP Q9NBA1 VAL 145 VARIANT
SEQADV 2V5R ASP B 111 UNP Q9NBA1 ASN 146 VARIANT
SEQADV 2V5R ASN B 112 UNP Q9NBA1 LYS 147 VARIANT
SEQADV 2V5R TYR B 114 UNP Q9NBA1 HIS 149 VARIANT
SEQADV 2V5R VAL B 121 UNP Q9NBA1 ALA 156 VARIANT
SEQADV 2V5R MET B 123 UNP Q9NBA1 ILE 158 VARIANT
SEQADV 2V5R GLU B 126 UNP Q9NBA1 LEU 161 VARIANT
SEQADV 2V5R TYR B 130 UNP Q9NBA1 PHE 165 VARIANT
SEQADV 2V5R PHE B 136 UNP Q9NBA1 GLU 171 VARIANT
SEQADV 2V5R ASP B 138 UNP Q9NBA1 VAL 173 VARIANT
SEQADV 2V5R LEU B 139 UNP Q9NBA1 SER 174 VARIANT
SEQADV 2V5R LEU B 141 UNP Q9NBA1 HIS 176 VARIANT
SEQADV 2V5R ASP B 142 UNP Q9NBA1 THR 177 VARIANT
SEQADV 2V5R SER B 143 UNP Q9NBA1 ASP 178 VARIANT
SEQADV 2V5R GLY B 145 UNP Q9NBA1 GLU 180 VARIANT
SEQADV 2V5R ARG B 146 UNP Q9NBA1 GLU 181 VARIANT
SEQADV 2V5R TYR B 149 UNP Q9NBA1 PHE 184 VARIANT
SEQADV 2V5R ALA B 153 UNP Q9NBA1 GLY 186 VARIANT
SEQADV 2V5R THR B 156 UNP Q9NBA1 TYR 189 VARIANT
SEQADV 2V5R GLY B 210 UNP Q9NBA1 SER 243 VARIANT
SEQADV 2V5R VAL B 212 UNP Q9NBA1 SER 245 VARIANT
SEQADV 2V5R ARG B 213 UNP Q9NBA1 PRO 246 VARIANT
SEQADV 2V5R VAL B 216 UNP Q9NBA1 ILE 249 VARIANT
SEQADV 2V5R PRO B 218 UNP Q9NBA1 THR 251 VARIANT
SEQADV 2V5R GLN B 219 UNP Q9NBA1 LEU 252 VARIANT
SEQADV 2V5R ASP B 220 UNP Q9NBA1 THR 253 VARIANT
SEQADV 2V5R LYS B 221 UNP Q9NBA1 TYR 254 VARIANT
SEQADV 2V5R HIS B 222 UNP Q9NBA1 LYS 255 VARIANT
SEQADV 2V5R GLN B 223 UNP Q9NBA1 PRO 256 VARIANT
SEQADV 2V5R PHE B 224 UNP Q9NBA1 ASN 257 VARIANT
SEQADV 2V5R LEU B 229 UNP Q9NBA1 SER 261 VARIANT
SEQADV 2V5R ALA B 230 UNP Q9NBA1 MET 262 VARIANT
SEQADV 2V5R SER B 231 UNP Q9NBA1 ALA 263 VARIANT
SEQADV 2V5R TYR B 233 UNP Q9NBA1 THR 265 VARIANT
SEQADV 2V5R SER B 234 UNP Q9NBA1 ALA 266 VARIANT
SEQADV 2V5R LEU B 235 UNP Q9NBA1 ILE 267 VARIANT
SEQADV 2V5R MET B 238 UNP Q9NBA1 PRO 270 VARIANT
SEQADV 2V5R SER B 241 UNP Q9NBA1 GLY 273 VARIANT
SEQADV 2V5R THR B 244 UNP Q9NBA1 ALA 276 VARIANT
SEQRES 1 A 391 GLN LYS GLY PRO VAL PHE LEU LYS GLU PRO THR ASN ARG
SEQRES 2 A 391 ILE ASP PHE SER ASN SER THR GLY ALA GLU ILE GLU CYS
SEQRES 3 A 391 LYS ALA SER GLY ASN PRO MET PRO GLU ILE ILE TRP ILE
SEQRES 4 A 391 ARG SER ASP GLY THR ALA VAL GLY ASP VAL PRO GLY LEU
SEQRES 5 A 391 ARG GLN ILE SER SER ASP GLY LYS LEU VAL PHE PRO PRO
SEQRES 6 A 391 PHE ARG ALA GLU ASP TYR ARG GLN GLU VAL HIS ALA GLN
SEQRES 7 A 391 VAL TYR ALA CYS LEU ALA ARG ASN GLN PHE GLY SER ILE
SEQRES 8 A 391 ILE SER ARG ASP VAL HIS VAL ARG ALA VAL VAL ILE GLN
SEQRES 9 A 391 SER TYR GLU SER GLU ALA ASP ASN GLU TYR VAL ILE ARG
SEQRES 10 A 391 GLY ASN SER VAL VAL MET LYS CYS GLU ILE PRO SER TYR
SEQRES 11 A 391 VAL ALA ASP PHE VAL PHE VAL ASP LEU TRP LEU ASP SER
SEQRES 12 A 391 GLU GLY ARG ASN TYR TYR PRO ASN ASN ALA ALA GLU THR
SEQRES 13 A 391 ASP GLY LYS TYR LEU VAL LEU PRO SER GLY GLU LEU HIS
SEQRES 14 A 391 ILE ARG GLU VAL GLY PRO GLU ASP GLY TYR LYS SER TYR
SEQRES 15 A 391 GLN CYS ARG THR LYS HIS ARG LEU THR GLY GLU THR ARG
SEQRES 16 A 391 LEU SER ALA THR LYS GLY ARG LEU VAL ILE THR GLU PRO
SEQRES 17 A 391 VAL GLY SER VAL ARG PRO LYS VAL ASN PRO GLN ASP LYS
SEQRES 18 A 391 HIS GLN PHE ILE ASP VAL GLU LEU ALA SER SER TYR SER
SEQRES 19 A 391 LEU LEU CYS MET ALA GLN SER TYR PRO THR PRO SER PHE
SEQRES 20 A 391 ARG TRP TYR LYS PHE ILE GLU GLY THR THR ARG LYS GLN
SEQRES 21 A 391 ALA VAL VAL LEU ASN ASP ARG VAL LYS GLN VAL SER GLY
SEQRES 22 A 391 THR LEU ILE ILE LYS ASP ALA VAL VAL GLU ASP SER GLY
SEQRES 23 A 391 LYS TYR LEU CYS VAL VAL ASN ASN SER VAL GLY GLY GLU
SEQRES 24 A 391 SER VAL GLU THR VAL LEU THR VAL THR ALA PRO LEU SER
SEQRES 25 A 391 ALA LYS ILE ASP PRO PRO THR GLN THR VAL ASP PHE GLY
SEQRES 26 A 391 ARG PRO ALA VAL PHE THR CYS GLN TYR THR GLY ASN PRO
SEQRES 27 A 391 ILE LYS THR VAL SER TRP MET LYS ASP GLY LYS ALA ILE
SEQRES 28 A 391 GLY HIS SER GLU SER VAL LEU ARG ILE GLU SER VAL LYS
SEQRES 29 A 391 LYS GLU ASP LYS GLY MET TYR GLN CYS PHE VAL ARG ASN
SEQRES 30 A 391 ASP ARG GLU SER ALA GLU ALA SER ALA GLU LEU LYS LEU
SEQRES 31 A 391 GLY
SEQRES 1 B 391 GLN LYS GLY PRO VAL PHE LEU LYS GLU PRO THR ASN ARG
SEQRES 2 B 391 ILE ASP PHE SER ASN SER THR GLY ALA GLU ILE GLU CYS
SEQRES 3 B 391 LYS ALA SER GLY ASN PRO MET PRO GLU ILE ILE TRP ILE
SEQRES 4 B 391 ARG SER ASP GLY THR ALA VAL GLY ASP VAL PRO GLY LEU
SEQRES 5 B 391 ARG GLN ILE SER SER ASP GLY LYS LEU VAL PHE PRO PRO
SEQRES 6 B 391 PHE ARG ALA GLU ASP TYR ARG GLN GLU VAL HIS ALA GLN
SEQRES 7 B 391 VAL TYR ALA CYS LEU ALA ARG ASN GLN PHE GLY SER ILE
SEQRES 8 B 391 ILE SER ARG ASP VAL HIS VAL ARG ALA VAL VAL ILE GLN
SEQRES 9 B 391 SER TYR GLU SER GLU ALA ASP ASN GLU TYR VAL ILE ARG
SEQRES 10 B 391 GLY ASN SER VAL VAL MET LYS CYS GLU ILE PRO SER TYR
SEQRES 11 B 391 VAL ALA ASP PHE VAL PHE VAL ASP LEU TRP LEU ASP SER
SEQRES 12 B 391 GLU GLY ARG ASN TYR TYR PRO ASN ASN ALA ALA GLU THR
SEQRES 13 B 391 ASP GLY LYS TYR LEU VAL LEU PRO SER GLY GLU LEU HIS
SEQRES 14 B 391 ILE ARG GLU VAL GLY PRO GLU ASP GLY TYR LYS SER TYR
SEQRES 15 B 391 GLN CYS ARG THR LYS HIS ARG LEU THR GLY GLU THR ARG
SEQRES 16 B 391 LEU SER ALA THR LYS GLY ARG LEU VAL ILE THR GLU PRO
SEQRES 17 B 391 VAL GLY SER VAL ARG PRO LYS VAL ASN PRO GLN ASP LYS
SEQRES 18 B 391 HIS GLN PHE ILE ASP VAL GLU LEU ALA SER SER TYR SER
SEQRES 19 B 391 LEU LEU CYS MET ALA GLN SER TYR PRO THR PRO SER PHE
SEQRES 20 B 391 ARG TRP TYR LYS PHE ILE GLU GLY THR THR ARG LYS GLN
SEQRES 21 B 391 ALA VAL VAL LEU ASN ASP ARG VAL LYS GLN VAL SER GLY
SEQRES 22 B 391 THR LEU ILE ILE LYS ASP ALA VAL VAL GLU ASP SER GLY
SEQRES 23 B 391 LYS TYR LEU CYS VAL VAL ASN ASN SER VAL GLY GLY GLU
SEQRES 24 B 391 SER VAL GLU THR VAL LEU THR VAL THR ALA PRO LEU SER
SEQRES 25 B 391 ALA LYS ILE ASP PRO PRO THR GLN THR VAL ASP PHE GLY
SEQRES 26 B 391 ARG PRO ALA VAL PHE THR CYS GLN TYR THR GLY ASN PRO
SEQRES 27 B 391 ILE LYS THR VAL SER TRP MET LYS ASP GLY LYS ALA ILE
SEQRES 28 B 391 GLY HIS SER GLU SER VAL LEU ARG ILE GLU SER VAL LYS
SEQRES 29 B 391 LYS GLU ASP LYS GLY MET TYR GLN CYS PHE VAL ARG ASN
SEQRES 30 B 391 ASP ARG GLU SER ALA GLU ALA SER ALA GLU LEU LYS LEU
SEQRES 31 B 391 GLY
HET NAG A1392 14
HET NAG A1393 14
HET NAG A1394 14
HET NAG A1395 14
HET GOL B1392 6
HET NAG B1393 14
HET NAG B1394 14
HET NAG B1395 14
HET NAG B1396 14
HET GOL B1397 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GOL GLYCEROL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 8(C8 H15 N O6)
FORMUL 7 GOL 2(C3 H8 O3)
HELIX 1 1 ARG A 72 HIS A 76 1 5
HELIX 2 2 PRO A 128 ASP A 133 1 6
HELIX 3 3 GLY A 174 GLY A 178 5 5
HELIX 4 4 ASN A 217 ASP A 220 5 4
HELIX 5 5 VAL A 281 SER A 285 5 5
HELIX 6 6 ARG B 72 HIS B 76 1 5
HELIX 7 7 PRO B 128 ASP B 133 1 6
HELIX 8 8 GLY B 174 GLY B 178 5 5
HELIX 9 9 ASN B 217 ASP B 220 5 4
HELIX 10 10 VAL B 281 SER B 285 5 5
SHEET 1 AA 2 PHE A 6 LYS A 8 0
SHEET 2 AA 2 LYS A 27 ALA A 28 -1 O LYS A 27 N LYS A 8
SHEET 1 AB 4 ARG A 13 SER A 17 0
SHEET 2 AB 4 VAL A 96 VAL A 101 1 O HIS A 97 N ILE A 14
SHEET 3 AB 4 ALA A 77 ARG A 85 -1 O GLN A 78 N VAL A 98
SHEET 4 AB 4 GLU A 35 ARG A 40 -1 O GLU A 35 N ARG A 85
SHEET 1 AC 4 ARG A 13 SER A 17 0
SHEET 2 AC 4 VAL A 96 VAL A 101 1 O HIS A 97 N ILE A 14
SHEET 3 AC 4 ALA A 77 ARG A 85 -1 O GLN A 78 N VAL A 98
SHEET 4 AC 4 SER A 90 ILE A 92 -1 O ILE A 91 N ALA A 84
SHEET 1 AD 3 ALA A 22 GLU A 23 0
SHEET 2 AD 3 LEU A 61 PHE A 63 -1 O PHE A 63 N ALA A 22
SHEET 3 AD 3 GLN A 54 ILE A 55 -1 O GLN A 54 N VAL A 62
SHEET 1 AE 4 GLU A 113 ILE A 116 0
SHEET 2 AE 4 GLY A 201 THR A 206 1 O ARG A 202 N GLU A 113
SHEET 3 AE 4 SER A 181 HIS A 188 -1 O TYR A 182 N GLY A 201
SHEET 4 AE 4 VAL A 135 ASP A 142 -1 O PHE A 136 N LYS A 187
SHEET 1 AF 4 GLU A 113 ILE A 116 0
SHEET 2 AF 4 GLY A 201 THR A 206 1 O ARG A 202 N GLU A 113
SHEET 3 AF 4 SER A 181 HIS A 188 -1 O TYR A 182 N GLY A 201
SHEET 4 AF 4 THR A 194 LEU A 196 -1 O ARG A 195 N THR A 186
SHEET 1 AG 2 VAL A 121 MET A 123 0
SHEET 2 AG 2 LEU A 168 ILE A 170 -1 O LEU A 168 N MET A 123
SHEET 1 AH 2 VAL A 212 LYS A 215 0
SHEET 2 AH 2 GLN A 240 TYR A 242 -1 O GLN A 240 N LYS A 215
SHEET 1 AI 5 HIS A 222 GLU A 228 0
SHEET 2 AI 5 GLY A 297 THR A 308 1 O GLU A 302 N GLN A 223
SHEET 3 AI 5 GLY A 286 ASN A 294 -1 O GLY A 286 N LEU A 305
SHEET 4 AI 5 SER A 246 PHE A 252 -1 O SER A 246 N ASN A 293
SHEET 5 AI 5 LYS A 259 ALA A 261 -1 O GLN A 260 N LYS A 251
SHEET 1 AJ 3 TYR A 233 LEU A 235 0
SHEET 2 AJ 3 THR A 274 ILE A 277 -1 O LEU A 275 N LEU A 235
SHEET 3 AJ 3 VAL A 268 VAL A 271 -1 O LYS A 269 N ILE A 276
SHEET 1 AK 2 LYS A 314 ASP A 316 0
SHEET 2 AK 2 THR A 331 GLN A 333 -1 O THR A 331 N ASP A 316
SHEET 1 AL 4 LYS A 349 ALA A 350 0
SHEET 2 AL 4 TRP A 344 LYS A 346 -1 O LYS A 346 N LYS A 349
SHEET 3 AL 4 MET A 370 VAL A 375 -1 O GLN A 372 N MET A 345
SHEET 4 AL 4 ALA A 386 GLU A 387 -1 O ALA A 386 N TYR A 371
SHEET 1 AM 4 LYS A 349 ALA A 350 0
SHEET 2 AM 4 TRP A 344 LYS A 346 -1 O LYS A 346 N LYS A 349
SHEET 3 AM 4 MET A 370 VAL A 375 -1 O GLN A 372 N MET A 345
SHEET 4 AM 4 ALA A 382 GLU A 383 -1 O ALA A 382 N VAL A 375
SHEET 1 BA 2 PHE B 6 LYS B 8 0
SHEET 2 BA 2 LYS B 27 ALA B 28 -1 O LYS B 27 N LYS B 8
SHEET 1 BB 7 ARG B 13 SER B 17 0
SHEET 2 BB 7 VAL B 96 VAL B 101 1 O HIS B 97 N ILE B 14
SHEET 3 BB 7 ALA B 77 ARG B 85 -1 O GLN B 78 N VAL B 98
SHEET 4 BB 7 GLU B 35 ARG B 40 -1 O GLU B 35 N ARG B 85
SHEET 5 BB 7 ALA B 77 ARG B 85 -1 O ALA B 81 N ILE B 39
SHEET 6 BB 7 SER B 90 ILE B 92 -1 O ILE B 91 N ALA B 84
SHEET 7 BB 7 ALA B 77 ARG B 85 -1 O ALA B 84 N ILE B 91
SHEET 1 BC 3 ALA B 22 GLU B 23 0
SHEET 2 BC 3 LEU B 61 PHE B 63 -1 O PHE B 63 N ALA B 22
SHEET 3 BC 3 GLN B 54 ILE B 55 -1 O GLN B 54 N VAL B 62
SHEET 1 BD 7 GLU B 113 ILE B 116 0
SHEET 2 BD 7 GLY B 201 THR B 206 1 O ARG B 202 N GLU B 113
SHEET 3 BD 7 SER B 181 HIS B 188 -1 O TYR B 182 N GLY B 201
SHEET 4 BD 7 VAL B 135 ASP B 142 -1 O PHE B 136 N LYS B 187
SHEET 5 BD 7 SER B 181 HIS B 188 -1 O GLN B 183 N LEU B 141
SHEET 6 BD 7 THR B 194 LEU B 196 -1 O ARG B 195 N THR B 186
SHEET 7 BD 7 SER B 181 HIS B 188 -1 O THR B 186 N ARG B 195
SHEET 1 BE 2 VAL B 121 MET B 123 0
SHEET 2 BE 2 LEU B 168 ILE B 170 -1 O LEU B 168 N MET B 123
SHEET 1 BF 2 VAL B 212 LYS B 215 0
SHEET 2 BF 2 GLN B 240 TYR B 242 -1 O GLN B 240 N LYS B 215
SHEET 1 BG 5 HIS B 222 GLU B 228 0
SHEET 2 BG 5 GLY B 297 THR B 308 1 O GLU B 302 N GLN B 223
SHEET 3 BG 5 GLY B 286 ASN B 294 -1 O GLY B 286 N LEU B 305
SHEET 4 BG 5 SER B 246 PHE B 252 -1 O SER B 246 N ASN B 293
SHEET 5 BG 5 LYS B 259 ALA B 261 -1 O GLN B 260 N LYS B 251
SHEET 1 BH 3 TYR B 233 LEU B 235 0
SHEET 2 BH 3 THR B 274 ILE B 277 -1 O LEU B 275 N LEU B 235
SHEET 3 BH 3 VAL B 268 VAL B 271 -1 O LYS B 269 N ILE B 276
SHEET 1 BI 2 LYS B 314 ASP B 316 0
SHEET 2 BI 2 THR B 331 GLN B 333 -1 O THR B 331 N ASP B 316
SHEET 1 BJ 7 LYS B 349 ALA B 350 0
SHEET 2 BJ 7 TRP B 344 LYS B 346 -1 O LYS B 346 N LYS B 349
SHEET 3 BJ 7 MET B 370 VAL B 375 -1 O GLN B 372 N MET B 345
SHEET 4 BJ 7 ALA B 382 GLU B 383 -1 O ALA B 382 N VAL B 375
SHEET 5 BJ 7 MET B 370 VAL B 375 -1 O VAL B 375 N ALA B 382
SHEET 6 BJ 7 ALA B 386 GLU B 387 -1 O ALA B 386 N TYR B 371
SHEET 7 BJ 7 MET B 370 VAL B 375 -1 O TYR B 371 N ALA B 386
SSBOND 1 CYS A 26 CYS A 82 1555 1555 2.04
SSBOND 2 CYS A 125 CYS A 184 1555 1555 2.09
SSBOND 3 CYS A 237 CYS A 290 1555 1555 2.02
SSBOND 4 CYS B 26 CYS B 82 1555 1555 2.04
SSBOND 5 CYS B 125 CYS B 184 1555 1555 2.09
SSBOND 6 CYS B 237 CYS B 290 1555 1555 2.02
CISPEP 1 TYR A 242 PRO A 243 0 -6.62
CISPEP 2 SER A 272 GLY A 273 0 2.40
CISPEP 3 ASP A 316 PRO A 317 0 1.49
CISPEP 4 ASN A 337 PRO A 338 0 -0.29
CISPEP 5 TYR B 242 PRO B 243 0 -6.64
CISPEP 6 SER B 272 GLY B 273 0 2.86
CISPEP 7 ASP B 316 PRO B 317 0 0.94
CISPEP 8 ASN B 337 PRO B 338 0 -0.32
CRYST1 277.781 70.548 72.771 90.00 105.13 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 0.003600 0.000000 0.000973 0.00000
SCALE2 0.000000 0.014175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014235 0.00000
MTRIX1 1 0.863000 -0.001000 0.506000 -19.04812 1
MTRIX2 1 0.000000 -1.000000 -0.001000 -46.12549 1
MTRIX3 1 0.506000 0.000000 -0.863000 70.22813 1
(ATOM LINES ARE NOT SHOWN.)
END
