HEADER CELL ADHESION/HYDROLASE 09-OCT-15 5E5U
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBONIC ANHYDRASE-LIKE
TITLE 2 DOMAIN OF PTPRG AND IMMUNOGLOBULIN DOMAINS 2-3 OF CNTN6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: CA DOMAIN, UNP RESIDUES 57-320;
COMPND 5 SYNONYM: R-PTP-GAMMA;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CONTACTIN-6;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: IMMUNOGLOBULIN DOMAINS 2-3, UNP RESIDUES 119-316;
COMPND 12 SYNONYM: NEURAL RECOGNITION MOLECULE NB-3,MNB-3;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTPRG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32HP;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 GENE: CNTN6;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: T7 SHUFFLE EXPRESS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PT7HMP
KEYWDS NEURAL CELL ADHESION MOLECULE, RECEPTOR-TYPE PROTEIN TYROSINE
KEYWDS 2 PHOSPHATASE, IMMUNOGLOBULIN DOMAINS, CARBONIC ANHYDRASE-LIKE DOMAIN,
KEYWDS 3 CELL ADHESION-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.NIKOLAIENKO,S.BOUYAIN
REVDAT 5 27-SEP-23 5E5U 1 HETSYN
REVDAT 4 25-DEC-19 5E5U 1 REMARK
REVDAT 3 27-SEP-17 5E5U 1 JRNL
REVDAT 2 23-NOV-16 5E5U 1 JRNL
REVDAT 1 31-AUG-16 5E5U 0
JRNL AUTH R.M.NIKOLAIENKO,M.HAMMEL,V.DUBREUIL,R.ZALMAI,D.R.HALL,
JRNL AUTH 2 N.MEHZABEEN,S.J.KARUPPAN,S.HARROCH,S.L.STELLA,S.BOUYAIN
JRNL TITL STRUCTURAL BASIS FOR INTERACTIONS BETWEEN CONTACTIN FAMILY
JRNL TITL 2 MEMBERS AND PROTEIN-TYROSINE PHOSPHATASE RECEPTOR TYPE G IN
JRNL TITL 3 NEURAL TISSUES.
JRNL REF J.BIOL.CHEM. V. 291 21335 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27539848
JRNL DOI 10.1074/JBC.M116.742163
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 70357
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3517
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.8927 - 5.8250 1.00 2906 155 0.1487 0.1759
REMARK 3 2 5.8250 - 4.6332 1.00 2791 147 0.1263 0.1701
REMARK 3 3 4.6332 - 4.0504 1.00 2747 146 0.1198 0.1658
REMARK 3 4 4.0504 - 3.6813 1.00 2762 144 0.1387 0.1651
REMARK 3 5 3.6813 - 3.4182 1.00 2717 147 0.1504 0.1920
REMARK 3 6 3.4182 - 3.2171 1.00 2741 140 0.1670 0.2183
REMARK 3 7 3.2171 - 3.0563 1.00 2724 145 0.1878 0.2540
REMARK 3 8 3.0563 - 2.9234 1.00 2689 138 0.1884 0.2288
REMARK 3 9 2.9234 - 2.8111 1.00 2705 147 0.2053 0.2629
REMARK 3 10 2.8111 - 2.7142 1.00 2707 145 0.2090 0.2911
REMARK 3 11 2.7142 - 2.6294 1.00 2696 145 0.2031 0.2805
REMARK 3 12 2.6294 - 2.5543 1.00 2699 138 0.2009 0.2632
REMARK 3 13 2.5543 - 2.4871 1.00 2711 134 0.2029 0.2702
REMARK 3 14 2.4871 - 2.4265 1.00 2660 152 0.1954 0.2597
REMARK 3 15 2.4265 - 2.3714 1.00 2711 141 0.1879 0.2209
REMARK 3 16 2.3714 - 2.3210 1.00 2676 141 0.1921 0.2299
REMARK 3 17 2.3210 - 2.2746 1.00 2695 135 0.1858 0.2404
REMARK 3 18 2.2746 - 2.2317 1.00 2658 150 0.1922 0.2614
REMARK 3 19 2.2317 - 2.1918 1.00 2695 133 0.1993 0.2777
REMARK 3 20 2.1918 - 2.1547 1.00 2656 139 0.1939 0.2729
REMARK 3 21 2.1547 - 2.1200 0.99 2679 144 0.2074 0.2490
REMARK 3 22 2.1200 - 2.0874 0.97 2592 148 0.2037 0.2777
REMARK 3 23 2.0874 - 2.0567 0.96 2549 114 0.2139 0.2819
REMARK 3 24 2.0567 - 2.0277 0.90 2423 137 0.2198 0.2955
REMARK 3 25 2.0277 - 2.0003 0.83 2251 112 0.2252 0.2788
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.80
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 : 0.007 7710
REMARK 3 ANGLE : 1.049 10442
REMARK 3 CHIRALITY : 0.044 1078
REMARK 3 PLANARITY : 0.005 1378
REMARK 3 DIHEDRAL : 13.380 2822
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESSEQ 56:320))
REMARK 3 ORIGIN FOR THE GROUP (A): 55.0017 64.8273 63.8056
REMARK 3 T TENSOR
REMARK 3 T11: 0.1933 T22: 0.2432
REMARK 3 T33: 0.3007 T12: 0.0251
REMARK 3 T13: -0.0272 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 2.3235 L22: 1.5482
REMARK 3 L33: 3.0251 L12: -0.3607
REMARK 3 L13: -0.8051 L23: -0.5856
REMARK 3 S TENSOR
REMARK 3 S11: 0.0158 S12: -0.0917 S13: 0.3914
REMARK 3 S21: 0.1242 S22: 0.1429 S23: 0.0321
REMARK 3 S31: -0.2797 S32: -0.1246 S33: -0.1466
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 118:221))
REMARK 3 ORIGIN FOR THE GROUP (A): 80.8920 36.0992 54.3414
REMARK 3 T TENSOR
REMARK 3 T11: 0.2181 T22: 0.1740
REMARK 3 T33: 0.1746 T12: 0.0214
REMARK 3 T13: 0.0382 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 5.4839 L22: 4.4007
REMARK 3 L33: 5.5361 L12: -0.6820
REMARK 3 L13: 2.0422 L23: -1.0361
REMARK 3 S TENSOR
REMARK 3 S11: -0.0590 S12: -0.1290 S13: -0.3105
REMARK 3 S21: 0.1089 S22: -0.0170 S23: -0.0229
REMARK 3 S31: 0.1749 S32: 0.0546 S33: 0.0288
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 222:316))
REMARK 3 ORIGIN FOR THE GROUP (A): 89.6317 57.0137 48.8632
REMARK 3 T TENSOR
REMARK 3 T11: 0.2572 T22: 0.2805
REMARK 3 T33: 0.1636 T12: 0.0126
REMARK 3 T13: 0.0160 T23: 0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 7.5501 L22: 1.7413
REMARK 3 L33: 1.9297 L12: 2.5843
REMARK 3 L13: 1.0298 L23: 0.8016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0669 S12: 0.0284 S13: 0.1053
REMARK 3 S21: -0.2160 S22: 0.0071 S23: 0.0185
REMARK 3 S31: -0.2259 S32: 0.2401 S33: 0.0423
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND ((RESSEQ 56:320))
REMARK 3 ORIGIN FOR THE GROUP (A): 86.6774 55.4601 83.5103
REMARK 3 T TENSOR
REMARK 3 T11: 0.1726 T22: 0.1690
REMARK 3 T33: 0.1840 T12: -0.0172
REMARK 3 T13: -0.0218 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 2.6468 L22: 1.3848
REMARK 3 L33: 2.1722 L12: 0.6128
REMARK 3 L13: 0.2017 L23: 0.2119
REMARK 3 S TENSOR
REMARK 3 S11: 0.0127 S12: -0.0106 S13: 0.2186
REMARK 3 S21: -0.0045 S22: -0.0119 S23: -0.0042
REMARK 3 S31: -0.1522 S32: 0.1126 S33: 0.0074
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 118:221))
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3415 31.7302 70.7996
REMARK 3 T TENSOR
REMARK 3 T11: 0.2753 T22: 0.1951
REMARK 3 T33: 0.2365 T12: -0.1179
REMARK 3 T13: -0.0186 T23: -0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 3.9800 L22: 3.9715
REMARK 3 L33: 4.5863 L12: -0.5391
REMARK 3 L13: 2.0134 L23: -0.3647
REMARK 3 S TENSOR
REMARK 3 S11: -0.1712 S12: 0.4143 S13: 0.1468
REMARK 3 S21: -0.3032 S22: 0.1094 S23: 0.0874
REMARK 3 S31: -0.0596 S32: 0.0553 S33: 0.0078
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 222:316))
REMARK 3 ORIGIN FOR THE GROUP (A): 51.8629 42.1208 90.2212
REMARK 3 T TENSOR
REMARK 3 T11: 0.1974 T22: 0.2973
REMARK 3 T33: 0.2005 T12: -0.0533
REMARK 3 T13: -0.0126 T23: -0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 5.2639 L22: 3.5683
REMARK 3 L33: 1.8274 L12: -2.5645
REMARK 3 L13: -0.5331 L23: -0.2319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0514 S12: -0.0994 S13: -0.1622
REMARK 3 S21: 0.1212 S22: 0.0014 S23: 0.3884
REMARK 3 S31: 0.0494 S32: -0.4546 S33: 0.0078
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70482
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.59300
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: PHASER
REMARK 200 STARTING MODEL: 3KLD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 55% (V/V) TACSIMATE PH 7.0, 150 MM
REMARK 280 NDSB 201, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 39.32050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.52300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.76500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.52300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.32050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.76500
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: 2820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ASP D 169 O HOH D 501 2.15
REMARK 500 O VAL D 166 O HOH D 501 2.18
REMARK 500 O HOH C 558 O HOH C 590 2.19
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 ARG A 195 -63.38 -108.50
REMARK 500 HIS A 227 120.88 -37.62
REMARK 500 GLU A 228 -3.83 82.10
REMARK 500 HIS A 295 22.44 -147.09
REMARK 500 ASN A 313 -121.23 58.44
REMARK 500 HIS C 227 125.64 -37.48
REMARK 500 GLU C 228 -5.71 84.24
REMARK 500 GLN C 293 -164.77 -107.88
REMARK 500 ASN C 313 -119.01 56.87
REMARK 500 LYS D 286 59.51 39.95
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 1PS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PS C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PS C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLT D 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5E4Q RELATED DB: PDB
REMARK 900 RELATED ID: 5E4I RELATED DB: PDB
REMARK 900 RELATED ID: 5E4S RELATED DB: PDB
REMARK 900 RELATED ID: 5E52 RELATED DB: PDB
REMARK 900 RELATED ID: 5E53 RELATED DB: PDB
REMARK 900 RELATED ID: 5E55 RELATED DB: PDB
REMARK 900 RELATED ID: 5E5R RELATED DB: PDB
DBREF 5E5U A 57 320 UNP Q05909 PTPRG_MOUSE 57 320
DBREF 5E5U B 119 316 UNP Q9JMB8 CNTN6_MOUSE 119 316
DBREF 5E5U C 57 320 UNP Q05909 PTPRG_MOUSE 57 320
DBREF 5E5U D 119 316 UNP Q9JMB8 CNTN6_MOUSE 119 316
SEQADV 5E5U SER B 118 UNP Q9JMB8 EXPRESSION TAG
SEQADV 5E5U SER D 118 UNP Q9JMB8 EXPRESSION TAG
SEQRES 1 A 264 ASP PRO TYR TRP ALA TYR SER GLY ALA TYR GLY PRO GLU
SEQRES 2 A 264 HIS TRP VAL THR SER SER VAL SER CYS GLY GLY SER HIS
SEQRES 3 A 264 GLN SER PRO ILE ASP ILE LEU ASP HIS HIS ALA ARG VAL
SEQRES 4 A 264 GLY ASP GLU TYR GLN GLU LEU GLN LEU ASP GLY PHE ASP
SEQRES 5 A 264 ASN GLU SER SER ASN LYS THR TRP MET LYS ASN THR GLY
SEQRES 6 A 264 LYS THR VAL ALA ILE LEU LEU LYS ASP ASP TYR PHE VAL
SEQRES 7 A 264 SER GLY ALA GLY LEU PRO GLY ARG PHE LYS ALA GLU LYS
SEQRES 8 A 264 VAL GLU PHE HIS TRP GLY HIS SER ASN GLY SER ALA GLY
SEQRES 9 A 264 SER GLU HIS SER VAL ASN GLY ARG ARG PHE PRO VAL GLU
SEQRES 10 A 264 MET GLN ILE PHE PHE TYR ASN PRO ASP ASP PHE ASP SER
SEQRES 11 A 264 PHE GLN THR ALA ILE SER GLU ASN ARG ILE ILE GLY ALA
SEQRES 12 A 264 MET ALA ILE PHE PHE GLN VAL SER PRO ARG ASP ASN SER
SEQRES 13 A 264 ALA LEU ASP PRO ILE ILE HIS GLY LEU LYS GLY VAL VAL
SEQRES 14 A 264 HIS HIS GLU LYS GLU THR PHE LEU ASP PRO PHE ILE LEU
SEQRES 15 A 264 ARG ASP LEU LEU PRO ALA SER LEU GLY SER TYR TYR ARG
SEQRES 16 A 264 TYR THR GLY SER LEU THR THR PRO PRO CYS SER GLU ILE
SEQRES 17 A 264 VAL GLU TRP ILE VAL PHE ARG ARG PRO VAL PRO ILE SER
SEQRES 18 A 264 TYR HIS GLN LEU GLU ALA PHE TYR SER ILE PHE THR THR
SEQRES 19 A 264 GLU GLN GLN ASP HIS VAL LYS SER VAL GLU TYR LEU ARG
SEQRES 20 A 264 ASN ASN PHE ARG PRO GLN GLN ALA LEU ASN ASP ARG VAL
SEQRES 21 A 264 VAL SER LYS SER
SEQRES 1 B 199 SER ALA TYR ILE GLU ASP PHE GLU THR LYS THR ARG SER
SEQRES 2 B 199 THR VAL SER VAL ARG GLU GLY GLN GLY VAL VAL LEU LEU
SEQRES 3 B 199 CYS GLY PRO PRO PRO HIS PHE GLY GLU LEU SER TYR ALA
SEQRES 4 B 199 TRP THR PHE ASN ASP SER PRO LEU TYR VAL GLN GLU ASP
SEQRES 5 B 199 LYS ARG ARG PHE VAL SER GLN ASP THR GLY ASN LEU TYR
SEQRES 6 B 199 PHE ALA LYS VAL GLU PRO SER ASP VAL GLY ASN TYR THR
SEQRES 7 B 199 CYS PHE VAL THR ASN LYS GLU ALA HIS ARG SER VAL GLN
SEQRES 8 B 199 GLY PRO PRO THR PRO LEU VAL LEU ARG THR ASP GLY VAL
SEQRES 9 B 199 MET GLY GLU TYR GLU PRO LYS ILE GLU VAL ARG PHE PRO
SEQRES 10 B 199 GLU THR ILE GLN ALA ALA LYS ASP SER SER ILE LYS LEU
SEQRES 11 B 199 GLU CYS PHE ALA LEU GLY ASN PRO VAL PRO ASP ILE SER
SEQRES 12 B 199 TRP LYS ARG LEU ASP GLY SER PRO MET PRO GLY LYS ILE
SEQRES 13 B 199 LYS TYR SER LYS SER GLN ALA ILE LEU GLU ILE PRO LYS
SEQRES 14 B 199 PHE GLN GLN GLU ASP GLU GLY PHE TYR GLU CYS ILE ALA
SEQRES 15 B 199 GLY ASN LEU ARG GLY ARG ASN LEU ALA LYS GLY GLN LEU
SEQRES 16 B 199 ILE PHE TYR ALA
SEQRES 1 C 264 ASP PRO TYR TRP ALA TYR SER GLY ALA TYR GLY PRO GLU
SEQRES 2 C 264 HIS TRP VAL THR SER SER VAL SER CYS GLY GLY SER HIS
SEQRES 3 C 264 GLN SER PRO ILE ASP ILE LEU ASP HIS HIS ALA ARG VAL
SEQRES 4 C 264 GLY ASP GLU TYR GLN GLU LEU GLN LEU ASP GLY PHE ASP
SEQRES 5 C 264 ASN GLU SER SER ASN LYS THR TRP MET LYS ASN THR GLY
SEQRES 6 C 264 LYS THR VAL ALA ILE LEU LEU LYS ASP ASP TYR PHE VAL
SEQRES 7 C 264 SER GLY ALA GLY LEU PRO GLY ARG PHE LYS ALA GLU LYS
SEQRES 8 C 264 VAL GLU PHE HIS TRP GLY HIS SER ASN GLY SER ALA GLY
SEQRES 9 C 264 SER GLU HIS SER VAL ASN GLY ARG ARG PHE PRO VAL GLU
SEQRES 10 C 264 MET GLN ILE PHE PHE TYR ASN PRO ASP ASP PHE ASP SER
SEQRES 11 C 264 PHE GLN THR ALA ILE SER GLU ASN ARG ILE ILE GLY ALA
SEQRES 12 C 264 MET ALA ILE PHE PHE GLN VAL SER PRO ARG ASP ASN SER
SEQRES 13 C 264 ALA LEU ASP PRO ILE ILE HIS GLY LEU LYS GLY VAL VAL
SEQRES 14 C 264 HIS HIS GLU LYS GLU THR PHE LEU ASP PRO PHE ILE LEU
SEQRES 15 C 264 ARG ASP LEU LEU PRO ALA SER LEU GLY SER TYR TYR ARG
SEQRES 16 C 264 TYR THR GLY SER LEU THR THR PRO PRO CYS SER GLU ILE
SEQRES 17 C 264 VAL GLU TRP ILE VAL PHE ARG ARG PRO VAL PRO ILE SER
SEQRES 18 C 264 TYR HIS GLN LEU GLU ALA PHE TYR SER ILE PHE THR THR
SEQRES 19 C 264 GLU GLN GLN ASP HIS VAL LYS SER VAL GLU TYR LEU ARG
SEQRES 20 C 264 ASN ASN PHE ARG PRO GLN GLN ALA LEU ASN ASP ARG VAL
SEQRES 21 C 264 VAL SER LYS SER
SEQRES 1 D 199 SER ALA TYR ILE GLU ASP PHE GLU THR LYS THR ARG SER
SEQRES 2 D 199 THR VAL SER VAL ARG GLU GLY GLN GLY VAL VAL LEU LEU
SEQRES 3 D 199 CYS GLY PRO PRO PRO HIS PHE GLY GLU LEU SER TYR ALA
SEQRES 4 D 199 TRP THR PHE ASN ASP SER PRO LEU TYR VAL GLN GLU ASP
SEQRES 5 D 199 LYS ARG ARG PHE VAL SER GLN ASP THR GLY ASN LEU TYR
SEQRES 6 D 199 PHE ALA LYS VAL GLU PRO SER ASP VAL GLY ASN TYR THR
SEQRES 7 D 199 CYS PHE VAL THR ASN LYS GLU ALA HIS ARG SER VAL GLN
SEQRES 8 D 199 GLY PRO PRO THR PRO LEU VAL LEU ARG THR ASP GLY VAL
SEQRES 9 D 199 MET GLY GLU TYR GLU PRO LYS ILE GLU VAL ARG PHE PRO
SEQRES 10 D 199 GLU THR ILE GLN ALA ALA LYS ASP SER SER ILE LYS LEU
SEQRES 11 D 199 GLU CYS PHE ALA LEU GLY ASN PRO VAL PRO ASP ILE SER
SEQRES 12 D 199 TRP LYS ARG LEU ASP GLY SER PRO MET PRO GLY LYS ILE
SEQRES 13 D 199 LYS TYR SER LYS SER GLN ALA ILE LEU GLU ILE PRO LYS
SEQRES 14 D 199 PHE GLN GLN GLU ASP GLU GLY PHE TYR GLU CYS ILE ALA
SEQRES 15 D 199 GLY ASN LEU ARG GLY ARG ASN LEU ALA LYS GLY GLN LEU
SEQRES 16 D 199 ILE PHE TYR ALA
HET 1PS A 401 13
HET 1PS A 402 13
HET FMT A 403 3
HET FMT A 404 3
HET MLI A 405 7
HET ACY B 401 4
HET FMT B 402 3
HET MLT B 403 9
HET 1PS C 401 13
HET 1PS C 402 13
HET MLT C 403 9
HET MLT D 401 9
HET ACY D 402 4
HET MLT D 403 9
HETNAM 1PS 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE
HETNAM FMT FORMIC ACID
HETNAM MLI MALONATE ION
HETNAM ACY ACETIC ACID
HETNAM MLT D-MALATE
HETSYN 1PS 1-(3-SULFOPROPYL) PYRIDINIUM; PPS
HETSYN MLT (2R)-2-HYDROXYBUTANEDIOIC ACID; 2-HYDROXY-SUCCINIC ACID
FORMUL 5 1PS 4(C8 H11 N O3 S)
FORMUL 7 FMT 3(C H2 O2)
FORMUL 9 MLI C3 H2 O4 2-
FORMUL 10 ACY 2(C2 H4 O2)
FORMUL 12 MLT 4(C4 H6 O5)
FORMUL 19 HOH *535(H2 O)
HELIX 1 AA1 SER A 63 GLY A 67 5 5
HELIX 2 AA2 HIS A 70 SER A 75 1 6
HELIX 3 AA3 VAL A 76 GLY A 80 5 5
HELIX 4 AA4 LEU A 89 ALA A 93 5 5
HELIX 5 AA5 SER A 186 ASN A 194 1 9
HELIX 6 AA6 ASN A 211 ALA A 213 5 3
HELIX 7 AA7 LEU A 214 GLY A 223 1 10
HELIX 8 AA8 ILE A 237 LEU A 242 5 6
HELIX 9 AA9 TYR A 278 GLU A 282 1 5
HELIX 10 AB1 GLU B 187 VAL B 191 5 5
HELIX 11 AB2 GLN B 288 GLU B 292 5 5
HELIX 12 AB3 GLY C 67 SER C 74 5 8
HELIX 13 AB4 SER C 75 GLY C 80 5 6
HELIX 14 AB5 LEU C 89 ALA C 93 5 5
HELIX 15 AB6 SER C 186 GLU C 193 1 8
HELIX 16 AB7 ASN C 211 ALA C 213 5 3
HELIX 17 AB8 LEU C 214 GLY C 223 1 10
HELIX 18 AB9 ILE C 237 LEU C 242 5 6
HELIX 19 AC1 TYR C 278 SER C 286 1 9
HELIX 20 AC2 GLU D 187 VAL D 191 5 5
HELIX 21 AC3 GLN D 288 GLU D 292 5 5
SHEET 1 AA1 2 ASP A 87 ILE A 88 0
SHEET 2 AA1 2 SER A 164 VAL A 165 1 O SER A 164 N ILE A 88
SHEET 1 AA210 ARG A 94 VAL A 95 0
SHEET 2 AA210 SER A 318 LYS A 319 1 O LYS A 319 N ARG A 94
SHEET 3 AA210 TYR A 249 GLY A 254 -1 N ARG A 251 O SER A 318
SHEET 4 AA210 VAL A 265 PHE A 270 -1 O VAL A 265 N GLY A 254
SHEET 5 AA210 ILE A 197 SER A 207 1 N ALA A 199 O ILE A 268
SHEET 6 AA210 VAL A 172 TYR A 179 -1 N PHE A 178 O GLY A 198
SHEET 7 AA210 PHE A 143 TRP A 152 -1 N LYS A 144 O TYR A 179
SHEET 8 AA210 VAL A 124 LEU A 127 -1 N ILE A 126 O VAL A 148
SHEET 9 AA210 TRP A 116 ASN A 119 -1 N LYS A 118 O ALA A 125
SHEET 10 AA210 GLU A 230 PHE A 232 -1 O THR A 231 N MET A 117
SHEET 1 AA3 6 GLN A 103 ASP A 105 0
SHEET 2 AA3 6 PHE A 133 SER A 135 -1 O PHE A 133 N ASP A 105
SHEET 3 AA3 6 PHE A 143 TRP A 152 -1 O PHE A 143 N VAL A 134
SHEET 4 AA3 6 VAL A 172 TYR A 179 -1 O TYR A 179 N LYS A 144
SHEET 5 AA3 6 ILE A 197 SER A 207 -1 O GLY A 198 N PHE A 178
SHEET 6 AA3 6 VAL A 274 SER A 277 1 O VAL A 274 N PHE A 203
SHEET 1 AA4 5 PHE A 288 GLN A 292 0
SHEET 2 AA4 5 VAL A 296 TYR A 301 -1 O GLU A 300 N THR A 289
SHEET 3 AA4 5 VAL B 140 LEU B 142 -1 O VAL B 141 N LYS A 297
SHEET 4 AA4 5 LEU B 181 PHE B 183 -1 O PHE B 183 N VAL B 140
SHEET 5 AA4 5 ARG B 172 VAL B 174 -1 N PHE B 173 O TYR B 182
SHEET 1 AA5 2 TYR B 120 ILE B 121 0
SHEET 2 AA5 2 HIS B 149 PHE B 150 -1 O PHE B 150 N TYR B 120
SHEET 1 AA6 5 VAL B 132 VAL B 134 0
SHEET 2 AA6 5 THR B 212 LEU B 216 1 O PRO B 213 N VAL B 132
SHEET 3 AA6 5 GLY B 192 ASN B 200 -1 N GLY B 192 O LEU B 214
SHEET 4 AA6 5 LEU B 153 PHE B 159 -1 N ALA B 156 O PHE B 197
SHEET 5 AA6 5 SER B 162 PRO B 163 -1 O SER B 162 N PHE B 159
SHEET 1 AA7 4 VAL B 132 VAL B 134 0
SHEET 2 AA7 4 THR B 212 LEU B 216 1 O PRO B 213 N VAL B 132
SHEET 3 AA7 4 GLY B 192 ASN B 200 -1 N GLY B 192 O LEU B 214
SHEET 4 AA7 4 ARG B 205 GLN B 208 -1 O ARG B 205 N ASN B 200
SHEET 1 AA8 2 TYR B 225 VAL B 231 0
SHEET 2 AA8 2 PHE B 250 ASN B 254 -1 O LEU B 252 N LYS B 228
SHEET 1 AA9 4 THR B 236 ALA B 240 0
SHEET 2 AA9 4 GLY B 304 TYR B 315 1 O ILE B 313 N ALA B 239
SHEET 3 AA9 4 GLY B 293 ASN B 301 -1 N ALA B 299 O ASN B 306
SHEET 4 AA9 4 ASP B 258 ARG B 263 -1 N SER B 260 O ILE B 298
SHEET 1 AB1 3 ILE B 245 GLU B 248 0
SHEET 2 AB1 3 ILE B 281 ILE B 284 -1 O ILE B 284 N ILE B 245
SHEET 3 AB1 3 LYS B 274 SER B 276 -1 N LYS B 274 O GLU B 283
SHEET 1 AB2 2 ASP C 87 ILE C 88 0
SHEET 2 AB2 2 SER C 164 VAL C 165 1 O SER C 164 N ILE C 88
SHEET 1 AB310 ARG C 94 VAL C 95 0
SHEET 2 AB310 SER C 318 LYS C 319 1 O LYS C 319 N ARG C 94
SHEET 3 AB310 TYR C 249 GLY C 254 -1 N ARG C 251 O SER C 318
SHEET 4 AB310 VAL C 265 PHE C 270 -1 O VAL C 265 N GLY C 254
SHEET 5 AB310 ILE C 197 SER C 207 1 N ALA C 199 O ILE C 268
SHEET 6 AB310 VAL C 172 TYR C 179 -1 N PHE C 178 O GLY C 198
SHEET 7 AB310 PHE C 143 TRP C 152 -1 N LYS C 144 O TYR C 179
SHEET 8 AB310 VAL C 124 LEU C 127 -1 N ILE C 126 O VAL C 148
SHEET 9 AB310 TRP C 116 ASN C 119 -1 N LYS C 118 O ALA C 125
SHEET 10 AB310 GLU C 230 PHE C 232 -1 O THR C 231 N MET C 117
SHEET 1 AB4 6 GLN C 103 ASP C 105 0
SHEET 2 AB4 6 PHE C 133 SER C 135 -1 O PHE C 133 N ASP C 105
SHEET 3 AB4 6 PHE C 143 TRP C 152 -1 O PHE C 143 N VAL C 134
SHEET 4 AB4 6 VAL C 172 TYR C 179 -1 O TYR C 179 N LYS C 144
SHEET 5 AB4 6 ILE C 197 SER C 207 -1 O GLY C 198 N PHE C 178
SHEET 6 AB4 6 VAL C 274 SER C 277 1 O VAL C 274 N GLN C 205
SHEET 1 AB5 5 PHE C 288 GLN C 292 0
SHEET 2 AB5 5 VAL C 296 TYR C 301 -1 O GLU C 300 N THR C 289
SHEET 3 AB5 5 VAL D 140 LEU D 142 -1 O VAL D 141 N LYS C 297
SHEET 4 AB5 5 LEU D 181 PHE D 183 -1 O PHE D 183 N VAL D 140
SHEET 5 AB5 5 ARG D 172 VAL D 174 -1 N PHE D 173 O TYR D 182
SHEET 1 AB6 2 TYR D 120 ILE D 121 0
SHEET 2 AB6 2 HIS D 149 PHE D 150 -1 O PHE D 150 N TYR D 120
SHEET 1 AB7 5 VAL D 132 GLU D 136 0
SHEET 2 AB7 5 THR D 212 VAL D 221 1 O PRO D 213 N VAL D 132
SHEET 3 AB7 5 GLY D 192 ASN D 200 -1 N GLY D 192 O LEU D 214
SHEET 4 AB7 5 LEU D 153 PHE D 159 -1 N ALA D 156 O PHE D 197
SHEET 5 AB7 5 SER D 162 PRO D 163 -1 O SER D 162 N PHE D 159
SHEET 1 AB8 4 VAL D 132 GLU D 136 0
SHEET 2 AB8 4 THR D 212 VAL D 221 1 O PRO D 213 N VAL D 132
SHEET 3 AB8 4 GLY D 192 ASN D 200 -1 N GLY D 192 O LEU D 214
SHEET 4 AB8 4 ARG D 205 GLN D 208 -1 O VAL D 207 N VAL D 198
SHEET 1 AB9 4 TYR D 225 ARG D 232 0
SHEET 2 AB9 4 ILE D 245 ASN D 254 -1 O LEU D 252 N LYS D 228
SHEET 3 AB9 4 ILE D 281 ILE D 284 -1 O ILE D 284 N ILE D 245
SHEET 4 AB9 4 LYS D 274 SER D 276 -1 N LYS D 274 O GLU D 283
SHEET 1 AC1 4 THR D 236 ALA D 240 0
SHEET 2 AC1 4 GLY D 304 TYR D 315 1 O ILE D 313 N ALA D 239
SHEET 3 AC1 4 GLY D 293 ASN D 301 -1 N CYS D 297 O ALA D 308
SHEET 4 AC1 4 ASP D 258 ARG D 263 -1 N SER D 260 O ILE D 298
SSBOND 1 CYS A 78 CYS A 261 1555 1555 2.03
SSBOND 2 CYS B 144 CYS B 196 1555 1555 2.03
SSBOND 3 CYS B 249 CYS B 297 1555 1555 2.04
SSBOND 4 CYS C 78 CYS C 261 1555 1555 2.04
SSBOND 5 CYS D 144 CYS D 196 1555 1555 2.03
SSBOND 6 CYS D 249 CYS D 297 1555 1555 2.01
CISPEP 1 SER A 84 PRO A 85 0 4.34
CISPEP 2 PRO A 259 PRO A 260 0 9.54
CISPEP 3 ASN B 254 PRO B 255 0 4.85
CISPEP 4 SER C 84 PRO C 85 0 0.63
CISPEP 5 PRO C 259 PRO C 260 0 6.96
CISPEP 6 ASN D 254 PRO D 255 0 1.55
SITE 1 AC1 3 TRP A 116 GLU A 230 PHE A 232
SITE 1 AC2 10 HIS A 91 HIS A 92 HOH A 580 TYR B 315
SITE 2 AC2 10 ALA B 316 HIS C 92 ASN C 313 ASP C 314
SITE 3 AC2 10 ARG C 315 HOH C 525
SITE 1 AC3 5 GLN A 293 ASP A 294 HIS A 295 VAL A 296
SITE 2 AC3 5 ASP C 294
SITE 1 AC4 3 SER A 286 HOH A 505 HOH A 601
SITE 1 AC5 11 GLY A 64 ALA A 65 GLY A 67 PRO A 68
SITE 2 AC5 11 GLU A 69 HIS A 70 HOH A 504 PRO D 146
SITE 3 AC5 11 HIS D 149 TYR D 155 THR D 178
SITE 1 AC6 2 TYR B 165 ARG B 172
SITE 1 AC7 7 VAL B 166 ASP B 169 ARG B 172 PHE B 173
SITE 2 AC7 7 LYS B 277 HOH B 503 HOH B 581
SITE 1 AC8 4 ARG B 303 LEU D 264 PHE D 294 LYS D 309
SITE 1 AC9 3 TRP C 116 GLU C 230 PHE C 232
SITE 1 AD1 7 TYR A 59 GLN A 292 PRO C 58 TYR C 59
SITE 2 AD1 7 TYR C 66 GLN C 292 HOH C 562
SITE 1 AD2 5 VAL C 165 ASN C 166 ARG C 168 ARG C 271
SITE 2 AD2 5 LYS D 241
SITE 1 AD3 6 GLU D 168 TYR D 275 SER D 276 LYS D 277
SITE 2 AD3 6 SER D 278 GLN D 279
SITE 1 AD4 5 TYR B 165 TYR D 155 VAL D 166 GLN D 167
SITE 2 AD4 5 HOH D 516
SITE 1 AD5 7 GLY A 64 ALA A 65 HIS C 295 PHE D 124
SITE 2 AD5 7 GLU D 125 THR D 126 ARG D 129
CRYST1 78.641 113.530 117.046 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 0.012716 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008544 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
