HEADER SIGNALING PROTEIN 14-DEC-15 5FBH
TITLE CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN CALCIUM SENSING
TITLE 2 RECEPTOR WITH BOUND GD3+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXTRACELLULAR CALCIUM-SENSING RECEPTOR;
COMPND 3 CHAIN: B, A;
COMPND 4 FRAGMENT: UNP RESIDUES 20-541;
COMPND 5 SYNONYM: CASR,PARATHYROID CELL CALCIUM-SENSING RECEPTOR 1,PCAR1;
COMPND 6 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: CASR, GPRC2A, PCAR1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS MEMBRANE PROTEIN, G-PROTEIN COUPLED RECEPTOR, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ZHANG,C.ZHANG,C.L.MILLER,J.ZOU,K.W.MOREMEN,E.M.BROWN,J.J.YANG,J.HU
REVDAT 3 29-JUL-20 5FBH 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 20-JUL-16 5FBH 1 JRNL
REVDAT 1 22-JUN-16 5FBH 0
JRNL AUTH C.ZHANG,T.ZHANG,J.ZOU,C.L.MILLER,R.GORKHALI,J.Y.YANG,
JRNL AUTH 2 A.SCHILMILLER,S.WANG,K.HUANG,E.M.BROWN,K.W.MOREMEN,J.HU,
JRNL AUTH 3 J.J.YANG
JRNL TITL STRUCTURAL BASIS FOR REGULATION OF HUMAN CALCIUM-SENSING
JRNL TITL 2 RECEPTOR BY MAGNESIUM IONS AND AN UNEXPECTED TRYPTOPHAN
JRNL TITL 3 DERIVATIVE CO-AGONIST.
JRNL REF SCI ADV V. 2 00241 2016
JRNL REFN ESSN 2375-2548
JRNL PMID 27386547
JRNL DOI 10.1126/SCIADV.1600241
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 33039
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1733
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1994
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.3430
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7232
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 145
REMARK 3 SOLVENT ATOMS : 17
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : 0.88000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.741
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.309
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.233
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.524
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7577 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6857 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10324 ; 1.578 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15627 ; 0.913 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 936 ; 6.396 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 333 ;32.835 ;23.814
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1099 ;17.149 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;17.986 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1160 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8671 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1830 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3766 ; 4.619 ; 6.528
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3766 ; 4.618 ; 6.528
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4694 ; 6.859 ; 9.788
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 4
REMARK 4 5FBH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-15
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 : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.6985
REMARK 200 MONOCHROMATOR : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34777
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.77200
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: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 200 MM MGCL2, 10 MM
REMARK 280 CACL2 AND 100 MM TRIS-HCL, 0.5 MM GDCL3, PH 7.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 86.05350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.55300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 86.05350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.55300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: 7350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 MET B -26
REMARK 465 ARG B -25
REMARK 465 LEU B -24
REMARK 465 LEU B -23
REMARK 465 THR B -22
REMARK 465 ALA B -21
REMARK 465 LEU B -20
REMARK 465 PHE B -19
REMARK 465 ALA B -18
REMARK 465 TYR B -17
REMARK 465 PHE B -16
REMARK 465 ILE B -15
REMARK 465 VAL B -14
REMARK 465 ALA B -13
REMARK 465 LEU B -12
REMARK 465 ILE B -11
REMARK 465 LEU B -10
REMARK 465 ALA B -9
REMARK 465 PHE B -8
REMARK 465 SER B -7
REMARK 465 VAL B -6
REMARK 465 SER B -5
REMARK 465 ALA B -4
REMARK 465 LYS B -3
REMARK 465 SER B -2
REMARK 465 MET B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 ALA B 9
REMARK 465 TRP B 10
REMARK 465 SER B 11
REMARK 465 HIS B 12
REMARK 465 PRO B 13
REMARK 465 GLN B 14
REMARK 465 PHE B 15
REMARK 465 GLU B 16
REMARK 465 LYS B 17
REMARK 465 GLU B 18
REMARK 465 PHE B 19
REMARK 465 TYR B 20
REMARK 465 SER B 122
REMARK 465 LEU B 123
REMARK 465 ASN B 124
REMARK 465 LEU B 125
REMARK 465 ASP B 126
REMARK 465 GLU B 127
REMARK 465 PHE B 128
REMARK 465 CYS B 129
REMARK 465 ASN B 130
REMARK 465 CYS B 131
REMARK 465 SER B 132
REMARK 465 GLU B 133
REMARK 465 HIS B 134
REMARK 465 ILE B 135
REMARK 465 PRO B 136
REMARK 465 GLU B 362
REMARK 465 GLY B 363
REMARK 465 ALA B 364
REMARK 465 LYS B 365
REMARK 465 GLY B 366
REMARK 465 PRO B 367
REMARK 465 LEU B 368
REMARK 465 PRO B 369
REMARK 465 VAL B 370
REMARK 465 ASP B 371
REMARK 465 THR B 372
REMARK 465 PHE B 373
REMARK 465 LEU B 374
REMARK 465 ARG B 375
REMARK 465 GLY B 376
REMARK 465 HIS B 377
REMARK 465 GLU B 378
REMARK 465 GLU B 379
REMARK 465 SER B 380
REMARK 465 GLY B 381
REMARK 465 ASP B 382
REMARK 465 ARG B 383
REMARK 465 PHE B 384
REMARK 465 SER B 385
REMARK 465 ASN B 386
REMARK 465 SER B 387
REMARK 465 SER B 388
REMARK 465 THR B 389
REMARK 465 ALA B 390
REMARK 465 ARG B 535
REMARK 465 GLU B 536
REMARK 465 VAL B 537
REMARK 465 PRO B 538
REMARK 465 PHE B 539
REMARK 465 SER B 540
REMARK 465 ASN B 541
REMARK 465 MET A -26
REMARK 465 ARG A -25
REMARK 465 LEU A -24
REMARK 465 LEU A -23
REMARK 465 THR A -22
REMARK 465 ALA A -21
REMARK 465 LEU A -20
REMARK 465 PHE A -19
REMARK 465 ALA A -18
REMARK 465 TYR A -17
REMARK 465 PHE A -16
REMARK 465 ILE A -15
REMARK 465 VAL A -14
REMARK 465 ALA A -13
REMARK 465 LEU A -12
REMARK 465 ILE A -11
REMARK 465 LEU A -10
REMARK 465 ALA A -9
REMARK 465 PHE A -8
REMARK 465 SER A -7
REMARK 465 VAL A -6
REMARK 465 SER A -5
REMARK 465 ALA A -4
REMARK 465 LYS A -3
REMARK 465 SER A -2
REMARK 465 MET A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 TRP A 10
REMARK 465 SER A 11
REMARK 465 HIS A 12
REMARK 465 PRO A 13
REMARK 465 GLN A 14
REMARK 465 PHE A 15
REMARK 465 GLU A 16
REMARK 465 LYS A 17
REMARK 465 GLU A 18
REMARK 465 PHE A 19
REMARK 465 TYR A 20
REMARK 465 GLY A 21
REMARK 465 SER A 122
REMARK 465 LEU A 123
REMARK 465 ASN A 124
REMARK 465 LEU A 125
REMARK 465 ASP A 126
REMARK 465 GLU A 127
REMARK 465 PHE A 128
REMARK 465 CYS A 129
REMARK 465 ASN A 130
REMARK 465 CYS A 131
REMARK 465 SER A 132
REMARK 465 GLU A 133
REMARK 465 HIS A 134
REMARK 465 ILE A 135
REMARK 465 PRO A 136
REMARK 465 GLU A 362
REMARK 465 GLY A 363
REMARK 465 ALA A 364
REMARK 465 LYS A 365
REMARK 465 GLY A 366
REMARK 465 PRO A 367
REMARK 465 LEU A 368
REMARK 465 PRO A 369
REMARK 465 VAL A 370
REMARK 465 ASP A 371
REMARK 465 THR A 372
REMARK 465 PHE A 373
REMARK 465 LEU A 374
REMARK 465 ARG A 375
REMARK 465 GLY A 376
REMARK 465 HIS A 377
REMARK 465 GLU A 378
REMARK 465 GLU A 379
REMARK 465 SER A 380
REMARK 465 GLY A 381
REMARK 465 ASP A 382
REMARK 465 ARG A 383
REMARK 465 PHE A 384
REMARK 465 SER A 385
REMARK 465 ASN A 386
REMARK 465 SER A 387
REMARK 465 SER A 388
REMARK 465 THR A 389
REMARK 465 ALA A 390
REMARK 465 PHE A 391
REMARK 465 PHE A 539
REMARK 465 SER A 540
REMARK 465 ASN A 541
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 LYS B 29 CG CD CE NZ
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 ASP B 48 CG OD1 OD2
REMARK 470 GLU B 56 CG CD OE1 OE2
REMARK 470 VAL B 58 CG1 CG2
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 ASN B 90 CG OD1 ND2
REMARK 470 ILE B 120 CG1 CG2 CD1
REMARK 470 GLU B 231 CG CD OE1 OE2
REMARK 470 GLU B 249 CG CD OE1 OE2
REMARK 470 GLU B 250 CG CD OE1 OE2
REMARK 470 GLN B 253 CG CD OE1 NE2
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 ARG B 340 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 341 CG CD CE NZ
REMARK 470 VAL B 343 CG1 CG2
REMARK 470 LYS B 349 CG CD CE NZ
REMARK 470 GLN B 361 CG CD OE1 NE2
REMARK 470 LEU B 394 CG CD1 CD2
REMARK 470 SER B 402 OG
REMARK 470 GLU B 405 CG CD OE1 OE2
REMARK 470 ARG B 441 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 454 CG CD CE NZ
REMARK 470 GLU B 481 CG CD OE1 OE2
REMARK 470 GLU B 499 CG CD OE1 OE2
REMARK 470 LYS B 516 CG CD CE NZ
REMARK 470 LYS B 517 CG CD CE NZ
REMARK 470 GLU B 519 CG CD OE1 OE2
REMARK 470 LEU B 529 CG CD1 CD2
REMARK 470 PHE B 533 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 534 OG
REMARK 470 PRO A 22 CG CD
REMARK 470 LYS A 28 CG CD CE NZ
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 ASP A 48 CG OD1 OD2
REMARK 470 GLU A 56 CG CD OE1 OE2
REMARK 470 VAL A 58 CG1 CG2
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 ASN A 90 CG OD1 ND2
REMARK 470 ILE A 120 CG1 CG2 CD1
REMARK 470 ASN A 207 CG OD1 ND2
REMARK 470 GLU A 231 CG CD OE1 OE2
REMARK 470 GLU A 249 CG CD OE1 OE2
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 GLN A 253 CG CD OE1 NE2
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 GLU A 332 CG CD OE1 OE2
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 ARG A 340 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 341 CG CD CE NZ
REMARK 470 VAL A 343 CG1 CG2
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 GLN A 361 CG CD OE1 NE2
REMARK 470 ARG A 392 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 394 CG CD1 CD2
REMARK 470 SER A 402 OG
REMARK 470 GLU A 405 CG CD OE1 OE2
REMARK 470 ARG A 441 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 453 CG CD CE NZ
REMARK 470 LYS A 454 CG CD CE NZ
REMARK 470 GLU A 481 CG CD OE1 OE2
REMARK 470 GLU A 499 CG CD OE1 OE2
REMARK 470 LYS A 516 CG CD CE NZ
REMARK 470 LYS A 517 CG CD CE NZ
REMARK 470 GLU A 519 CG CD OE1 OE2
REMARK 470 GLU A 526 CG CD OE1 OE2
REMARK 470 LYS A 527 CG CD CE NZ
REMARK 470 ARG A 535 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 536 CG CD OE1 OE2
REMARK 470 VAL A 537 CG1 CG2
REMARK 470 PRO A 538 CG CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 538 C - N - CA ANGL. DEV. = 31.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA B 46 55.30 -91.76
REMARK 500 ARG B 62 96.85 70.44
REMARK 500 LEU B 88 76.86 45.33
REMARK 500 GLN B 117 -75.55 -68.74
REMARK 500 ASN B 118 -43.90 -21.15
REMARK 500 THR B 145 -63.70 -92.66
REMARK 500 ALA B 168 -8.47 -141.63
REMARK 500 ASN B 207 17.68 -146.95
REMARK 500 ARG B 340 -66.79 -93.09
REMARK 500 LYS B 349 -72.65 -56.27
REMARK 500 ARG B 415 -78.74 -118.13
REMARK 500 ARG B 441 43.03 -100.20
REMARK 500 ASN B 472 -34.90 -37.89
REMARK 500 LYS B 517 119.50 -38.49
REMARK 500 ALA A 46 41.56 -86.56
REMARK 500 ARG A 62 109.90 65.90
REMARK 500 LEU A 88 80.22 50.47
REMARK 500 ALA A 144 -159.37 -81.84
REMARK 500 ALA A 168 -6.11 -149.11
REMARK 500 ASN A 207 -38.99 -137.28
REMARK 500 ASP A 215 72.90 -68.97
REMARK 500 ASP A 216 -165.95 -162.79
REMARK 500 ASN A 261 7.15 -67.34
REMARK 500 ARG A 340 -77.22 -72.71
REMARK 500 ARG A 415 -76.90 -115.20
REMARK 500 PHE A 444 -154.91 -91.18
REMARK 500 PHE A 533 -36.05 -132.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 81 O
REMARK 620 2 LEU B 87 O 84.9
REMARK 620 3 LEU B 88 O 145.0 61.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD3 B 601 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 229 OE1
REMARK 620 2 GLU B 229 OE2 48.2
REMARK 620 3 GLU B 232 OE1 79.7 94.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 240 O
REMARK 620 2 SER B 240 OG 62.4
REMARK 620 3 HOH B 706 O 69.2 78.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 81 O
REMARK 620 2 SER A 84 O 77.5
REMARK 620 3 LEU A 87 O 90.9 80.5
REMARK 620 4 LEU A 88 O 147.7 116.1 64.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 GD3 A 601 GD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 229 OE1
REMARK 620 2 GLU A 229 OE2 47.5
REMARK 620 3 GLU A 232 OE1 80.2 89.3
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FBK RELATED DB: PDB
DBREF 5FBH B 20 541 UNP P41180 CASR_HUMAN 20 541
DBREF 5FBH A 20 541 UNP P41180 CASR_HUMAN 20 541
SEQADV 5FBH MET B -26 UNP P41180 INITIATING METHIONINE
SEQADV 5FBH ARG B -25 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU B -24 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU B -23 UNP P41180 EXPRESSION TAG
SEQADV 5FBH THR B -22 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA B -21 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU B -20 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE B -19 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA B -18 UNP P41180 EXPRESSION TAG
SEQADV 5FBH TYR B -17 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE B -16 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ILE B -15 UNP P41180 EXPRESSION TAG
SEQADV 5FBH VAL B -14 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA B -13 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU B -12 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ILE B -11 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU B -10 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA B -9 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE B -8 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER B -7 UNP P41180 EXPRESSION TAG
SEQADV 5FBH VAL B -6 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER B -5 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA B -4 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LYS B -3 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER B -2 UNP P41180 EXPRESSION TAG
SEQADV 5FBH MET B -1 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 0 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 1 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 2 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 3 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 4 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 5 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 6 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 7 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER B 8 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA B 9 UNP P41180 EXPRESSION TAG
SEQADV 5FBH TRP B 10 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER B 11 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS B 12 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PRO B 13 UNP P41180 EXPRESSION TAG
SEQADV 5FBH GLN B 14 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE B 15 UNP P41180 EXPRESSION TAG
SEQADV 5FBH GLU B 16 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LYS B 17 UNP P41180 EXPRESSION TAG
SEQADV 5FBH GLU B 18 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE B 19 UNP P41180 EXPRESSION TAG
SEQADV 5FBH MET A -26 UNP P41180 INITIATING METHIONINE
SEQADV 5FBH ARG A -25 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU A -24 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU A -23 UNP P41180 EXPRESSION TAG
SEQADV 5FBH THR A -22 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA A -21 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU A -20 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE A -19 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA A -18 UNP P41180 EXPRESSION TAG
SEQADV 5FBH TYR A -17 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE A -16 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ILE A -15 UNP P41180 EXPRESSION TAG
SEQADV 5FBH VAL A -14 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA A -13 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU A -12 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ILE A -11 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LEU A -10 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA A -9 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE A -8 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER A -7 UNP P41180 EXPRESSION TAG
SEQADV 5FBH VAL A -6 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER A -5 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA A -4 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LYS A -3 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER A -2 UNP P41180 EXPRESSION TAG
SEQADV 5FBH MET A -1 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 0 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 1 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 2 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 3 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 4 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 5 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 6 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 7 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER A 8 UNP P41180 EXPRESSION TAG
SEQADV 5FBH ALA A 9 UNP P41180 EXPRESSION TAG
SEQADV 5FBH TRP A 10 UNP P41180 EXPRESSION TAG
SEQADV 5FBH SER A 11 UNP P41180 EXPRESSION TAG
SEQADV 5FBH HIS A 12 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PRO A 13 UNP P41180 EXPRESSION TAG
SEQADV 5FBH GLN A 14 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE A 15 UNP P41180 EXPRESSION TAG
SEQADV 5FBH GLU A 16 UNP P41180 EXPRESSION TAG
SEQADV 5FBH LYS A 17 UNP P41180 EXPRESSION TAG
SEQADV 5FBH GLU A 18 UNP P41180 EXPRESSION TAG
SEQADV 5FBH PHE A 19 UNP P41180 EXPRESSION TAG
SEQRES 1 B 568 MET ARG LEU LEU THR ALA LEU PHE ALA TYR PHE ILE VAL
SEQRES 2 B 568 ALA LEU ILE LEU ALA PHE SER VAL SER ALA LYS SER MET
SEQRES 3 B 568 HIS HIS HIS HIS HIS HIS HIS HIS SER ALA TRP SER HIS
SEQRES 4 B 568 PRO GLN PHE GLU LYS GLU PHE TYR GLY PRO ASP GLN ARG
SEQRES 5 B 568 ALA GLN LYS LYS GLY ASP ILE ILE LEU GLY GLY LEU PHE
SEQRES 6 B 568 PRO ILE HIS PHE GLY VAL ALA ALA LYS ASP GLN ASP LEU
SEQRES 7 B 568 LYS SER ARG PRO GLU SER VAL GLU CYS ILE ARG TYR ASN
SEQRES 8 B 568 PHE ARG GLY PHE ARG TRP LEU GLN ALA MET ILE PHE ALA
SEQRES 9 B 568 ILE GLU GLU ILE ASN SER SER PRO ALA LEU LEU PRO ASN
SEQRES 10 B 568 LEU THR LEU GLY TYR ARG ILE PHE ASP THR CYS ASN THR
SEQRES 11 B 568 VAL SER LYS ALA LEU GLU ALA THR LEU SER PHE VAL ALA
SEQRES 12 B 568 GLN ASN LYS ILE ASP SER LEU ASN LEU ASP GLU PHE CYS
SEQRES 13 B 568 ASN CYS SER GLU HIS ILE PRO SER THR ILE ALA VAL VAL
SEQRES 14 B 568 GLY ALA THR GLY SER GLY VAL SER THR ALA VAL ALA ASN
SEQRES 15 B 568 LEU LEU GLY LEU PHE TYR ILE PRO GLN VAL SER TYR ALA
SEQRES 16 B 568 SER SER SER ARG LEU LEU SER ASN LYS ASN GLN PHE LYS
SEQRES 17 B 568 SER PHE LEU ARG THR ILE PRO ASN ASP GLU HIS GLN ALA
SEQRES 18 B 568 THR ALA MET ALA ASP ILE ILE GLU TYR PHE ARG TRP ASN
SEQRES 19 B 568 TRP VAL GLY THR ILE ALA ALA ASP ASP ASP TYR GLY ARG
SEQRES 20 B 568 PRO GLY ILE GLU LYS PHE ARG GLU GLU ALA GLU GLU ARG
SEQRES 21 B 568 ASP ILE CSO ILE ASP PHE SER GLU LEU ILE SER GLN TYR
SEQRES 22 B 568 SER ASP GLU GLU GLU ILE GLN HIS VAL VAL GLU VAL ILE
SEQRES 23 B 568 GLN ASN SER THR ALA LYS VAL ILE VAL VAL PHE SER SER
SEQRES 24 B 568 GLY PRO ASP LEU GLU PRO LEU ILE LYS GLU ILE VAL ARG
SEQRES 25 B 568 ARG ASN ILE THR GLY LYS ILE TRP LEU ALA SER GLU ALA
SEQRES 26 B 568 TRP ALA SER SER SER LEU ILE ALA MET PRO GLN TYR PHE
SEQRES 27 B 568 HIS VAL VAL GLY GLY THR ILE GLY PHE ALA LEU LYS ALA
SEQRES 28 B 568 GLY GLN ILE PRO GLY PHE ARG GLU PHE LEU LYS LYS VAL
SEQRES 29 B 568 HIS PRO ARG LYS SER VAL HIS ASN GLY PHE ALA LYS GLU
SEQRES 30 B 568 PHE TRP GLU GLU THR PHE ASN CYS HIS LEU GLN GLU GLY
SEQRES 31 B 568 ALA LYS GLY PRO LEU PRO VAL ASP THR PHE LEU ARG GLY
SEQRES 32 B 568 HIS GLU GLU SER GLY ASP ARG PHE SER ASN SER SER THR
SEQRES 33 B 568 ALA PHE ARG PRO LEU CYS THR GLY ASP GLU ASN ILE SER
SEQRES 34 B 568 SER VAL GLU THR PRO TYR ILE ASP TYR THR HIS LEU ARG
SEQRES 35 B 568 ILE SER TYR ASN VAL TYR LEU ALA VAL TYR SER ILE ALA
SEQRES 36 B 568 HIS ALA LEU GLN ASP ILE TYR THR CYS LEU PRO GLY ARG
SEQRES 37 B 568 GLY LEU PHE THR ASN GLY SER CYS ALA ASP ILE LYS LYS
SEQRES 38 B 568 VAL GLU ALA TRP GLN VAL LEU LYS HIS LEU ARG HIS LEU
SEQRES 39 B 568 ASN PHE THR ASN ASN MET GLY GLU GLN VAL THR PHE ASP
SEQRES 40 B 568 GLU CSO GLY ASP LEU VAL GLY ASN TYR SER ILE ILE ASN
SEQRES 41 B 568 TRP HIS LEU SER PRO GLU ASP GLY SER ILE VAL PHE LYS
SEQRES 42 B 568 GLU VAL GLY TYR TYR ASN VAL TYR ALA LYS LYS GLY GLU
SEQRES 43 B 568 ARG LEU PHE ILE ASN GLU GLU LYS ILE LEU TRP SER GLY
SEQRES 44 B 568 PHE SER ARG GLU VAL PRO PHE SER ASN
SEQRES 1 A 568 MET ARG LEU LEU THR ALA LEU PHE ALA TYR PHE ILE VAL
SEQRES 2 A 568 ALA LEU ILE LEU ALA PHE SER VAL SER ALA LYS SER MET
SEQRES 3 A 568 HIS HIS HIS HIS HIS HIS HIS HIS SER ALA TRP SER HIS
SEQRES 4 A 568 PRO GLN PHE GLU LYS GLU PHE TYR GLY PRO ASP GLN ARG
SEQRES 5 A 568 ALA GLN LYS LYS GLY ASP ILE ILE LEU GLY GLY LEU PHE
SEQRES 6 A 568 PRO ILE HIS PHE GLY VAL ALA ALA LYS ASP GLN ASP LEU
SEQRES 7 A 568 LYS SER ARG PRO GLU SER VAL GLU CYS ILE ARG TYR ASN
SEQRES 8 A 568 PHE ARG GLY PHE ARG TRP LEU GLN ALA MET ILE PHE ALA
SEQRES 9 A 568 ILE GLU GLU ILE ASN SER SER PRO ALA LEU LEU PRO ASN
SEQRES 10 A 568 LEU THR LEU GLY TYR ARG ILE PHE ASP THR CYS ASN THR
SEQRES 11 A 568 VAL SER LYS ALA LEU GLU ALA THR LEU SER PHE VAL ALA
SEQRES 12 A 568 GLN ASN LYS ILE ASP SER LEU ASN LEU ASP GLU PHE CYS
SEQRES 13 A 568 ASN CYS SER GLU HIS ILE PRO SER THR ILE ALA VAL VAL
SEQRES 14 A 568 GLY ALA THR GLY SER GLY VAL SER THR ALA VAL ALA ASN
SEQRES 15 A 568 LEU LEU GLY LEU PHE TYR ILE PRO GLN VAL SER TYR ALA
SEQRES 16 A 568 SER SER SER ARG LEU LEU SER ASN LYS ASN GLN PHE LYS
SEQRES 17 A 568 SER PHE LEU ARG THR ILE PRO ASN ASP GLU HIS GLN ALA
SEQRES 18 A 568 THR ALA MET ALA ASP ILE ILE GLU TYR PHE ARG TRP ASN
SEQRES 19 A 568 TRP VAL GLY THR ILE ALA ALA ASP ASP ASP TYR GLY ARG
SEQRES 20 A 568 PRO GLY ILE GLU LYS PHE ARG GLU GLU ALA GLU GLU ARG
SEQRES 21 A 568 ASP ILE CSO ILE ASP PHE SER GLU LEU ILE SER GLN TYR
SEQRES 22 A 568 SER ASP GLU GLU GLU ILE GLN HIS VAL VAL GLU VAL ILE
SEQRES 23 A 568 GLN ASN SER THR ALA LYS VAL ILE VAL VAL PHE SER SER
SEQRES 24 A 568 GLY PRO ASP LEU GLU PRO LEU ILE LYS GLU ILE VAL ARG
SEQRES 25 A 568 ARG ASN ILE THR GLY LYS ILE TRP LEU ALA SER GLU ALA
SEQRES 26 A 568 TRP ALA SER SER SER LEU ILE ALA MET PRO GLN TYR PHE
SEQRES 27 A 568 HIS VAL VAL GLY GLY THR ILE GLY PHE ALA LEU LYS ALA
SEQRES 28 A 568 GLY GLN ILE PRO GLY PHE ARG GLU PHE LEU LYS LYS VAL
SEQRES 29 A 568 HIS PRO ARG LYS SER VAL HIS ASN GLY PHE ALA LYS GLU
SEQRES 30 A 568 PHE TRP GLU GLU THR PHE ASN CYS HIS LEU GLN GLU GLY
SEQRES 31 A 568 ALA LYS GLY PRO LEU PRO VAL ASP THR PHE LEU ARG GLY
SEQRES 32 A 568 HIS GLU GLU SER GLY ASP ARG PHE SER ASN SER SER THR
SEQRES 33 A 568 ALA PHE ARG PRO LEU CYS THR GLY ASP GLU ASN ILE SER
SEQRES 34 A 568 SER VAL GLU THR PRO TYR ILE ASP TYR THR HIS LEU ARG
SEQRES 35 A 568 ILE SER TYR ASN VAL TYR LEU ALA VAL TYR SER ILE ALA
SEQRES 36 A 568 HIS ALA LEU GLN ASP ILE TYR THR CYS LEU PRO GLY ARG
SEQRES 37 A 568 GLY LEU PHE THR ASN GLY SER CYS ALA ASP ILE LYS LYS
SEQRES 38 A 568 VAL GLU ALA TRP GLN VAL LEU LYS HIS LEU ARG HIS LEU
SEQRES 39 A 568 ASN PHE THR ASN ASN MET GLY GLU GLN VAL THR PHE ASP
SEQRES 40 A 568 GLU CSO GLY ASP LEU VAL GLY ASN TYR SER ILE ILE ASN
SEQRES 41 A 568 TRP HIS LEU SER PRO GLU ASP GLY SER ILE VAL PHE LYS
SEQRES 42 A 568 GLU VAL GLY TYR TYR ASN VAL TYR ALA LYS LYS GLY GLU
SEQRES 43 A 568 ARG LEU PHE ILE ASN GLU GLU LYS ILE LEU TRP SER GLY
SEQRES 44 A 568 PHE SER ARG GLU VAL PRO PHE SER ASN
MODRES 5FBH CSO B 236 CYS MODIFIED RESIDUE
MODRES 5FBH CSO B 482 CYS MODIFIED RESIDUE
MODRES 5FBH CSO A 236 CYS MODIFIED RESIDUE
MODRES 5FBH CSO A 482 CYS MODIFIED RESIDUE
HET CSO B 236 7
HET CSO B 482 7
HET CSO A 236 7
HET CSO A 482 7
HET GD3 B 601 1
HET MG B 602 1
HET MG B 603 1
HET BCT B 604 4
HET CL B 605 1
HET NAG B 606 14
HET NAG B 607 14
HET NAG B 608 14
HET TCR B 609 16
HET GD3 A 601 1
HET MG A 602 1
HET BCT A 603 4
HET CL A 604 1
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET TCR A 609 16
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM GD3 GADOLINIUM ION
HETNAM MG MAGNESIUM ION
HETNAM BCT BICARBONATE ION
HETNAM CL CHLORIDE ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM TCR CYCLOMETHYLTRYPTOPHAN
FORMUL 1 CSO 4(C3 H7 N O3 S)
FORMUL 3 GD3 2(GD 3+)
FORMUL 4 MG 3(MG 2+)
FORMUL 6 BCT 2(C H O3 1-)
FORMUL 7 CL 2(CL 1-)
FORMUL 8 NAG 7(C8 H15 N O6)
FORMUL 11 TCR 2(C12 H12 N2 O2)
FORMUL 21 HOH *17(H2 O)
HELIX 1 AA1 ASN B 64 SER B 84 1 21
HELIX 2 AA2 THR B 103 VAL B 115 1 13
HELIX 3 AA3 VAL B 115 ASP B 121 1 7
HELIX 4 AA4 GLY B 146 GLY B 158 1 13
HELIX 5 AA5 LEU B 159 TYR B 161 5 3
HELIX 6 AA6 SER B 171 ASN B 176 5 6
HELIX 7 AA7 ASN B 189 PHE B 204 1 16
HELIX 8 AA8 TYR B 218 ARG B 233 1 16
HELIX 9 AA9 ASP B 248 ASN B 261 1 14
HELIX 10 AB1 SER B 272 ARG B 286 1 15
HELIX 11 AB2 MET B 307 GLN B 309 5 3
HELIX 12 AB3 TYR B 310 GLY B 315 1 6
HELIX 13 AB4 GLY B 329 LYS B 335 1 7
HELIX 14 AB5 PHE B 347 ASN B 357 1 11
HELIX 15 AB6 ASN B 400 VAL B 404 5 5
HELIX 16 AB7 ARG B 415 THR B 436 1 22
HELIX 17 AB8 PHE B 444 SER B 448 5 5
HELIX 18 AB9 ASP B 451 VAL B 455 5 5
HELIX 19 AC1 GLU B 456 LEU B 467 1 12
HELIX 20 AC2 GLU B 525 ILE B 528 5 4
HELIX 21 AC3 ASN A 64 SER A 84 1 21
HELIX 22 AC4 THR A 103 VAL A 115 1 13
HELIX 23 AC5 VAL A 115 ASP A 121 1 7
HELIX 24 AC6 GLY A 146 PHE A 160 1 15
HELIX 25 AC7 SER A 171 ASN A 176 5 6
HELIX 26 AC8 ASP A 190 PHE A 204 1 15
HELIX 27 AC9 TYR A 218 ARG A 233 1 16
HELIX 28 AD1 ASP A 248 ASN A 261 1 14
HELIX 29 AD2 SER A 272 ARG A 286 1 15
HELIX 30 AD3 SER A 296 SER A 301 1 6
HELIX 31 AD4 MET A 307 GLN A 309 5 3
HELIX 32 AD5 TYR A 310 GLY A 315 1 6
HELIX 33 AD6 GLY A 329 LYS A 336 1 8
HELIX 34 AD7 PHE A 347 ASN A 357 1 11
HELIX 35 AD8 ASN A 400 VAL A 404 5 5
HELIX 36 AD9 ARG A 415 THR A 436 1 22
HELIX 37 AE1 PHE A 444 SER A 448 5 5
HELIX 38 AE2 GLU A 456 LEU A 467 1 12
HELIX 39 AE3 GLU A 525 ILE A 528 5 4
SHEET 1 AA1 6 ALA B 26 LYS B 28 0
SHEET 2 AA1 6 LEU B 93 ASP B 99 -1 O ILE B 97 N ALA B 26
SHEET 3 AA1 6 ILE B 32 PHE B 38 1 N ILE B 32 O GLY B 94
SHEET 4 AA1 6 THR B 138 VAL B 142 1 O ILE B 139 N ILE B 33
SHEET 5 AA1 6 GLN B 164 SER B 166 1 O VAL B 165 N VAL B 141
SHEET 6 AA1 6 PHE B 183 ARG B 185 1 O LEU B 184 N GLN B 164
SHEET 1 AA2 2 HIS B 41 VAL B 44 0
SHEET 2 AA2 2 CYS B 60 TYR B 63 -1 O ILE B 61 N GLY B 43
SHEET 1 AA3 8 CSO B 236 ILE B 243 0
SHEET 2 AA3 8 TRP B 208 ALA B 214 1 N VAL B 209 O ASP B 238
SHEET 3 AA3 8 VAL B 266 PHE B 270 1 O VAL B 268 N GLY B 210
SHEET 4 AA3 8 ILE B 292 ALA B 295 1 O ILE B 292 N ILE B 267
SHEET 5 AA3 8 ILE B 318 LEU B 322 1 O ILE B 318 N ALA B 295
SHEET 6 AA3 8 TYR B 489 LEU B 496 -1 O SER B 490 N ALA B 321
SHEET 7 AA3 8 ILE B 503 TYR B 511 -1 O LYS B 506 N ASN B 493
SHEET 8 AA3 8 LEU B 521 ILE B 523 -1 O PHE B 522 N TYR B 510
SHEET 1 AA4 2 PHE B 469 THR B 470 0
SHEET 2 AA4 2 GLN B 476 VAL B 477 -1 O VAL B 477 N PHE B 469
SHEET 1 AA5 6 ALA A 26 LYS A 28 0
SHEET 2 AA5 6 LEU A 93 ASP A 99 -1 O ILE A 97 N ALA A 26
SHEET 3 AA5 6 ILE A 32 PHE A 38 1 N ILE A 32 O GLY A 94
SHEET 4 AA5 6 THR A 138 VAL A 142 1 O ALA A 140 N GLY A 35
SHEET 5 AA5 6 GLN A 164 SER A 166 1 O VAL A 165 N VAL A 141
SHEET 6 AA5 6 PHE A 183 ARG A 185 1 O LEU A 184 N SER A 166
SHEET 1 AA6 2 HIS A 41 VAL A 44 0
SHEET 2 AA6 2 CYS A 60 TYR A 63 -1 O ILE A 61 N GLY A 43
SHEET 1 AA7 8 CSO A 236 ILE A 243 0
SHEET 2 AA7 8 TRP A 208 ALA A 214 1 N VAL A 209 O ASP A 238
SHEET 3 AA7 8 VAL A 266 PHE A 270 1 O VAL A 266 N GLY A 210
SHEET 4 AA7 8 ILE A 292 ALA A 295 1 O ILE A 292 N ILE A 267
SHEET 5 AA7 8 ILE A 318 ALA A 321 1 O ILE A 318 N ALA A 295
SHEET 6 AA7 8 TYR A 489 LEU A 496 -1 O SER A 490 N ALA A 321
SHEET 7 AA7 8 ILE A 503 TYR A 511 -1 O VAL A 508 N ILE A 491
SHEET 8 AA7 8 LEU A 521 ILE A 523 -1 O PHE A 522 N TYR A 510
SHEET 1 AA8 2 ASN A 468 THR A 470 0
SHEET 2 AA8 2 GLN A 476 THR A 478 -1 O VAL A 477 N PHE A 469
SSBOND 1 CYS B 60 CYS B 101 1555 1555 2.02
SSBOND 2 CYS B 358 CYS B 395 1555 1555 2.05
SSBOND 3 CYS B 437 CYS B 449 1555 1555 2.06
SSBOND 4 CYS A 60 CYS A 101 1555 1555 2.04
SSBOND 5 CYS A 358 CYS A 395 1555 1555 2.04
SSBOND 6 CYS A 437 CYS A 449 1555 1555 2.06
LINK C ILE B 235 N CSO B 236 1555 1555 1.33
LINK C CSO B 236 N ILE B 237 1555 1555 1.33
LINK ND2 ASN B 261 C1 NAG B 606 1555 1555 1.44
LINK ND2 ASN B 287 C1 NAG B 607 1555 1555 1.45
LINK ND2 ASN B 468 C1 NAG B 608 1555 1555 1.44
LINK C GLU B 481 N CSO B 482 1555 1555 1.33
LINK C CSO B 482 N GLY B 483 1555 1555 1.33
LINK C ILE A 235 N CSO A 236 1555 1555 1.33
LINK C CSO A 236 N ILE A 237 1555 1555 1.33
LINK ND2 ASN A 261 C1 NAG A 605 1555 1555 1.44
LINK ND2 ASN A 287 C1 NAG A 606 1555 1555 1.44
LINK ND2 ASN A 468 C1 NAG A 607 1555 1555 1.47
LINK C GLU A 481 N CSO A 482 1555 1555 1.34
LINK C CSO A 482 N GLY A 483 1555 1555 1.33
LINK ND2 ASN A 488 C1 NAG A 608 1555 1555 1.45
LINK O ILE B 81 MG MG B 603 1555 1555 2.79
LINK O LEU B 87 MG MG B 603 1555 1555 2.92
LINK O LEU B 88 MG MG B 603 1555 1555 2.61
LINK OE1 GLU B 229 GD GD3 B 601 1555 1555 2.74
LINK OE2 GLU B 229 GD GD3 B 601 1555 1555 2.70
LINK OE1 GLU B 232 GD GD3 B 601 1555 1555 2.68
LINK O SER B 240 MG MG B 602 1555 1555 2.57
LINK OG SER B 240 MG MG B 602 1555 1555 2.38
LINK MG MG B 602 O HOH B 706 1555 1555 2.54
LINK O ILE A 81 MG MG A 602 1555 1555 2.52
LINK O SER A 84 MG MG A 602 1555 1555 2.75
LINK O LEU A 87 MG MG A 602 1555 1555 2.53
LINK O LEU A 88 MG MG A 602 1555 1555 2.67
LINK OE1 GLU A 229 GD GD3 A 601 1555 1555 2.73
LINK OE2 GLU A 229 GD GD3 A 601 1555 1555 2.71
LINK OE1 GLU A 232 GD GD3 A 601 1555 1555 2.53
CISPEP 1 GLY B 143 ALA B 144 0 -10.16
CISPEP 2 GLY A 143 ALA A 144 0 -12.12
CRYST1 172.107 83.106 94.470 90.00 105.15 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005810 0.000000 0.001573 0.00000
SCALE2 0.000000 0.012033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010967 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
