HEADER HYDROLASE/CELL ADHESION 09-OCT-15 5E5R
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBONIC ANHYDRASE-LIKE
TITLE 2 DOMAIN OF PTPRG AND IMMUNOGLOBULIN DOMAINS 2-3 OF CNTN3
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 56-320;
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-3;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: IMMUNOGLOBULIN DOMAINS 2-3, UNP RESIDUES 124-316;
COMPND 12 SYNONYM: BRAIN-DERIVED IMMUNOGLOBULIN SUPERFAMILY PROTEIN 1,BIG-1,
COMPND 13 PLASMACYTOMA-ASSOCIATED NEURONAL GLYCOPROTEIN;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTPRG, PTPG;
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: CNTN3, PANG, PCS;
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 HYDROLASE-CELL ADHESION COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.NIKOLAIENKO,S.BOUYAIN
REVDAT 5 27-SEP-23 5E5R 1 REMARK
REVDAT 4 25-DEC-19 5E5R 1 REMARK
REVDAT 3 27-SEP-17 5E5R 1 JRNL
REVDAT 2 23-NOV-16 5E5R 1 JRNL
REVDAT 1 31-AUG-16 5E5R 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. 2.60 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 31039
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1553
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 49.1581 - 5.7792 0.99 2871 152 0.1587 0.1968
REMARK 3 2 5.7792 - 4.5882 1.00 2731 144 0.1445 0.1683
REMARK 3 3 4.5882 - 4.0085 0.99 2702 141 0.1529 0.2329
REMARK 3 4 4.0085 - 3.6422 0.99 2688 142 0.1932 0.2821
REMARK 3 5 3.6422 - 3.3812 1.00 2673 140 0.2037 0.2656
REMARK 3 6 3.3812 - 3.1819 1.00 2686 142 0.2300 0.3300
REMARK 3 7 3.1819 - 3.0225 1.00 2662 139 0.2375 0.3152
REMARK 3 8 3.0225 - 2.8910 1.00 2655 141 0.2432 0.3049
REMARK 3 9 2.8910 - 2.7797 1.00 2656 140 0.2520 0.3394
REMARK 3 10 2.7797 - 2.6838 0.99 2633 139 0.2477 0.3738
REMARK 3 11 2.6838 - 2.6000 0.95 2529 133 0.2666 0.3391
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.22
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 : 0.009 7425
REMARK 3 ANGLE : 1.101 10054
REMARK 3 CHIRALITY : 0.043 1054
REMARK 3 PLANARITY : 0.005 1325
REMARK 3 DIHEDRAL : 14.013 2730
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): -50.8968 -30.1627 26.6603
REMARK 3 T TENSOR
REMARK 3 T11: 0.5856 T22: 0.6535
REMARK 3 T33: 0.3219 T12: -0.1063
REMARK 3 T13: 0.1227 T23: -0.1415
REMARK 3 L TENSOR
REMARK 3 L11: 4.6285 L22: 8.6906
REMARK 3 L33: 5.7250 L12: 1.6527
REMARK 3 L13: 0.7752 L23: -1.3528
REMARK 3 S TENSOR
REMARK 3 S11: 0.5948 S12: -1.0018 S13: 0.5469
REMARK 3 S21: 1.2093 S22: -0.6945 S23: 0.4008
REMARK 3 S31: -0.7238 S32: -0.0995 S33: 0.1015
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 125:221))
REMARK 3 ORIGIN FOR THE GROUP (A): -59.1349 -62.0775 8.0005
REMARK 3 T TENSOR
REMARK 3 T11: 0.7823 T22: 0.4516
REMARK 3 T33: 0.4836 T12: -0.1177
REMARK 3 T13: 0.1296 T23: 0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 7.0585 L22: 8.4455
REMARK 3 L33: 8.5221 L12: -1.8588
REMARK 3 L13: -2.0720 L23: -0.4639
REMARK 3 S TENSOR
REMARK 3 S11: -0.6550 S12: -0.3695 S13: -1.3076
REMARK 3 S21: 0.5627 S22: 0.0813 S23: 0.3603
REMARK 3 S31: 1.6062 S32: -0.0560 S33: 0.5597
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND ((RESSEQ 222:316))
REMARK 3 ORIGIN FOR THE GROUP (A): -53.3906 -46.0216 -7.1526
REMARK 3 T TENSOR
REMARK 3 T11: 0.6385 T22: 0.4954
REMARK 3 T33: 0.3857 T12: -0.2102
REMARK 3 T13: -0.1806 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 7.6105 L22: 2.8320
REMARK 3 L33: 8.9292 L12: 0.1366
REMARK 3 L13: -4.6610 L23: 1.7228
REMARK 3 S TENSOR
REMARK 3 S11: -0.5929 S12: 1.1433 S13: 0.2597
REMARK 3 S21: -0.6984 S22: 0.2089 S23: 0.1894
REMARK 3 S31: -0.1797 S32: -0.6112 S33: 0.4157
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND ((RESSEQ 57:320))
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1068 -20.7316 45.2127
REMARK 3 T TENSOR
REMARK 3 T11: 0.3818 T22: 0.4762
REMARK 3 T33: 0.2915 T12: -0.1012
REMARK 3 T13: 0.0477 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 5.5280 L22: 6.1894
REMARK 3 L33: 4.9602 L12: 2.3702
REMARK 3 L13: -1.9941 L23: -0.4220
REMARK 3 S TENSOR
REMARK 3 S11: -0.4434 S12: 0.9460 S13: -0.0926
REMARK 3 S21: -0.7902 S22: 0.4963 S23: -0.6132
REMARK 3 S31: 0.0381 S32: 0.0242 S33: -0.0618
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 124:221))
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9765 -7.5001 79.5404
REMARK 3 T TENSOR
REMARK 3 T11: 0.5033 T22: 0.2381
REMARK 3 T33: 0.3290 T12: -0.0097
REMARK 3 T13: 0.0958 T23: -0.0447
REMARK 3 L TENSOR
REMARK 3 L11: 8.1294 L22: 6.9970
REMARK 3 L33: 8.2253 L12: 0.5034
REMARK 3 L13: 3.5043 L23: 0.6640
REMARK 3 S TENSOR
REMARK 3 S11: -0.2538 S12: -0.1499 S13: 0.5514
REMARK 3 S21: 0.4235 S22: -0.0788 S23: -0.1909
REMARK 3 S31: -1.0936 S32: 0.0514 S33: 0.3293
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'D' AND ((RESSEQ 222:316))
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6258 -29.8919 81.0980
REMARK 3 T TENSOR
REMARK 3 T11: 0.4422 T22: 0.2954
REMARK 3 T33: 0.3969 T12: -0.0845
REMARK 3 T13: 0.1638 T23: -0.1155
REMARK 3 L TENSOR
REMARK 3 L11: 4.8729 L22: 7.5844
REMARK 3 L33: 8.7254 L12: -4.9212
REMARK 3 L13: 5.5912 L23: -7.1076
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: -0.1330 S13: 0.0500
REMARK 3 S21: -0.0420 S22: -0.0639 S23: -0.2441
REMARK 3 S31: 0.2498 S32: -0.0085 S33: 0.0625
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 5E5R 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_1000214401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
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 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31166
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.58800
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: 3JXH, 5E4I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1% (V/V) TACSIMATE PH 7.0, 20% (W/V)
REMARK 280 PEG 3350, 50MM IMIDAZOLE-HCL PH 6.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 37.06900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.26300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.06900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.26300
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 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 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 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 VAL A 95
REMARK 465 GLY A 96
REMARK 465 GLU A 97
REMARK 465 GLU A 98
REMARK 465 TYR A 99
REMARK 465 GLN A 100
REMARK 465 ILE A 165
REMARK 465 PHE B 124
REMARK 465 PRO B 148
REMARK 465 HIS B 149
REMARK 465 SER B 150
REMARK 465 GLY B 151
REMARK 465 SER B 164
REMARK 465 GLY C 56
REMARK 465 HIS D 149
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 ASN A 156 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH2 ARG C 169 O HOH C 501 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 278 OE1 GLN C 100 1455 2.14
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 GLU A 228 -12.88 94.06
REMARK 500 ASP A 294 -131.51 52.76
REMARK 500 HIS A 295 40.23 -104.98
REMARK 500 ASN A 305 58.74 -93.29
REMARK 500 HIS A 313 -127.34 54.10
REMARK 500 ASN B 160 -52.69 66.21
REMARK 500 ASP B 169 -161.58 -165.38
REMARK 500 THR B 203 -158.58 -143.61
REMARK 500 GLU B 226 151.64 -44.34
REMARK 500 ALA C 93 -156.77 -79.17
REMARK 500 GLU C 98 28.83 46.73
REMARK 500 HIS C 154 -57.30 -126.79
REMARK 500 PRO C 181 -168.87 -68.90
REMARK 500 ASP C 182 -18.33 66.74
REMARK 500 HIS C 227 129.31 -34.20
REMARK 500 GLU C 228 -2.80 77.77
REMARK 500 ILE C 264 15.32 -144.09
REMARK 500 ASP C 294 73.58 46.24
REMARK 500 HIS C 313 -123.47 52.46
REMARK 500 CYS D 144 -68.58 -92.13
REMARK 500 ASN D 160 -119.36 58.14
REMARK 500 PRO D 163 48.75 -102.63
REMARK 500 ASP D 169 -153.27 -151.15
REMARK 500 VAL D 202 -75.23 -78.41
REMARK 500 CYS D 249 114.73 -162.38
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 MLI A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI D 401
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: 5E5U RELATED DB: PDB
DBREF 5E5R A 56 320 UNP P23470 PTPRG_HUMAN 56 320
DBREF 5E5R B 124 316 UNP Q07409 CNTN3_MOUSE 124 316
DBREF 5E5R C 56 320 UNP P23470 PTPRG_HUMAN 56 320
DBREF 5E5R D 124 316 UNP Q07409 CNTN3_MOUSE 124 316
SEQRES 1 A 265 GLY ASP PRO TYR TRP ALA TYR SER GLY ALA TYR GLY PRO
SEQRES 2 A 265 GLU HIS TRP VAL THR SER SER VAL SER CYS GLY GLY ARG
SEQRES 3 A 265 HIS GLN SER PRO ILE ASP ILE LEU ASP GLN TYR ALA ARG
SEQRES 4 A 265 VAL GLY GLU GLU TYR GLN GLU LEU GLN LEU ASP GLY PHE
SEQRES 5 A 265 ASP ASN GLU SER SER ASN LYS THR TRP MET LYS ASN THR
SEQRES 6 A 265 GLY LYS THR VAL ALA ILE LEU LEU LYS ASP ASP TYR PHE
SEQRES 7 A 265 VAL SER GLY ALA GLY LEU PRO GLY ARG PHE LYS ALA GLU
SEQRES 8 A 265 LYS VAL GLU PHE HIS TRP GLY HIS SER ASN GLY SER ALA
SEQRES 9 A 265 GLY SER GLU HIS SER ILE ASN GLY ARG ARG PHE PRO VAL
SEQRES 10 A 265 GLU MET GLN ILE PHE PHE TYR ASN PRO ASP ASP PHE ASP
SEQRES 11 A 265 SER PHE GLN THR ALA ILE SER GLU ASN ARG ILE ILE GLY
SEQRES 12 A 265 ALA MET ALA ILE PHE PHE GLN VAL SER PRO ARG ASP ASN
SEQRES 13 A 265 SER ALA LEU ASP PRO ILE ILE HIS GLY LEU LYS GLY VAL
SEQRES 14 A 265 VAL HIS HIS GLU LYS GLU THR PHE LEU ASP PRO PHE VAL
SEQRES 15 A 265 LEU ARG ASP LEU LEU PRO ALA SER LEU GLY SER TYR TYR
SEQRES 16 A 265 ARG TYR THR GLY SER LEU THR THR PRO PRO CYS SER GLU
SEQRES 17 A 265 ILE VAL GLU TRP ILE VAL PHE ARG ARG PRO VAL PRO ILE
SEQRES 18 A 265 SER TYR HIS GLN LEU GLU ALA PHE TYR SER ILE PHE THR
SEQRES 19 A 265 THR GLU GLN GLN ASP HIS VAL LYS SER VAL GLU TYR LEU
SEQRES 20 A 265 ARG ASN ASN PHE ARG PRO GLN GLN ARG LEU HIS ASP ARG
SEQRES 21 A 265 VAL VAL SER LYS SER
SEQRES 1 B 193 PHE LYS THR ARG MET ARG SER THR VAL SER VAL ARG GLU
SEQRES 2 B 193 GLY GLN GLY VAL VAL LEU LEU CYS GLY PRO PRO PRO HIS
SEQRES 3 B 193 SER GLY GLU LEU SER TYR ALA TRP VAL PHE ASN GLU TYR
SEQRES 4 B 193 PRO SER PHE VAL GLU GLU ASP SER ARG ARG PHE VAL SER
SEQRES 5 B 193 GLN GLU THR GLY HIS LEU TYR ILE ALA LYS VAL GLU PRO
SEQRES 6 B 193 SER ASP VAL GLY ASN TYR THR CYS VAL VAL THR SER THR
SEQRES 7 B 193 VAL THR ASN THR ARG VAL LEU GLY SER PRO THR PRO LEU
SEQRES 8 B 193 VAL LEU ARG SER ASP GLY VAL MET GLY GLU TYR GLU PRO
SEQRES 9 B 193 LYS ILE GLU VAL GLN PHE PRO GLU THR LEU PRO ALA ALA
SEQRES 10 B 193 LYS GLY SER THR VAL ARG LEU GLU CYS PHE ALA LEU GLY
SEQRES 11 B 193 ASN PRO VAL PRO GLN ILE ASN TRP ARG ARG SER ASP GLY
SEQRES 12 B 193 MET PRO PHE PRO ASN LYS ILE LYS LEU ARG LYS PHE ASN
SEQRES 13 B 193 GLY MET LEU GLU ILE GLN ASN PHE GLN GLN GLU ASP THR
SEQRES 14 B 193 GLY SER TYR GLU CYS ILE ALA GLU ASN SER ARG GLY LYS
SEQRES 15 B 193 ASN VAL ALA ARG GLY ARG LEU THR TYR TYR ALA
SEQRES 1 C 265 GLY ASP PRO TYR TRP ALA TYR SER GLY ALA TYR GLY PRO
SEQRES 2 C 265 GLU HIS TRP VAL THR SER SER VAL SER CYS GLY GLY ARG
SEQRES 3 C 265 HIS GLN SER PRO ILE ASP ILE LEU ASP GLN TYR ALA ARG
SEQRES 4 C 265 VAL GLY GLU GLU TYR GLN GLU LEU GLN LEU ASP GLY PHE
SEQRES 5 C 265 ASP ASN GLU SER SER ASN LYS THR TRP MET LYS ASN THR
SEQRES 6 C 265 GLY LYS THR VAL ALA ILE LEU LEU LYS ASP ASP TYR PHE
SEQRES 7 C 265 VAL SER GLY ALA GLY LEU PRO GLY ARG PHE LYS ALA GLU
SEQRES 8 C 265 LYS VAL GLU PHE HIS TRP GLY HIS SER ASN GLY SER ALA
SEQRES 9 C 265 GLY SER GLU HIS SER ILE ASN GLY ARG ARG PHE PRO VAL
SEQRES 10 C 265 GLU MET GLN ILE PHE PHE TYR ASN PRO ASP ASP PHE ASP
SEQRES 11 C 265 SER PHE GLN THR ALA ILE SER GLU ASN ARG ILE ILE GLY
SEQRES 12 C 265 ALA MET ALA ILE PHE PHE GLN VAL SER PRO ARG ASP ASN
SEQRES 13 C 265 SER ALA LEU ASP PRO ILE ILE HIS GLY LEU LYS GLY VAL
SEQRES 14 C 265 VAL HIS HIS GLU LYS GLU THR PHE LEU ASP PRO PHE VAL
SEQRES 15 C 265 LEU ARG ASP LEU LEU PRO ALA SER LEU GLY SER TYR TYR
SEQRES 16 C 265 ARG TYR THR GLY SER LEU THR THR PRO PRO CYS SER GLU
SEQRES 17 C 265 ILE VAL GLU TRP ILE VAL PHE ARG ARG PRO VAL PRO ILE
SEQRES 18 C 265 SER TYR HIS GLN LEU GLU ALA PHE TYR SER ILE PHE THR
SEQRES 19 C 265 THR GLU GLN GLN ASP HIS VAL LYS SER VAL GLU TYR LEU
SEQRES 20 C 265 ARG ASN ASN PHE ARG PRO GLN GLN ARG LEU HIS ASP ARG
SEQRES 21 C 265 VAL VAL SER LYS SER
SEQRES 1 D 193 PHE LYS THR ARG MET ARG SER THR VAL SER VAL ARG GLU
SEQRES 2 D 193 GLY GLN GLY VAL VAL LEU LEU CYS GLY PRO PRO PRO HIS
SEQRES 3 D 193 SER GLY GLU LEU SER TYR ALA TRP VAL PHE ASN GLU TYR
SEQRES 4 D 193 PRO SER PHE VAL GLU GLU ASP SER ARG ARG PHE VAL SER
SEQRES 5 D 193 GLN GLU THR GLY HIS LEU TYR ILE ALA LYS VAL GLU PRO
SEQRES 6 D 193 SER ASP VAL GLY ASN TYR THR CYS VAL VAL THR SER THR
SEQRES 7 D 193 VAL THR ASN THR ARG VAL LEU GLY SER PRO THR PRO LEU
SEQRES 8 D 193 VAL LEU ARG SER ASP GLY VAL MET GLY GLU TYR GLU PRO
SEQRES 9 D 193 LYS ILE GLU VAL GLN PHE PRO GLU THR LEU PRO ALA ALA
SEQRES 10 D 193 LYS GLY SER THR VAL ARG LEU GLU CYS PHE ALA LEU GLY
SEQRES 11 D 193 ASN PRO VAL PRO GLN ILE ASN TRP ARG ARG SER ASP GLY
SEQRES 12 D 193 MET PRO PHE PRO ASN LYS ILE LYS LEU ARG LYS PHE ASN
SEQRES 13 D 193 GLY MET LEU GLU ILE GLN ASN PHE GLN GLN GLU ASP THR
SEQRES 14 D 193 GLY SER TYR GLU CYS ILE ALA GLU ASN SER ARG GLY LYS
SEQRES 15 D 193 ASN VAL ALA ARG GLY ARG LEU THR TYR TYR ALA
HET MLI A 401 7
HET MLI C 401 7
HET FMT C 402 3
HET FMT C 403 3
HET MLI D 401 7
HETNAM MLI MALONATE ION
HETNAM FMT FORMIC ACID
FORMUL 5 MLI 3(C3 H2 O4 2-)
FORMUL 7 FMT 2(C H2 O2)
FORMUL 10 HOH *59(H2 O)
HELIX 1 AA1 SER A 63 GLU A 69 5 7
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 GLU A 193 1 8
HELIX 6 AA6 ASN A 211 ALA A 213 5 3
HELIX 7 AA7 LEU A 214 VAL A 224 1 11
HELIX 8 AA8 VAL A 237 LEU A 242 5 6
HELIX 9 AA9 SER A 277 SER A 286 1 10
HELIX 10 AB1 GLU B 187 VAL B 191 5 5
HELIX 11 AB2 LYS B 277 ASN B 279 5 3
HELIX 12 AB3 GLN B 288 THR B 292 5 5
HELIX 13 AB4 SER C 63 GLU C 69 5 7
HELIX 14 AB5 HIS C 70 SER C 75 1 6
HELIX 15 AB6 VAL C 76 GLY C 80 5 5
HELIX 16 AB7 LEU C 89 ALA C 93 5 5
HELIX 17 AB8 SER C 186 GLU C 193 1 8
HELIX 18 AB9 LEU C 214 LYS C 222 1 9
HELIX 19 AC1 VAL C 237 LEU C 242 5 6
HELIX 20 AC2 SER C 277 GLU C 282 1 6
HELIX 21 AC3 ALA C 283 SER C 286 5 4
HELIX 22 AC4 GLU D 187 VAL D 191 5 5
HELIX 23 AC5 LYS D 277 ASN D 279 5 3
HELIX 24 AC6 GLN D 288 THR D 292 5 5
SHEET 1 AA1 6 GLN A 103 ASP A 105 0
SHEET 2 AA1 6 PHE A 133 SER A 135 -1 O SER A 135 N GLN A 103
SHEET 3 AA1 6 PHE A 143 TRP A 152 -1 O PHE A 143 N VAL A 134
SHEET 4 AA1 6 VAL A 124 LEU A 127 -1 N ILE A 126 O VAL A 148
SHEET 5 AA1 6 TRP A 116 ASN A 119 -1 N LYS A 118 O ALA A 125
SHEET 6 AA1 6 GLU A 230 PHE A 232 -1 O THR A 231 N MET A 117
SHEET 1 AA2 8 GLN A 103 ASP A 105 0
SHEET 2 AA2 8 PHE A 133 SER A 135 -1 O SER A 135 N GLN A 103
SHEET 3 AA2 8 PHE A 143 TRP A 152 -1 O PHE A 143 N VAL A 134
SHEET 4 AA2 8 VAL A 172 TYR A 179 -1 O PHE A 177 N GLU A 146
SHEET 5 AA2 8 ILE A 197 VAL A 206 -1 O ILE A 202 N MET A 174
SHEET 6 AA2 8 VAL A 265 ILE A 276 1 O ILE A 268 N ALA A 201
SHEET 7 AA2 8 TYR A 249 GLY A 254 -1 N GLY A 254 O VAL A 265
SHEET 8 AA2 8 SER A 318 SER A 320 -1 O SER A 320 N TYR A 249
SHEET 1 AA3 5 PHE A 288 GLN A 293 0
SHEET 2 AA3 5 VAL A 296 TYR A 301 -1 O GLU A 300 N THR A 289
SHEET 3 AA3 5 VAL B 140 LEU B 142 -1 O VAL B 141 N LYS A 297
SHEET 4 AA3 5 LEU B 181 ILE B 183 -1 O LEU B 181 N LEU B 142
SHEET 5 AA3 5 ARG B 172 VAL B 174 -1 N PHE B 173 O TYR B 182
SHEET 1 AA4 4 VAL B 132 VAL B 134 0
SHEET 2 AA4 4 THR B 212 LEU B 216 1 O VAL B 215 N VAL B 134
SHEET 3 AA4 4 GLY B 192 SER B 200 -1 N TYR B 194 O THR B 212
SHEET 4 AA4 4 LEU B 153 PHE B 159 -1 N SER B 154 O THR B 199
SHEET 1 AA5 4 VAL B 132 VAL B 134 0
SHEET 2 AA5 4 THR B 212 LEU B 216 1 O VAL B 215 N VAL B 134
SHEET 3 AA5 4 GLY B 192 SER B 200 -1 N TYR B 194 O THR B 212
SHEET 4 AA5 4 ARG B 206 LEU B 208 -1 O VAL B 207 N VAL B 198
SHEET 1 AA6 4 TYR B 225 GLN B 232 0
SHEET 2 AA6 4 VAL B 245 ASN B 254 -1 O LEU B 252 N LYS B 228
SHEET 3 AA6 4 MET B 281 ILE B 284 -1 O ILE B 284 N VAL B 245
SHEET 4 AA6 4 ILE B 273 ARG B 276 -1 N LYS B 274 O GLU B 283
SHEET 1 AA7 4 THR B 236 ALA B 240 0
SHEET 2 AA7 4 GLY B 304 TYR B 315 1 O ARG B 311 N LEU B 237
SHEET 3 AA7 4 GLY B 293 ASN B 301 -1 N CYS B 297 O ALA B 308
SHEET 4 AA7 4 GLN B 258 ARG B 263 -1 N ASN B 260 O ILE B 298
SHEET 1 AA8 2 ASP C 87 ILE C 88 0
SHEET 2 AA8 2 SER C 164 ILE C 165 1 O SER C 164 N ILE C 88
SHEET 1 AA9 6 GLN C 103 ASP C 105 0
SHEET 2 AA9 6 PHE C 133 GLY C 136 -1 O SER C 135 N GLN C 103
SHEET 3 AA9 6 LEU C 139 TRP C 152 -1 O PHE C 143 N VAL C 134
SHEET 4 AA9 6 VAL C 172 TYR C 179 -1 O PHE C 177 N GLU C 146
SHEET 5 AA9 6 ILE C 197 VAL C 206 -1 O ILE C 202 N MET C 174
SHEET 6 AA9 6 VAL C 274 ILE C 276 1 O VAL C 274 N PHE C 203
SHEET 1 AB1 9 GLU C 230 PHE C 232 0
SHEET 2 AB1 9 TRP C 116 ASN C 119 -1 N MET C 117 O THR C 231
SHEET 3 AB1 9 VAL C 124 LEU C 127 -1 O ALA C 125 N LYS C 118
SHEET 4 AB1 9 LEU C 139 TRP C 152 -1 O VAL C 148 N ILE C 126
SHEET 5 AB1 9 VAL C 172 TYR C 179 -1 O PHE C 177 N GLU C 146
SHEET 6 AB1 9 ILE C 197 VAL C 206 -1 O ILE C 202 N MET C 174
SHEET 7 AB1 9 VAL C 265 PHE C 270 1 O ILE C 268 N ALA C 201
SHEET 8 AB1 9 TYR C 249 GLY C 254 -1 N GLY C 254 O VAL C 265
SHEET 9 AB1 9 SER C 318 LYS C 319 -1 O SER C 318 N ARG C 251
SHEET 1 AB2 5 PHE C 288 GLN C 293 0
SHEET 2 AB2 5 VAL C 296 TYR C 301 -1 O GLU C 300 N THR C 289
SHEET 3 AB2 5 VAL D 140 LEU D 142 -1 O VAL D 141 N LYS C 297
SHEET 4 AB2 5 LEU D 181 ILE D 183 -1 O ILE D 183 N VAL D 140
SHEET 5 AB2 5 ARG D 172 VAL D 174 -1 N PHE D 173 O TYR D 182
SHEET 1 AB3 4 VAL D 132 VAL D 134 0
SHEET 2 AB3 4 THR D 212 LEU D 216 1 O VAL D 215 N VAL D 134
SHEET 3 AB3 4 GLY D 192 SER D 200 -1 N GLY D 192 O LEU D 214
SHEET 4 AB3 4 LEU D 153 PHE D 159 -1 N ALA D 156 O VAL D 197
SHEET 1 AB4 4 VAL D 132 VAL D 134 0
SHEET 2 AB4 4 THR D 212 LEU D 216 1 O VAL D 215 N VAL D 134
SHEET 3 AB4 4 GLY D 192 SER D 200 -1 N GLY D 192 O LEU D 214
SHEET 4 AB4 4 VAL D 207 LEU D 208 -1 O VAL D 207 N VAL D 198
SHEET 1 AB5 4 TYR D 225 GLN D 232 0
SHEET 2 AB5 4 VAL D 245 ASN D 254 -1 O LEU D 252 N LYS D 228
SHEET 3 AB5 4 MET D 281 ILE D 284 -1 O ILE D 284 N VAL D 245
SHEET 4 AB5 4 LYS D 274 ARG D 276 -1 N ARG D 276 O MET D 281
SHEET 1 AB6 4 THR D 236 ALA D 239 0
SHEET 2 AB6 4 GLY D 304 TYR D 314 1 O ARG D 311 N LEU D 237
SHEET 3 AB6 4 GLY D 293 ASN D 301 -1 N TYR D 295 O GLY D 310
SHEET 4 AB6 4 GLN D 258 ARG D 263 -1 N ASN 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 2.04
SSBOND 3 CYS B 249 CYS B 297 1555 1555 2.01
SSBOND 4 CYS C 78 CYS C 261 1555 1555 2.04
SSBOND 5 CYS D 144 CYS D 196 1555 1555 2.04
SSBOND 6 CYS D 249 CYS D 297 1555 1555 2.02
CISPEP 1 SER A 84 PRO A 85 0 0.57
CISPEP 2 PRO A 259 PRO A 260 0 10.34
CISPEP 3 TYR B 162 PRO B 163 0 -5.01
CISPEP 4 ASN B 254 PRO B 255 0 2.15
CISPEP 5 SER C 84 PRO C 85 0 -1.05
CISPEP 6 PRO C 259 PRO C 260 0 8.60
CISPEP 7 TYR D 162 PRO D 163 0 7.12
CISPEP 8 ASN D 254 PRO D 255 0 -2.91
SITE 1 AC1 2 TRP A 116 PHE A 232
SITE 1 AC2 2 GLU C 230 PHE C 232
SITE 1 AC3 5 THR C 120 GLY C 121 LYS C 122 HIS C 227
SITE 2 AC3 5 THR C 290
SITE 1 AC4 3 THR C 120 LYS C 122 THR C 258
SITE 1 AC5 5 GLU D 177 PHE D 233 PRO D 234 ARG D 246
SITE 2 AC5 5 GLU D 248
CRYST1 74.138 90.526 147.448 90.00 90.00 90.00 P 21 21 2 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 0.013488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006782 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
