HEADER SIGNALING PROTEIN 05-JUN-16 5KC6
TITLE CRYSTAL STRUCTURE OF CBLN1 (VAL55-GLY58 DELETION MUTANT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEREBELLIN-1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PRECEREBELLIN;
COMPND 5 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: CBLN1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PHLSEC
KEYWDS CEREBELLIN, NEUROTRANSMISSION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ELEGHEERT,J.E.CLAY,A.R.ARICESCU
REVDAT 5 10-JAN-24 5KC6 1 HETSYN
REVDAT 4 29-JUL-20 5KC6 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 18-DEC-19 5KC6 1 REMARK
REVDAT 2 03-AUG-16 5KC6 1 TITLE
REVDAT 1 27-JUL-16 5KC6 0
JRNL AUTH J.ELEGHEERT,W.KAKEGAWA,J.E.CLAY,N.F.SHANKS,E.BEHIELS,
JRNL AUTH 2 K.MATSUDA,K.KOHDA,E.MIURA,M.ROSSMANN,N.MITAKIDIS,
JRNL AUTH 3 J.MOTOHASHI,V.T.CHANG,C.SIEBOLD,I.H.GREGER,T.NAKAGAWA,
JRNL AUTH 4 M.YUZAKI,A.R.ARICESCU
JRNL TITL STRUCTURAL BASIS FOR INTEGRATION OF GLUD RECEPTORS WITHIN
JRNL TITL 2 SYNAPTIC ORGANIZER COMPLEXES.
JRNL REF SCIENCE V. 353 295 2016
JRNL REFN ESSN 1095-9203
JRNL PMID 27418511
JRNL DOI 10.1126/SCIENCE.AAE0104
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1772
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 73.2
REMARK 3 NUMBER OF REFLECTIONS : 14561
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) : 0.188
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 708
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 68.7908 - 4.7884 0.99 3925 192 0.1798 0.2187
REMARK 3 2 4.7884 - 3.8008 0.99 3760 185 0.1631 0.2036
REMARK 3 3 3.8008 - 3.3203 0.83 3082 176 0.2190 0.2539
REMARK 3 4 3.3203 - 3.0167 0.55 2075 107 0.2422 0.2797
REMARK 3 5 3.0167 - 2.8005 0.27 1011 48 0.2387 0.2220
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 1.00
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.10
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 : 0.003 3451
REMARK 3 ANGLE : 0.722 4666
REMARK 3 CHIRALITY : 0.031 507
REMARK 3 PLANARITY : 0.002 600
REMARK 3 DIHEDRAL : 13.202 1244
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 59:195)
REMARK 3 ORIGIN FOR THE GROUP (A): 70.0901 34.2115 16.3107
REMARK 3 T TENSOR
REMARK 3 T11: 0.2536 T22: 0.4491
REMARK 3 T33: 0.3266 T12: -0.0557
REMARK 3 T13: 0.0416 T23: 0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 2.8648 L22: 2.2085
REMARK 3 L33: 2.9376 L12: -0.3874
REMARK 3 L13: 0.0827 L23: -0.0422
REMARK 3 S TENSOR
REMARK 3 S11: -0.1598 S12: -0.7242 S13: -0.4212
REMARK 3 S21: 0.0763 S22: 0.0742 S23: 0.2506
REMARK 3 S31: 0.0351 S32: -0.4344 S33: 0.0850
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESSEQ 59:202)
REMARK 3 ORIGIN FOR THE GROUP (A): 92.6351 39.2103 11.1711
REMARK 3 T TENSOR
REMARK 3 T11: 0.2607 T22: 0.2986
REMARK 3 T33: 0.1908 T12: 0.0545
REMARK 3 T13: -0.0295 T23: 0.0479
REMARK 3 L TENSOR
REMARK 3 L11: 4.4245 L22: 2.5369
REMARK 3 L33: 3.1198 L12: 0.6674
REMARK 3 L13: -0.2355 L23: 0.5682
REMARK 3 S TENSOR
REMARK 3 S11: -0.1842 S12: -0.4570 S13: -0.0292
REMARK 3 S21: -0.0835 S22: 0.1518 S23: -0.0626
REMARK 3 S31: -0.1888 S32: 0.1864 S33: 0.0343
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN C AND RESSEQ 59:194)
REMARK 3 ORIGIN FOR THE GROUP (A): 76.9018 40.0466 -5.2777
REMARK 3 T TENSOR
REMARK 3 T11: 0.2745 T22: 0.2920
REMARK 3 T33: 0.2424 T12: -0.0242
REMARK 3 T13: 0.0028 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 3.5721 L22: 2.3326
REMARK 3 L33: 2.5196 L12: -1.0460
REMARK 3 L13: 0.3216 L23: -0.0325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: 0.4311 S13: 0.0950
REMARK 3 S21: -0.1173 S22: 0.1785 S23: -0.1803
REMARK 3 S31: 0.0648 S32: -0.1133 S33: -0.1028
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 5KC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000221708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-11
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 : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97630
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14603
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 85.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.4
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 19.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
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: 5KC5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% (V/V) GLYCEROL, 8.5% (V/V)
REMARK 280 ISOPROPANOL, 17% (W/V) POLYETHYLENE GLYCOL 4000, 0.085 M
REMARK 280 NA.HEPES PH 7.5 AND 0.02 M SODIUM BROMIDE, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 58.21500
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 58.21500
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 39.79000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 85.22500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.79000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 85.22500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.21500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.79000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 85.22500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.21500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.79000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 85.22500
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR
REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C2).
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLU A 25
REMARK 465 THR A 26
REMARK 465 GLY A 27
REMARK 465 GLU A 28
REMARK 465 THR A 29
REMARK 465 GLU A 30
REMARK 465 PRO A 31
REMARK 465 ILE A 32
REMARK 465 VAL A 33
REMARK 465 LEU A 34
REMARK 465 GLU A 35
REMARK 465 GLY A 36
REMARK 465 LYS A 37
REMARK 465 CYS A 38
REMARK 465 LEU A 39
REMARK 465 VAL A 40
REMARK 465 VAL A 41
REMARK 465 CYS A 42
REMARK 465 ASP A 43
REMARK 465 SER A 44
REMARK 465 ASN A 45
REMARK 465 PRO A 46
REMARK 465 THR A 47
REMARK 465 SER A 48
REMARK 465 ASP A 49
REMARK 465 PRO A 50
REMARK 465 THR A 51
REMARK 465 GLY A 52
REMARK 465 THR A 53
REMARK 465 ALA A 54
REMARK 465 LEU A 55
REMARK 465 GLY A 56
REMARK 465 ILE A 57
REMARK 465 SER A 58
REMARK 465 LYS A 196
REMARK 465 HIS A 197
REMARK 465 HIS A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
REMARK 465 GLU B 25
REMARK 465 THR B 26
REMARK 465 GLY B 27
REMARK 465 GLU B 28
REMARK 465 THR B 29
REMARK 465 GLU B 30
REMARK 465 PRO B 31
REMARK 465 ILE B 32
REMARK 465 VAL B 33
REMARK 465 LEU B 34
REMARK 465 GLU B 35
REMARK 465 GLY B 36
REMARK 465 LYS B 37
REMARK 465 CYS B 38
REMARK 465 LEU B 39
REMARK 465 VAL B 40
REMARK 465 VAL B 41
REMARK 465 CYS B 42
REMARK 465 ASP B 43
REMARK 465 SER B 44
REMARK 465 ASN B 45
REMARK 465 PRO B 46
REMARK 465 THR B 47
REMARK 465 SER B 48
REMARK 465 ASP B 49
REMARK 465 PRO B 50
REMARK 465 THR B 51
REMARK 465 GLY B 52
REMARK 465 THR B 53
REMARK 465 ALA B 54
REMARK 465 LEU B 55
REMARK 465 GLY B 56
REMARK 465 ILE B 57
REMARK 465 SER B 58
REMARK 465 GLU C 25
REMARK 465 THR C 26
REMARK 465 GLY C 27
REMARK 465 GLU C 28
REMARK 465 THR C 29
REMARK 465 GLU C 30
REMARK 465 PRO C 31
REMARK 465 ILE C 32
REMARK 465 VAL C 33
REMARK 465 LEU C 34
REMARK 465 GLU C 35
REMARK 465 GLY C 36
REMARK 465 LYS C 37
REMARK 465 CYS C 38
REMARK 465 LEU C 39
REMARK 465 VAL C 40
REMARK 465 VAL C 41
REMARK 465 CYS C 42
REMARK 465 ASP C 43
REMARK 465 SER C 44
REMARK 465 ASN C 45
REMARK 465 PRO C 46
REMARK 465 THR C 47
REMARK 465 SER C 48
REMARK 465 ASP C 49
REMARK 465 PRO C 50
REMARK 465 THR C 51
REMARK 465 GLY C 52
REMARK 465 THR C 53
REMARK 465 ALA C 54
REMARK 465 LEU C 55
REMARK 465 GLY C 56
REMARK 465 ILE C 57
REMARK 465 SER C 58
REMARK 465 THR C 195
REMARK 465 LYS C 196
REMARK 465 HIS C 197
REMARK 465 HIS C 198
REMARK 465 HIS C 199
REMARK 465 HIS C 200
REMARK 465 HIS C 201
REMARK 465 HIS C 202
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 NZ LYS A 120 O GLN A 125 2.11
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 O LYS B 163 NH2 ARG C 173 8555 2.18
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 ASN A 92 60.44 -160.09
REMARK 500 ASN B 92 60.24 -160.20
REMARK 500 ASN C 92 60.29 -159.37
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5KC6 A 28 193 UNP P23435 CBLN1_HUMAN 24 193
DBREF 5KC6 B 28 193 UNP P23435 CBLN1_HUMAN 24 193
DBREF 5KC6 C 28 193 UNP P23435 CBLN1_HUMAN 24 193
SEQADV 5KC6 GLU A 25 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 THR A 26 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 GLY A 27 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 A UNP P23435 VAL 55 DELETION
SEQADV 5KC6 A UNP P23435 ARG 56 DELETION
SEQADV 5KC6 A UNP P23435 SER 57 DELETION
SEQADV 5KC6 A UNP P23435 GLY 58 DELETION
SEQADV 5KC6 GLY A 194 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 THR A 195 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 LYS A 196 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS A 197 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS A 198 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS A 199 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS A 200 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS A 201 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS A 202 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 GLU B 25 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 THR B 26 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 GLY B 27 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 B UNP P23435 VAL 55 DELETION
SEQADV 5KC6 B UNP P23435 ARG 56 DELETION
SEQADV 5KC6 B UNP P23435 SER 57 DELETION
SEQADV 5KC6 B UNP P23435 GLY 58 DELETION
SEQADV 5KC6 GLY B 194 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 THR B 195 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 LYS B 196 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS B 197 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS B 198 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS B 199 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS B 200 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS B 201 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS B 202 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 GLU C 25 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 THR C 26 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 GLY C 27 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 C UNP P23435 VAL 55 DELETION
SEQADV 5KC6 C UNP P23435 ARG 56 DELETION
SEQADV 5KC6 C UNP P23435 SER 57 DELETION
SEQADV 5KC6 C UNP P23435 GLY 58 DELETION
SEQADV 5KC6 GLY C 194 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 THR C 195 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 LYS C 196 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS C 197 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS C 198 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS C 199 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS C 200 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS C 201 UNP P23435 EXPRESSION TAG
SEQADV 5KC6 HIS C 202 UNP P23435 EXPRESSION TAG
SEQRES 1 A 178 GLU THR GLY GLU THR GLU PRO ILE VAL LEU GLU GLY LYS
SEQRES 2 A 178 CYS LEU VAL VAL CYS ASP SER ASN PRO THR SER ASP PRO
SEQRES 3 A 178 THR GLY THR ALA LEU GLY ILE SER SER ALA LYS VAL ALA
SEQRES 4 A 178 PHE SER ALA ILE ARG SER THR ASN HIS GLU PRO SER GLU
SEQRES 5 A 178 MET SER ASN ARG THR MET ILE ILE TYR PHE ASP GLN VAL
SEQRES 6 A 178 LEU VAL ASN ILE GLY ASN ASN PHE ASP SER GLU ARG SER
SEQRES 7 A 178 THR PHE ILE ALA PRO ARG LYS GLY ILE TYR SER PHE ASN
SEQRES 8 A 178 PHE HIS VAL VAL LYS VAL TYR ASN ARG GLN THR ILE GLN
SEQRES 9 A 178 VAL SER LEU MET LEU ASN GLY TRP PRO VAL ILE SER ALA
SEQRES 10 A 178 PHE ALA GLY ASP GLN ASP VAL THR ARG GLU ALA ALA SER
SEQRES 11 A 178 ASN GLY VAL LEU ILE GLN MET GLU LYS GLY ASP ARG ALA
SEQRES 12 A 178 TYR LEU LYS LEU GLU ARG GLY ASN LEU MET GLY GLY TRP
SEQRES 13 A 178 LYS TYR SER THR PHE SER GLY PHE LEU VAL PHE PRO LEU
SEQRES 14 A 178 GLY THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 178 GLU THR GLY GLU THR GLU PRO ILE VAL LEU GLU GLY LYS
SEQRES 2 B 178 CYS LEU VAL VAL CYS ASP SER ASN PRO THR SER ASP PRO
SEQRES 3 B 178 THR GLY THR ALA LEU GLY ILE SER SER ALA LYS VAL ALA
SEQRES 4 B 178 PHE SER ALA ILE ARG SER THR ASN HIS GLU PRO SER GLU
SEQRES 5 B 178 MET SER ASN ARG THR MET ILE ILE TYR PHE ASP GLN VAL
SEQRES 6 B 178 LEU VAL ASN ILE GLY ASN ASN PHE ASP SER GLU ARG SER
SEQRES 7 B 178 THR PHE ILE ALA PRO ARG LYS GLY ILE TYR SER PHE ASN
SEQRES 8 B 178 PHE HIS VAL VAL LYS VAL TYR ASN ARG GLN THR ILE GLN
SEQRES 9 B 178 VAL SER LEU MET LEU ASN GLY TRP PRO VAL ILE SER ALA
SEQRES 10 B 178 PHE ALA GLY ASP GLN ASP VAL THR ARG GLU ALA ALA SER
SEQRES 11 B 178 ASN GLY VAL LEU ILE GLN MET GLU LYS GLY ASP ARG ALA
SEQRES 12 B 178 TYR LEU LYS LEU GLU ARG GLY ASN LEU MET GLY GLY TRP
SEQRES 13 B 178 LYS TYR SER THR PHE SER GLY PHE LEU VAL PHE PRO LEU
SEQRES 14 B 178 GLY THR LYS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 178 GLU THR GLY GLU THR GLU PRO ILE VAL LEU GLU GLY LYS
SEQRES 2 C 178 CYS LEU VAL VAL CYS ASP SER ASN PRO THR SER ASP PRO
SEQRES 3 C 178 THR GLY THR ALA LEU GLY ILE SER SER ALA LYS VAL ALA
SEQRES 4 C 178 PHE SER ALA ILE ARG SER THR ASN HIS GLU PRO SER GLU
SEQRES 5 C 178 MET SER ASN ARG THR MET ILE ILE TYR PHE ASP GLN VAL
SEQRES 6 C 178 LEU VAL ASN ILE GLY ASN ASN PHE ASP SER GLU ARG SER
SEQRES 7 C 178 THR PHE ILE ALA PRO ARG LYS GLY ILE TYR SER PHE ASN
SEQRES 8 C 178 PHE HIS VAL VAL LYS VAL TYR ASN ARG GLN THR ILE GLN
SEQRES 9 C 178 VAL SER LEU MET LEU ASN GLY TRP PRO VAL ILE SER ALA
SEQRES 10 C 178 PHE ALA GLY ASP GLN ASP VAL THR ARG GLU ALA ALA SER
SEQRES 11 C 178 ASN GLY VAL LEU ILE GLN MET GLU LYS GLY ASP ARG ALA
SEQRES 12 C 178 TYR LEU LYS LEU GLU ARG GLY ASN LEU MET GLY GLY TRP
SEQRES 13 C 178 LYS TYR SER THR PHE SER GLY PHE LEU VAL PHE PRO LEU
SEQRES 14 C 178 GLY THR LYS HIS HIS HIS HIS HIS HIS
HET NAG A 301 14
HET NAG B 301 14
HET NAG C 301 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 4 NAG 3(C8 H15 N O6)
HELIX 1 AA1 SER A 75 MET A 82 1 8
HELIX 2 AA2 SER B 75 MET B 82 1 8
HELIX 3 AA3 SER C 75 MET C 82 1 8
SHEET 1 AA1 5 GLN A 88 ILE A 93 0
SHEET 2 AA1 5 ALA A 63 ILE A 67 -1 N ILE A 67 O GLN A 88
SHEET 3 AA1 5 THR A 184 PRO A 192 -1 O GLY A 187 N PHE A 64
SHEET 4 AA1 5 GLY A 110 LYS A 120 -1 N HIS A 117 O THR A 184
SHEET 5 AA1 5 GLU A 151 MET A 161 -1 O ILE A 159 N TYR A 112
SHEET 1 AA2 5 PHE A 97 ASP A 98 0
SHEET 2 AA2 5 THR A 103 ILE A 105 -1 O THR A 103 N ASP A 98
SHEET 3 AA2 5 ARG A 166 ARG A 173 -1 O ALA A 167 N PHE A 104
SHEET 4 AA2 5 ILE A 127 LEU A 133 -1 N MET A 132 O TYR A 168
SHEET 5 AA2 5 TRP A 136 ALA A 143 -1 O TRP A 136 N LEU A 133
SHEET 1 AA3 5 GLN B 88 ILE B 93 0
SHEET 2 AA3 5 ALA B 63 ILE B 67 -1 N ILE B 67 O GLN B 88
SHEET 3 AA3 5 THR B 184 PRO B 192 -1 O GLY B 187 N PHE B 64
SHEET 4 AA3 5 GLY B 110 LYS B 120 -1 N HIS B 117 O THR B 184
SHEET 5 AA3 5 GLU B 151 MET B 161 -1 O ILE B 159 N TYR B 112
SHEET 1 AA4 5 PHE B 97 ASP B 98 0
SHEET 2 AA4 5 THR B 103 ILE B 105 -1 O THR B 103 N ASP B 98
SHEET 3 AA4 5 ARG B 166 ARG B 173 -1 O ALA B 167 N PHE B 104
SHEET 4 AA4 5 ILE B 127 LEU B 133 -1 N MET B 132 O TYR B 168
SHEET 5 AA4 5 TRP B 136 ALA B 143 -1 O TRP B 136 N LEU B 133
SHEET 1 AA5 5 GLN C 88 ILE C 93 0
SHEET 2 AA5 5 ALA C 63 ILE C 67 -1 N ILE C 67 O GLN C 88
SHEET 3 AA5 5 THR C 184 PRO C 192 -1 O PHE C 185 N ALA C 66
SHEET 4 AA5 5 GLY C 110 LYS C 120 -1 N SER C 113 O PHE C 188
SHEET 5 AA5 5 GLU C 151 MET C 161 -1 O ILE C 159 N TYR C 112
SHEET 1 AA6 5 PHE C 97 ASP C 98 0
SHEET 2 AA6 5 THR C 103 ILE C 105 -1 O THR C 103 N ASP C 98
SHEET 3 AA6 5 ARG C 166 ARG C 173 -1 O ALA C 167 N PHE C 104
SHEET 4 AA6 5 ILE C 127 LEU C 133 -1 N MET C 132 O TYR C 168
SHEET 5 AA6 5 TRP C 136 ALA C 143 -1 O TRP C 136 N LEU C 133
LINK ND2 ASN A 79 C1 NAG A 301 1555 1555 1.43
LINK ND2 ASN B 79 C1 NAG B 301 1555 1555 1.44
LINK ND2 ASN C 79 C1 NAG C 301 1555 1555 1.44
CRYST1 79.580 170.450 116.430 90.00 90.00 90.00 C 2 2 21 24
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 0.012566 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005867 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008589 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
