HEADER SIGNALING PROTEIN 03-JUN-16 5L7N
TITLE PLEXIN A1 EXTRACELLULAR FRAGMENT, DOMAINS 7-10 (IPT3-IPT6)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLEXIN-A1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PLEXIN-1;
COMPND 5 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: PLXNA1, KIAA4053;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293 S
KEYWDS IPT DOMAIN, SIGNALING PROTEIN, RECEPTOR, AXON GUIDANCE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KONG,B.J.C.JANSSEN,T.MALINAUSKAS,V.R.VANGOOR,C.H.COLES,R.KAUFMANN,
AUTHOR 2 T.NI,R.J.C.GILBERT,S.PADILLA-PARRA,R.J.PASTERKAMP,E.Y.JONES
REVDAT 3 29-JUL-20 5L7N 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 13-SEP-17 5L7N 1 REMARK
REVDAT 1 15-MAR-17 5L7N 0
JRNL AUTH Y.KONG,B.J.JANSSEN,T.MALINAUSKAS,V.R.VANGOOR,C.H.COLES,
JRNL AUTH 2 R.KAUFMANN,T.NI,R.J.GILBERT,S.PADILLA-PARRA,R.J.PASTERKAMP,
JRNL AUTH 3 E.Y.JONES
JRNL TITL STRUCTURAL BASIS FOR PLEXIN ACTIVATION AND REGULATION.
JRNL REF NEURON V. 91 548 2016
JRNL REFN ISSN 1097-4199
JRNL PMID 27397516
JRNL DOI 10.1016/J.NEURON.2016.06.018
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2283: ???)
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 20361
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1032
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 62.8256 - 4.2082 1.00 2893 147 0.1996 0.2043
REMARK 3 2 4.2082 - 3.3402 1.00 2779 148 0.2057 0.2398
REMARK 3 3 3.3402 - 2.9180 1.00 2764 141 0.2421 0.3177
REMARK 3 4 2.9180 - 2.6512 1.00 2722 163 0.2609 0.3642
REMARK 3 5 2.6512 - 2.4612 1.00 2732 144 0.2593 0.3142
REMARK 3 6 2.4612 - 2.3161 1.00 2721 152 0.2711 0.3357
REMARK 3 7 2.3161 - 2.2001 0.99 2718 137 0.3434 0.4021
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.400
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 : 0.002 2753
REMARK 3 ANGLE : 0.519 3752
REMARK 3 CHIRALITY : 0.046 437
REMARK 3 PLANARITY : 0.004 487
REMARK 3 DIHEDRAL : 14.874 1678
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 861 THROUGH 934 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3325 -23.8216 -12.0202
REMARK 3 T TENSOR
REMARK 3 T11: 0.4684 T22: 0.2773
REMARK 3 T33: 0.2977 T12: 0.0464
REMARK 3 T13: -0.0491 T23: 0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 4.7743 L22: 5.6834
REMARK 3 L33: 4.2252 L12: -1.5786
REMARK 3 L13: -0.4936 L23: 1.0935
REMARK 3 S TENSOR
REMARK 3 S11: -0.1342 S12: 0.1380 S13: -0.4432
REMARK 3 S21: -0.1215 S22: 0.0650 S23: 0.0874
REMARK 3 S31: 0.7671 S32: 0.3521 S33: 0.0810
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 935 THROUGH 1046 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7799 -2.4290 -18.7286
REMARK 3 T TENSOR
REMARK 3 T11: 0.2826 T22: 0.3031
REMARK 3 T33: 0.2813 T12: -0.0258
REMARK 3 T13: -0.0297 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.5426 L22: 6.0773
REMARK 3 L33: 3.7465 L12: -1.6500
REMARK 3 L13: 0.8514 L23: -3.5276
REMARK 3 S TENSOR
REMARK 3 S11: -0.0422 S12: 0.0143 S13: -0.0546
REMARK 3 S21: 0.0262 S22: 0.1396 S23: 0.2667
REMARK 3 S31: 0.0921 S32: 0.0776 S33: -0.1121
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1047 THROUGH 1145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1454 20.1874 -44.8883
REMARK 3 T TENSOR
REMARK 3 T11: 0.3774 T22: 0.2736
REMARK 3 T33: 0.2347 T12: 0.0023
REMARK 3 T13: -0.0909 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 4.5460 L22: 0.8769
REMARK 3 L33: 5.0265 L12: -0.6474
REMARK 3 L13: -4.0976 L23: 1.0782
REMARK 3 S TENSOR
REMARK 3 S11: 0.1079 S12: 0.0754 S13: 0.1230
REMARK 3 S21: -0.0524 S22: 0.0364 S23: 0.0136
REMARK 3 S31: -0.1438 S32: -0.1649 S33: -0.1495
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1146 THROUGH 1227 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5543 33.8572 -46.7681
REMARK 3 T TENSOR
REMARK 3 T11: 0.5485 T22: 0.3959
REMARK 3 T33: 0.7924 T12: -0.1056
REMARK 3 T13: 0.0419 T23: -0.2223
REMARK 3 L TENSOR
REMARK 3 L11: 4.0479 L22: 6.5067
REMARK 3 L33: 3.9481 L12: 4.6393
REMARK 3 L13: -0.7313 L23: 0.2076
REMARK 3 S TENSOR
REMARK 3 S11: 0.2905 S12: -0.3801 S13: 0.6570
REMARK 3 S21: 0.0170 S22: 0.2958 S23: -1.2092
REMARK 3 S31: -0.7924 S32: 0.7120 S33: -0.2201
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 5L7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000235.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-13
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 : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20394
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 62.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.82500
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: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) POLYETHYLENE GLYCOL 3,350,
REMARK 280 100MM BIS-TRIS PH 5.5 AND 200MM POTASSIUM SODIUM TARTRATE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 62.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 37.94000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.25500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 37.94000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.25500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 62.80000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 37.94000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 41.25500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 62.80000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 37.94000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 41.25500
REMARK 290 SMTRY3 8 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 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1521 LIES ON A SPECIAL POSITION.
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 GLU A 858
REMARK 465 THR A 859
REMARK 465 GLY A 860
REMARK 465 ASP A 941
REMARK 465 CYS A 942
REMARK 465 SER A 943
REMARK 465 LEU A 1153
REMARK 465 SER A 1154
REMARK 465 PRO A 1155
REMARK 465 THR A 1156
REMARK 465 GLY A 1157
REMARK 465 LEU A 1158
REMARK 465 LEU A 1159
REMARK 465 GLU A 1160
REMARK 465 LEU A 1161
REMARK 465 LYS A 1162
REMARK 465 PRO A 1163
REMARK 465 SER A 1164
REMARK 465 ASN A 1210
REMARK 465 LEU A 1211
REMARK 465 THR A 1212
REMARK 465 GLY A 1213
REMARK 465 GLN A 1214
REMARK 465 HIS A 1215
REMARK 465 LYS A 1216
REMARK 465 VAL A 1217
REMARK 465 PRO A 1228
REMARK 465 GLY A 1229
REMARK 465 MET A 1230
REMARK 465 LEU A 1231
REMARK 465 GLN A 1232
REMARK 465 VAL A 1233
REMARK 465 TYR A 1234
REMARK 465 SER A 1235
REMARK 465 ASP A 1236
REMARK 465 SER A 1237
REMARK 465 LEU A 1238
REMARK 465 LEU A 1239
REMARK 465 THR A 1240
REMARK 465 LEU A 1241
REMARK 465 GLY A 1242
REMARK 465 THR A 1243
REMARK 465 LYS A 1244
REMARK 465 HIS A 1245
REMARK 465 HIS A 1246
REMARK 465 HIS A 1247
REMARK 465 HIS A 1248
REMARK 465 HIS A 1249
REMARK 465 HIS A 1250
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 916 -42.01 -134.93
REMARK 500 SER A1000 108.11 -57.10
REMARK 500 ASN A1029 -122.50 56.93
REMARK 500 ASN A1035 102.11 -160.15
REMARK 500 GLU A1054 42.88 -88.86
REMARK 500 ASP A1129 -130.12 52.84
REMARK 500 SER A1200 -165.80 -108.83
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5L7N A 861 1241 UNP P70206 PLXA1_MOUSE 861 1241
SEQADV 5L7N GLU A 858 UNP P70206 EXPRESSION TAG
SEQADV 5L7N THR A 859 UNP P70206 EXPRESSION TAG
SEQADV 5L7N GLY A 860 UNP P70206 EXPRESSION TAG
SEQADV 5L7N GLY A 1242 UNP P70206 EXPRESSION TAG
SEQADV 5L7N THR A 1243 UNP P70206 EXPRESSION TAG
SEQADV 5L7N LYS A 1244 UNP P70206 EXPRESSION TAG
SEQADV 5L7N HIS A 1245 UNP P70206 EXPRESSION TAG
SEQADV 5L7N HIS A 1246 UNP P70206 EXPRESSION TAG
SEQADV 5L7N HIS A 1247 UNP P70206 EXPRESSION TAG
SEQADV 5L7N HIS A 1248 UNP P70206 EXPRESSION TAG
SEQADV 5L7N HIS A 1249 UNP P70206 EXPRESSION TAG
SEQADV 5L7N HIS A 1250 UNP P70206 EXPRESSION TAG
SEQRES 1 A 393 GLU THR GLY ASP PRO LYS ILE LEU LYS LEU SER PRO GLU
SEQRES 2 A 393 THR GLY PRO ARG GLN GLY GLY THR ARG LEU THR ILE THR
SEQRES 3 A 393 GLY GLU ASN LEU GLY LEU ARG PHE GLU ASP VAL ARG LEU
SEQRES 4 A 393 GLY VAL HIS VAL GLY LYS VAL LEU CYS SER PRO VAL GLU
SEQRES 5 A 393 SER GLU TYR ILE SER ALA GLU GLN ILE VAL CYS GLU ILE
SEQRES 6 A 393 GLY ASP ALA SER THR LEU ARG ALA HIS ASP ALA LEU VAL
SEQRES 7 A 393 GLU VAL CYS VAL ARG ASP CYS SER LEU HIS TYR ARG ALA
SEQRES 8 A 393 LEU SER PRO LYS ARG PHE THR PHE VAL THR PRO THR PHE
SEQRES 9 A 393 TYR ARG VAL SER PRO SER ARG GLY PRO LEU SER GLY GLY
SEQRES 10 A 393 THR TRP ILE GLY ILE GLU GLY SER HIS LEU ASN ALA GLY
SEQRES 11 A 393 SER ASP VAL ALA VAL SER ILE GLY GLY ARG PRO CYS SER
SEQRES 12 A 393 PHE SER TRP ARG ASN SER ARG GLU ILE ARG CYS LEU THR
SEQRES 13 A 393 PRO PRO GLY HIS THR PRO GLY SER ALA PRO ILE VAL ILE
SEQRES 14 A 393 ASN ILE ASN ARG ALA GLN LEU SER ASN PRO GLU VAL LYS
SEQRES 15 A 393 TYR ASN TYR THR GLU ASP PRO THR ILE LEU ARG ILE ASP
SEQRES 16 A 393 PRO GLU TRP SER ILE ASN SER GLY GLY THR LEU LEU THR
SEQRES 17 A 393 VAL THR GLY THR ASN LEU ALA THR VAL ARG GLU PRO ARG
SEQRES 18 A 393 ILE ARG ALA LYS TYR GLY GLY ILE GLU ARG GLU ASN SER
SEQRES 19 A 393 CYS MET VAL TYR ASN ASP THR THR MET VAL CYS ARG ALA
SEQRES 20 A 393 PRO SER ILE ASP ASN PRO LYS ARG SER PRO PRO GLU LEU
SEQRES 21 A 393 GLY GLU ARG PRO ASP GLU ILE GLY PHE ILE MET ASP ASN
SEQRES 22 A 393 VAL ARG THR LEU LEU VAL LEU ASN SER SER SER PHE LEU
SEQRES 23 A 393 TYR TYR PRO ASP PRO VAL LEU GLU PRO LEU SER PRO THR
SEQRES 24 A 393 GLY LEU LEU GLU LEU LYS PRO SER SER PRO LEU ILE LEU
SEQRES 25 A 393 LYS GLY ARG ASN LEU LEU PRO PRO ALA PRO GLY ASN SER
SEQRES 26 A 393 ARG LEU ASN TYR THR VAL LEU ILE GLY SER THR PRO CYS
SEQRES 27 A 393 ILE LEU THR VAL SER GLU THR GLN LEU LEU CYS GLU ALA
SEQRES 28 A 393 PRO ASN LEU THR GLY GLN HIS LYS VAL THR VAL ARG ALA
SEQRES 29 A 393 GLY GLY PHE GLU PHE SER PRO GLY MET LEU GLN VAL TYR
SEQRES 30 A 393 SER ASP SER LEU LEU THR LEU GLY THR LYS HIS HIS HIS
SEQRES 31 A 393 HIS HIS HIS
HET NAG A1301 14
HET NAG A1302 14
HET NAG A1303 14
HET EDO A1304 4
HET PEG A1305 7
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 NAG 3(C8 H15 N O6)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 PEG C4 H10 O3
FORMUL 7 HOH *130(H2 O)
HELIX 1 AA1 ARG A 890 VAL A 894 5 5
HELIX 2 AA2 GLU A 909 TYR A 912 5 4
HELIX 3 AA3 ASN A 1070 VAL A 1074 5 5
HELIX 4 AA4 VAL A 1131 LEU A 1135 5 5
SHEET 1 AA1 7 LYS A 863 SER A 868 0
SHEET 2 AA1 7 ARG A 879 LEU A 887 -1 O GLU A 885 N LYS A 863
SHEET 3 AA1 7 ALA A 915 ILE A 922 -1 O GLU A 916 N GLY A 884
SHEET 4 AA1 7 VAL A 903 PRO A 907 -1 N SER A 906 O GLU A 921
SHEET 5 AA1 7 VAL A 898 VAL A 900 -1 N VAL A 900 O VAL A 903
SHEET 6 AA1 7 VAL A 935 CYS A 938 -1 O GLU A 936 N HIS A 899
SHEET 7 AA1 7 ARG A 947 LEU A 949 -1 O ALA A 948 N VAL A 937
SHEET 1 AA2 3 THR A 871 PRO A 873 0
SHEET 2 AA2 3 PHE A 954 VAL A 957 1 O VAL A 957 N GLY A 872
SHEET 3 AA2 3 ASP A 932 ALA A 933 -1 N ALA A 933 O PHE A 954
SHEET 1 AA3 8 THR A 960 SER A 965 0
SHEET 2 AA3 8 TRP A 976 SER A 982 -1 O GLU A 980 N ARG A 963
SHEET 3 AA3 8 GLU A1008 LEU A1012 -1 O CYS A1011 N ILE A 977
SHEET 4 AA3 8 ARG A 997 ARG A1004 -1 N SER A1002 O ARG A1010
SHEET 5 AA3 8 ALA A 991 ILE A 994 -1 N ILE A 994 O ARG A 997
SHEET 6 AA3 8 GLY A1020 ILE A1028 -1 O VAL A1025 N SER A 993
SHEET 7 AA3 8 ALA A1031 THR A1043 -1 O TYR A1042 N GLY A1020
SHEET 8 AA3 8 ARG A 968 PRO A 970 1 N GLY A 969 O THR A1043
SHEET 1 AA4 6 THR A1047 ASP A1052 0
SHEET 2 AA4 6 LEU A1063 THR A1069 -1 O THR A1065 N ASP A1052
SHEET 3 AA4 6 THR A1099 ARG A1103 -1 O CYS A1102 N LEU A1064
SHEET 4 AA4 6 ILE A1086 ASN A1096 -1 N MET A1093 O VAL A1101
SHEET 5 AA4 6 ARG A1078 TYR A1083 -1 N ILE A1079 O ASN A1090
SHEET 6 AA4 6 GLU A1123 ILE A1127 -1 O GLY A1125 N ARG A1080
SHEET 1 AA5 2 TRP A1055 ILE A1057 0
SHEET 2 AA5 2 LEU A1143 TYR A1145 1 O TYR A1145 N SER A1056
SHEET 1 AA6 3 VAL A1149 LEU A1150 0
SHEET 2 AA6 3 LEU A1167 ARG A1172 -1 O ARG A1172 N VAL A1149
SHEET 3 AA6 3 GLN A1203 CYS A1206 -1 O LEU A1204 N LEU A1169
SHEET 1 AA7 3 THR A1187 VAL A1188 0
SHEET 2 AA7 3 VAL A1219 ALA A1221 -1 O ARG A1220 N THR A1187
SHEET 3 AA7 3 PHE A1224 PHE A1226 -1 O PHE A1224 N ALA A1221
SSBOND 1 CYS A 905 CYS A 920 1555 1555 2.03
SSBOND 2 CYS A 999 CYS A 1011 1555 1555 2.04
SSBOND 3 CYS A 1092 CYS A 1102 1555 1555 2.03
SSBOND 4 CYS A 1195 CYS A 1206 1555 1555 2.03
LINK ND2 ASN A1041 C1 NAG A1303 1555 1555 1.44
LINK ND2 ASN A1096 C1 NAG A1301 1555 1555 1.44
LINK ND2 ASN A1185 C1 NAG A1302 1555 1555 1.44
CISPEP 1 SER A 868 PRO A 869 0 0.77
CISPEP 2 SER A 965 PRO A 966 0 -2.43
CISPEP 3 ASP A 1052 PRO A 1053 0 -1.30
CRYST1 75.880 82.510 125.600 90.00 90.00 90.00 C 2 2 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 0.013179 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012120 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007962 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
