HEADER HORMONE/GROWTH FACTOR RECEPTOR 16-JAN-05 1YK0
TITLE STRUCTURE OF NATRIURETIC PEPTIDE RECEPTOR-C COMPLEXED WITH ATRIAL
TITLE 2 NATRIURETIC PEPTIDE
CAVEAT 1YK0 NAG A 511 HAS WRONG CHIRALITY AT ATOM C1 NAG A 512 HAS WRONG
CAVEAT 2 1YK0 CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATRIAL NATRIURETIC PEPTIDE CLEARANCE RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ANP-C, ANPRC, NPR-C, ATRIAL NATRIURETIC PEPTIDE C-TYPE
COMPND 5 RECEPTOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ATRIAL NATRIURETIC FACTOR;
COMPND 9 CHAIN: E;
COMPND 10 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: NPR3, ANPRC;
SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: S2;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PRMHA3;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS HORMONE-RECEPTOR COMPLEX, NATRIURETIC PEPTIDE RECEPTOR, ALLOSTERIC
KEYWDS 2 ACTIVATION, HORMONE-GROWTH FACTOR RECEPTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
NUMMDL 2
AUTHOR X.HE,K.C.GARCIA
REVDAT 6 23-AUG-23 1YK0 1 HETSYN
REVDAT 5 29-JUL-20 1YK0 1 CAVEAT COMPND REMARK HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 13-JUL-11 1YK0 1 VERSN
REVDAT 3 24-FEB-09 1YK0 1 VERSN
REVDAT 2 03-OCT-06 1YK0 1 JRNL
REVDAT 1 18-APR-06 1YK0 0
JRNL AUTH X.L.HE,A.DUKKIPATI,K.C.GARCIA
JRNL TITL STRUCTURAL DETERMINANTS OF NATRIURETIC PEPTIDE RECEPTOR
JRNL TITL 2 SPECIFICITY AND DEGENERACY.
JRNL REF J.MOL.BIOL. V. 361 698 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16870210
JRNL DOI 10.1016/J.JMB.2006.06.060
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.49
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3940
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6371
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 72
REMARK 3 SOLVENT ATOMS : 320
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YK0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031601.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: CNS
REMARK 200 STARTING MODEL: 1JDP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.43300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.84900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.73400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.84900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.43300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.73400
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, 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 1 MET A -44
REMARK 465 1 PRO A -43
REMARK 465 1 SER A -42
REMARK 465 1 LEU A -41
REMARK 465 1 LEU A -40
REMARK 465 1 VAL A -39
REMARK 465 1 LEU A -38
REMARK 465 1 THR A -37
REMARK 465 1 PHE A -36
REMARK 465 1 SER A -35
REMARK 465 1 PRO A -34
REMARK 465 1 CYS A -33
REMARK 465 1 VAL A -32
REMARK 465 1 LEU A -31
REMARK 465 1 LEU A -30
REMARK 465 1 GLY A -29
REMARK 465 1 TRP A -28
REMARK 465 1 ALA A -27
REMARK 465 1 LEU A -26
REMARK 465 1 LEU A -25
REMARK 465 1 ALA A -24
REMARK 465 1 GLY A -23
REMARK 465 1 GLY A -22
REMARK 465 1 THR A -21
REMARK 465 1 GLY A -20
REMARK 465 1 GLY A -19
REMARK 465 1 GLY A -18
REMARK 465 1 GLY A -17
REMARK 465 1 VAL A -16
REMARK 465 1 GLY A -15
REMARK 465 1 GLY A -14
REMARK 465 1 GLY A -13
REMARK 465 1 GLY A -12
REMARK 465 1 GLY A -11
REMARK 465 1 GLY A -10
REMARK 465 1 ALA A -9
REMARK 465 1 GLY A -8
REMARK 465 1 ILE A -7
REMARK 465 1 GLY A -6
REMARK 465 1 GLY A -5
REMARK 465 1 GLY A -4
REMARK 465 1 ARG A -3
REMARK 465 1 GLN A -2
REMARK 465 1 GLU A -1
REMARK 465 1 ARG A 0
REMARK 465 1 GLU A 1
REMARK 465 1 ASN A 41
REMARK 465 1 GLY A 42
REMARK 465 1 THR A 43
REMARK 465 1 GLY A 44
REMARK 465 1 ARG A 45
REMARK 465 1 ARG A 46
REMARK 465 1 ASN A 402
REMARK 465 1 VAL A 403
REMARK 465 1 LYS A 404
REMARK 465 1 TYR A 405
REMARK 465 1 PRO A 406
REMARK 465 1 TRP A 407
REMARK 465 1 GLY A 408
REMARK 465 1 PRO A 409
REMARK 465 1 LEU A 410
REMARK 465 1 LYS A 411
REMARK 465 1 LEU A 412
REMARK 465 1 ARG A 413
REMARK 465 1 ILE A 414
REMARK 465 1 ASP A 415
REMARK 465 1 GLU A 416
REMARK 465 1 ASN A 417
REMARK 465 1 ARG A 418
REMARK 465 1 ILE A 419
REMARK 465 1 VAL A 420
REMARK 465 1 GLU A 421
REMARK 465 1 HIS A 422
REMARK 465 1 THR A 423
REMARK 465 1 ASN A 424
REMARK 465 1 SER A 425
REMARK 465 1 SER A 426
REMARK 465 1 PRO A 427
REMARK 465 1 CYS A 428
REMARK 465 1 LYS A 429
REMARK 465 1 SER A 430
REMARK 465 1 SER A 431
REMARK 465 1 GLY A 432
REMARK 465 1 GLY A 433
REMARK 465 1 LEU A 434
REMARK 465 1 GLU A 435
REMARK 465 1 MET B -44
REMARK 465 1 PRO B -43
REMARK 465 1 SER B -42
REMARK 465 1 LEU B -41
REMARK 465 1 LEU B -40
REMARK 465 1 VAL B -39
REMARK 465 1 LEU B -38
REMARK 465 1 THR B -37
REMARK 465 1 PHE B -36
REMARK 465 1 SER B -35
REMARK 465 1 PRO B -34
REMARK 465 1 CYS B -33
REMARK 465 1 VAL B -32
REMARK 465 1 LEU B -31
REMARK 465 1 LEU B -30
REMARK 465 1 GLY B -29
REMARK 465 1 TRP B -28
REMARK 465 1 ALA B -27
REMARK 465 1 LEU B -26
REMARK 465 1 LEU B -25
REMARK 465 1 ALA B -24
REMARK 465 1 GLY B -23
REMARK 465 1 GLY B -22
REMARK 465 1 THR B -21
REMARK 465 1 GLY B -20
REMARK 465 1 GLY B -19
REMARK 465 1 GLY B -18
REMARK 465 1 GLY B -17
REMARK 465 1 VAL B -16
REMARK 465 1 GLY B -15
REMARK 465 1 GLY B -14
REMARK 465 1 GLY B -13
REMARK 465 1 GLY B -12
REMARK 465 1 GLY B -11
REMARK 465 1 GLY B -10
REMARK 465 1 ALA B -9
REMARK 465 1 GLY B -8
REMARK 465 1 ILE B -7
REMARK 465 1 GLY B -6
REMARK 465 1 GLY B -5
REMARK 465 1 GLY B -4
REMARK 465 1 ARG B -3
REMARK 465 1 GLN B -2
REMARK 465 1 GLU B -1
REMARK 465 1 ARG B 0
REMARK 465 1 GLU B 1
REMARK 465 1 ASN B 41
REMARK 465 1 GLY B 42
REMARK 465 1 THR B 43
REMARK 465 1 GLY B 44
REMARK 465 1 ARG B 45
REMARK 465 1 ARG B 46
REMARK 465 1 ASN B 402
REMARK 465 1 VAL B 403
REMARK 465 1 LYS B 404
REMARK 465 1 TYR B 405
REMARK 465 1 PRO B 406
REMARK 465 1 TRP B 407
REMARK 465 1 GLY B 408
REMARK 465 1 PRO B 409
REMARK 465 1 LEU B 410
REMARK 465 1 LYS B 411
REMARK 465 1 LEU B 412
REMARK 465 1 ARG B 413
REMARK 465 1 ILE B 414
REMARK 465 1 ASP B 415
REMARK 465 1 GLU B 416
REMARK 465 1 ASN B 417
REMARK 465 1 ARG B 418
REMARK 465 1 ILE B 419
REMARK 465 1 VAL B 420
REMARK 465 1 GLU B 421
REMARK 465 1 HIS B 422
REMARK 465 1 THR B 423
REMARK 465 1 ASN B 424
REMARK 465 1 SER B 425
REMARK 465 1 SER B 426
REMARK 465 1 PRO B 427
REMARK 465 1 CYS B 428
REMARK 465 1 LYS B 429
REMARK 465 1 SER B 430
REMARK 465 1 SER B 431
REMARK 465 1 GLY B 432
REMARK 465 1 GLY B 433
REMARK 465 1 LEU B 434
REMARK 465 1 GLU B 435
REMARK 465 2 MET A -44
REMARK 465 2 PRO A -43
REMARK 465 2 SER A -42
REMARK 465 2 LEU A -41
REMARK 465 2 LEU A -40
REMARK 465 2 VAL A -39
REMARK 465 2 LEU A -38
REMARK 465 2 THR A -37
REMARK 465 2 PHE A -36
REMARK 465 2 SER A -35
REMARK 465 2 PRO A -34
REMARK 465 2 CYS A -33
REMARK 465 2 VAL A -32
REMARK 465 2 LEU A -31
REMARK 465 2 LEU A -30
REMARK 465 2 GLY A -29
REMARK 465 2 TRP A -28
REMARK 465 2 ALA A -27
REMARK 465 2 LEU A -26
REMARK 465 2 LEU A -25
REMARK 465 2 ALA A -24
REMARK 465 2 GLY A -23
REMARK 465 2 GLY A -22
REMARK 465 2 THR A -21
REMARK 465 2 GLY A -20
REMARK 465 2 GLY A -19
REMARK 465 2 GLY A -18
REMARK 465 2 GLY A -17
REMARK 465 2 VAL A -16
REMARK 465 2 GLY A -15
REMARK 465 2 GLY A -14
REMARK 465 2 GLY A -13
REMARK 465 2 GLY A -12
REMARK 465 2 GLY A -11
REMARK 465 2 GLY A -10
REMARK 465 2 ALA A -9
REMARK 465 2 GLY A -8
REMARK 465 2 ILE A -7
REMARK 465 2 GLY A -6
REMARK 465 2 GLY A -5
REMARK 465 2 GLY A -4
REMARK 465 2 ARG A -3
REMARK 465 2 GLN A -2
REMARK 465 2 GLU A -1
REMARK 465 2 ARG A 0
REMARK 465 2 GLU A 1
REMARK 465 2 ASN A 41
REMARK 465 2 GLY A 42
REMARK 465 2 THR A 43
REMARK 465 2 GLY A 44
REMARK 465 2 ARG A 45
REMARK 465 2 ARG A 46
REMARK 465 2 ASN A 402
REMARK 465 2 VAL A 403
REMARK 465 2 LYS A 404
REMARK 465 2 TYR A 405
REMARK 465 2 PRO A 406
REMARK 465 2 TRP A 407
REMARK 465 2 GLY A 408
REMARK 465 2 PRO A 409
REMARK 465 2 LEU A 410
REMARK 465 2 LYS A 411
REMARK 465 2 LEU A 412
REMARK 465 2 ARG A 413
REMARK 465 2 ILE A 414
REMARK 465 2 ASP A 415
REMARK 465 2 GLU A 416
REMARK 465 2 ASN A 417
REMARK 465 2 ARG A 418
REMARK 465 2 ILE A 419
REMARK 465 2 VAL A 420
REMARK 465 2 GLU A 421
REMARK 465 2 HIS A 422
REMARK 465 2 THR A 423
REMARK 465 2 ASN A 424
REMARK 465 2 SER A 425
REMARK 465 2 SER A 426
REMARK 465 2 PRO A 427
REMARK 465 2 CYS A 428
REMARK 465 2 LYS A 429
REMARK 465 2 SER A 430
REMARK 465 2 SER A 431
REMARK 465 2 GLY A 432
REMARK 465 2 GLY A 433
REMARK 465 2 LEU A 434
REMARK 465 2 GLU A 435
REMARK 465 2 MET B -44
REMARK 465 2 PRO B -43
REMARK 465 2 SER B -42
REMARK 465 2 LEU B -41
REMARK 465 2 LEU B -40
REMARK 465 2 VAL B -39
REMARK 465 2 LEU B -38
REMARK 465 2 THR B -37
REMARK 465 2 PHE B -36
REMARK 465 2 SER B -35
REMARK 465 2 PRO B -34
REMARK 465 2 CYS B -33
REMARK 465 2 VAL B -32
REMARK 465 2 LEU B -31
REMARK 465 2 LEU B -30
REMARK 465 2 GLY B -29
REMARK 465 2 TRP B -28
REMARK 465 2 ALA B -27
REMARK 465 2 LEU B -26
REMARK 465 2 LEU B -25
REMARK 465 2 ALA B -24
REMARK 465 2 GLY B -23
REMARK 465 2 GLY B -22
REMARK 465 2 THR B -21
REMARK 465 2 GLY B -20
REMARK 465 2 GLY B -19
REMARK 465 2 GLY B -18
REMARK 465 2 GLY B -17
REMARK 465 2 VAL B -16
REMARK 465 2 GLY B -15
REMARK 465 2 GLY B -14
REMARK 465 2 GLY B -13
REMARK 465 2 GLY B -12
REMARK 465 2 GLY B -11
REMARK 465 2 GLY B -10
REMARK 465 2 ALA B -9
REMARK 465 2 GLY B -8
REMARK 465 2 ILE B -7
REMARK 465 2 GLY B -6
REMARK 465 2 GLY B -5
REMARK 465 2 GLY B -4
REMARK 465 2 ARG B -3
REMARK 465 2 GLN B -2
REMARK 465 2 GLU B -1
REMARK 465 2 ARG B 0
REMARK 465 2 GLU B 1
REMARK 465 2 ASN B 41
REMARK 465 2 GLY B 42
REMARK 465 2 THR B 43
REMARK 465 2 GLY B 44
REMARK 465 2 ARG B 45
REMARK 465 2 ARG B 46
REMARK 465 2 ASN B 402
REMARK 465 2 VAL B 403
REMARK 465 2 LYS B 404
REMARK 465 2 TYR B 405
REMARK 465 2 PRO B 406
REMARK 465 2 TRP B 407
REMARK 465 2 GLY B 408
REMARK 465 2 PRO B 409
REMARK 465 2 LEU B 410
REMARK 465 2 LYS B 411
REMARK 465 2 LEU B 412
REMARK 465 2 ARG B 413
REMARK 465 2 ILE B 414
REMARK 465 2 ASP B 415
REMARK 465 2 GLU B 416
REMARK 465 2 ASN B 417
REMARK 465 2 ARG B 418
REMARK 465 2 ILE B 419
REMARK 465 2 VAL B 420
REMARK 465 2 GLU B 421
REMARK 465 2 HIS B 422
REMARK 465 2 THR B 423
REMARK 465 2 ASN B 424
REMARK 465 2 SER B 425
REMARK 465 2 SER B 426
REMARK 465 2 PRO B 427
REMARK 465 2 CYS B 428
REMARK 465 2 LYS B 429
REMARK 465 2 SER B 430
REMARK 465 2 SER B 431
REMARK 465 2 GLY B 432
REMARK 465 2 GLY B 433
REMARK 465 2 LEU B 434
REMARK 465 2 GLU B 435
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 1 ALA A 78 7.32 -64.73
REMARK 500 1 SER A 124 -89.20 -136.11
REMARK 500 1 LEU A 164 -95.19 -125.73
REMARK 500 1 SER A 209 -83.85 -101.84
REMARK 500 1 ALA A 217 -179.76 -170.97
REMARK 500 1 LYS A 300 31.08 -78.67
REMARK 500 1 ASP A 307 -66.90 -18.49
REMARK 500 1 ARG A 332 -8.68 -53.48
REMARK 500 1 ASN A 349 57.63 28.90
REMARK 500 1 ASP A 362 -178.24 -59.88
REMARK 500 1 PRO B 5 102.83 -58.84
REMARK 500 1 SER B 37 -2.42 -57.96
REMARK 500 1 ARG B 79 -135.49 50.10
REMARK 500 1 SER B 124 -89.56 -129.89
REMARK 500 1 SER B 153 -2.55 -145.20
REMARK 500 1 LEU B 164 -88.98 -132.49
REMARK 500 1 GLU B 193 2.82 -62.11
REMARK 500 1 LEU B 199 7.28 -54.64
REMARK 500 1 SER B 209 -112.43 -62.51
REMARK 500 1 CYS B 216 115.97 -160.14
REMARK 500 1 SER B 236 62.68 65.54
REMARK 500 1 ASP B 254 146.70 -36.98
REMARK 500 1 TYR B 271 -7.44 -58.89
REMARK 500 1 ASN B 304 98.04 -58.10
REMARK 500 1 MET B 305 120.75 -37.71
REMARK 500 1 GLU B 306 -83.78 -50.16
REMARK 500 1 ASP B 307 -32.53 -160.43
REMARK 500 1 TYR B 308 -156.54 179.20
REMARK 500 1 ALA B 333 4.42 -58.12
REMARK 500 1 ASP B 339 55.67 -93.92
REMARK 500 1 ASN B 349 65.75 39.26
REMARK 500 1 ASP B 378 88.29 -163.55
REMARK 500 1 PHE E 8 -40.47 -166.19
REMARK 500 1 ARG E 11 -142.67 -148.97
REMARK 500 1 MET E 12 3.26 179.95
REMARK 500 1 ASP E 13 -63.64 9.29
REMARK 500 1 ARG E 14 26.41 -66.48
REMARK 500 1 ALA E 17 -48.81 -132.38
REMARK 500 1 GLN E 18 -55.21 161.54
REMARK 500 1 SER E 19 76.63 -33.64
REMARK 500 1 CYS E 23 -150.27 -68.45
REMARK 500 1 SER E 25 144.29 162.04
REMARK 500 2 ALA A 78 7.32 -64.73
REMARK 500 2 SER A 124 -89.20 -136.11
REMARK 500 2 LEU A 164 -95.19 -125.73
REMARK 500 2 SER A 209 -83.85 -101.84
REMARK 500 2 ALA A 217 -179.76 -170.97
REMARK 500 2 LYS A 300 31.08 -78.67
REMARK 500 2 ASP A 307 -66.90 -18.49
REMARK 500 2 ARG A 332 -8.68 -53.48
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YK1 RELATED DB: PDB
DBREF 1YK0 A -44 435 UNP P17342 ANPC_HUMAN 1 480
DBREF 1YK0 B -44 435 UNP P17342 ANPC_HUMAN 1 480
DBREF 1YK0 E 6 26 UNP P01160 ANF_HUMAN 129 149
SEQRES 1 A 480 MET PRO SER LEU LEU VAL LEU THR PHE SER PRO CYS VAL
SEQRES 2 A 480 LEU LEU GLY TRP ALA LEU LEU ALA GLY GLY THR GLY GLY
SEQRES 3 A 480 GLY GLY VAL GLY GLY GLY GLY GLY GLY ALA GLY ILE GLY
SEQRES 4 A 480 GLY GLY ARG GLN GLU ARG GLU ALA LEU PRO PRO GLN LYS
SEQRES 5 A 480 ILE GLU VAL LEU VAL LEU LEU PRO GLN ASP ASP SER TYR
SEQRES 6 A 480 LEU PHE SER LEU THR ARG VAL ARG PRO ALA ILE GLU TYR
SEQRES 7 A 480 ALA LEU ARG SER VAL GLU GLY ASN GLY THR GLY ARG ARG
SEQRES 8 A 480 LEU LEU PRO PRO GLY THR ARG PHE GLN VAL ALA TYR GLU
SEQRES 9 A 480 ASP SER ASP CYS GLY ASN ARG ALA LEU PHE SER LEU VAL
SEQRES 10 A 480 ASP ARG VAL ALA ALA ALA ARG GLY ALA LYS PRO ASP LEU
SEQRES 11 A 480 ILE LEU GLY PRO VAL CYS GLU TYR ALA ALA ALA PRO VAL
SEQRES 12 A 480 ALA ARG LEU ALA SER HIS TRP ASP LEU PRO MET LEU SER
SEQRES 13 A 480 ALA GLY ALA LEU ALA ALA GLY PHE GLN HIS LYS ASP SER
SEQRES 14 A 480 GLU TYR SER HIS LEU THR ARG VAL ALA PRO ALA TYR ALA
SEQRES 15 A 480 LYS MET GLY GLU MET MET LEU ALA LEU PHE ARG HIS HIS
SEQRES 16 A 480 HIS TRP SER ARG ALA ALA LEU VAL TYR SER ASP ASP LYS
SEQRES 17 A 480 LEU GLU ARG ASN CYS TYR PHE THR LEU GLU GLY VAL HIS
SEQRES 18 A 480 GLU VAL PHE GLN GLU GLU GLY LEU HIS THR SER ILE TYR
SEQRES 19 A 480 SER PHE ASP GLU THR LYS ASP LEU ASP LEU GLU ASP ILE
SEQRES 20 A 480 VAL ARG ASN ILE GLN ALA SER GLU ARG VAL VAL ILE MET
SEQRES 21 A 480 CYS ALA SER SER ASP THR ILE ARG SER ILE MET LEU VAL
SEQRES 22 A 480 ALA HIS ARG HIS GLY MET THR SER GLY ASP TYR ALA PHE
SEQRES 23 A 480 PHE ASN ILE GLU LEU PHE ASN SER SER SER TYR GLY ASP
SEQRES 24 A 480 GLY SER TRP LYS ARG GLY ASP LYS HIS ASP PHE GLU ALA
SEQRES 25 A 480 LYS GLN ALA TYR SER SER LEU GLN THR VAL THR LEU LEU
SEQRES 26 A 480 ARG THR VAL LYS PRO GLU PHE GLU LYS PHE SER MET GLU
SEQRES 27 A 480 VAL LYS SER SER VAL GLU LYS GLN GLY LEU ASN MET GLU
SEQRES 28 A 480 ASP TYR VAL ASN MET PHE VAL GLU GLY PHE HIS ASP ALA
SEQRES 29 A 480 ILE LEU LEU TYR VAL LEU ALA LEU HIS GLU VAL LEU ARG
SEQRES 30 A 480 ALA GLY TYR SER LYS LYS ASP GLY GLY LYS ILE ILE GLN
SEQRES 31 A 480 GLN THR TRP ASN ARG THR PHE GLU GLY ILE ALA GLY GLN
SEQRES 32 A 480 VAL SER ILE ASP ALA ASN GLY ASP ARG TYR GLY ASP PHE
SEQRES 33 A 480 SER VAL ILE ALA MET THR ASP VAL GLU ALA GLY THR GLN
SEQRES 34 A 480 GLU VAL ILE GLY ASP TYR PHE GLY LYS GLU GLY ARG PHE
SEQRES 35 A 480 GLU MET ARG PRO ASN VAL LYS TYR PRO TRP GLY PRO LEU
SEQRES 36 A 480 LYS LEU ARG ILE ASP GLU ASN ARG ILE VAL GLU HIS THR
SEQRES 37 A 480 ASN SER SER PRO CYS LYS SER SER GLY GLY LEU GLU
SEQRES 1 B 480 MET PRO SER LEU LEU VAL LEU THR PHE SER PRO CYS VAL
SEQRES 2 B 480 LEU LEU GLY TRP ALA LEU LEU ALA GLY GLY THR GLY GLY
SEQRES 3 B 480 GLY GLY VAL GLY GLY GLY GLY GLY GLY ALA GLY ILE GLY
SEQRES 4 B 480 GLY GLY ARG GLN GLU ARG GLU ALA LEU PRO PRO GLN LYS
SEQRES 5 B 480 ILE GLU VAL LEU VAL LEU LEU PRO GLN ASP ASP SER TYR
SEQRES 6 B 480 LEU PHE SER LEU THR ARG VAL ARG PRO ALA ILE GLU TYR
SEQRES 7 B 480 ALA LEU ARG SER VAL GLU GLY ASN GLY THR GLY ARG ARG
SEQRES 8 B 480 LEU LEU PRO PRO GLY THR ARG PHE GLN VAL ALA TYR GLU
SEQRES 9 B 480 ASP SER ASP CYS GLY ASN ARG ALA LEU PHE SER LEU VAL
SEQRES 10 B 480 ASP ARG VAL ALA ALA ALA ARG GLY ALA LYS PRO ASP LEU
SEQRES 11 B 480 ILE LEU GLY PRO VAL CYS GLU TYR ALA ALA ALA PRO VAL
SEQRES 12 B 480 ALA ARG LEU ALA SER HIS TRP ASP LEU PRO MET LEU SER
SEQRES 13 B 480 ALA GLY ALA LEU ALA ALA GLY PHE GLN HIS LYS ASP SER
SEQRES 14 B 480 GLU TYR SER HIS LEU THR ARG VAL ALA PRO ALA TYR ALA
SEQRES 15 B 480 LYS MET GLY GLU MET MET LEU ALA LEU PHE ARG HIS HIS
SEQRES 16 B 480 HIS TRP SER ARG ALA ALA LEU VAL TYR SER ASP ASP LYS
SEQRES 17 B 480 LEU GLU ARG ASN CYS TYR PHE THR LEU GLU GLY VAL HIS
SEQRES 18 B 480 GLU VAL PHE GLN GLU GLU GLY LEU HIS THR SER ILE TYR
SEQRES 19 B 480 SER PHE ASP GLU THR LYS ASP LEU ASP LEU GLU ASP ILE
SEQRES 20 B 480 VAL ARG ASN ILE GLN ALA SER GLU ARG VAL VAL ILE MET
SEQRES 21 B 480 CYS ALA SER SER ASP THR ILE ARG SER ILE MET LEU VAL
SEQRES 22 B 480 ALA HIS ARG HIS GLY MET THR SER GLY ASP TYR ALA PHE
SEQRES 23 B 480 PHE ASN ILE GLU LEU PHE ASN SER SER SER TYR GLY ASP
SEQRES 24 B 480 GLY SER TRP LYS ARG GLY ASP LYS HIS ASP PHE GLU ALA
SEQRES 25 B 480 LYS GLN ALA TYR SER SER LEU GLN THR VAL THR LEU LEU
SEQRES 26 B 480 ARG THR VAL LYS PRO GLU PHE GLU LYS PHE SER MET GLU
SEQRES 27 B 480 VAL LYS SER SER VAL GLU LYS GLN GLY LEU ASN MET GLU
SEQRES 28 B 480 ASP TYR VAL ASN MET PHE VAL GLU GLY PHE HIS ASP ALA
SEQRES 29 B 480 ILE LEU LEU TYR VAL LEU ALA LEU HIS GLU VAL LEU ARG
SEQRES 30 B 480 ALA GLY TYR SER LYS LYS ASP GLY GLY LYS ILE ILE GLN
SEQRES 31 B 480 GLN THR TRP ASN ARG THR PHE GLU GLY ILE ALA GLY GLN
SEQRES 32 B 480 VAL SER ILE ASP ALA ASN GLY ASP ARG TYR GLY ASP PHE
SEQRES 33 B 480 SER VAL ILE ALA MET THR ASP VAL GLU ALA GLY THR GLN
SEQRES 34 B 480 GLU VAL ILE GLY ASP TYR PHE GLY LYS GLU GLY ARG PHE
SEQRES 35 B 480 GLU MET ARG PRO ASN VAL LYS TYR PRO TRP GLY PRO LEU
SEQRES 36 B 480 LYS LEU ARG ILE ASP GLU ASN ARG ILE VAL GLU HIS THR
SEQRES 37 B 480 ASN SER SER PRO CYS LYS SER SER GLY GLY LEU GLU
SEQRES 1 E 21 SER CYS PHE GLY GLY ARG MET ASP ARG ILE GLY ALA GLN
SEQRES 2 E 21 SER GLY LEU GLY CYS ASN SER PHE
MODRES 1YK0 ASN A 248 ASN GLYCOSYLATION SITE
MODRES 1YK0 ASN A 349 ASN GLYCOSYLATION SITE
MODRES 1YK0 ASN B 248 ASN GLYCOSYLATION SITE
MODRES 1YK0 ASN B 349 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 511 14
HET NAG A 512 14
HET CL A 513 1
HET NAG B 511 14
HET CL B 512 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CL CHLORIDE ION
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 5(C8 H15 N O6)
FORMUL 7 CL 2(CL 1-)
FORMUL 10 HOH *320(H2 O)
HELIX 1 1 SER A 23 GLU A 39 1 17
HELIX 2 2 ASN A 65 ALA A 78 1 14
HELIX 3 3 CYS A 91 TRP A 105 1 15
HELIX 4 4 ALA A 116 HIS A 121 5 6
HELIX 5 5 ALA A 135 HIS A 151 1 17
HELIX 6 6 ARG A 166 GLY A 183 1 18
HELIX 7 7 ASP A 198 SER A 209 1 12
HELIX 8 8 SER A 218 ARG A 231 1 14
HELIX 9 9 HIS A 263 TYR A 271 1 9
HELIX 10 10 LYS A 284 LYS A 300 1 17
HELIX 11 11 ASN A 310 ARG A 332 1 23
HELIX 12 12 ASP A 339 TRP A 348 1 10
HELIX 13 13 SER B 23 SER B 37 1 15
HELIX 14 14 ASN B 65 ALA B 78 1 14
HELIX 15 15 CYS B 91 TRP B 105 1 15
HELIX 16 16 ALA B 116 HIS B 121 5 6
HELIX 17 17 ALA B 135 HIS B 151 1 17
HELIX 18 18 ARG B 166 GLY B 183 1 18
HELIX 19 19 ASP B 198 GLN B 207 1 10
HELIX 20 20 SER B 218 HIS B 232 1 15
HELIX 21 21 HIS B 263 TYR B 271 1 9
HELIX 22 22 LYS B 284 GLN B 301 1 18
HELIX 23 23 ASN B 310 ALA B 333 1 24
HELIX 24 24 ASP B 339 GLN B 346 1 8
SHEET 1 A 5 ARG A 53 ASP A 60 0
SHEET 2 A 5 LYS A 7 LEU A 14 1 N ILE A 8 O GLN A 55
SHEET 3 A 5 LEU A 85 LEU A 87 1 O LEU A 85 N LEU A 11
SHEET 4 A 5 MET A 109 SER A 111 1 O LEU A 110 N ILE A 86
SHEET 5 A 5 LEU A 129 ARG A 131 1 O THR A 130 N MET A 109
SHEET 1 B 8 HIS A 185 PHE A 191 0
SHEET 2 B 8 ARG A 154 SER A 160 1 N LEU A 157 O SER A 187
SHEET 3 B 8 VAL A 212 CYS A 216 1 O ILE A 214 N ALA A 156
SHEET 4 B 8 ALA A 240 ILE A 244 1 O PHE A 242 N MET A 215
SHEET 5 B 8 LEU A 274 LEU A 279 1 O VAL A 277 N ASN A 243
SHEET 6 B 8 ASP A 370 ASP A 378 -1 O ILE A 374 N THR A 276
SHEET 7 B 8 THR A 383 PHE A 391 -1 O TYR A 390 N PHE A 371
SHEET 8 B 8 ARG A 396 MET A 399 -1 O GLU A 398 N ASP A 389
SHEET 1 C 2 ARG A 350 GLU A 353 0
SHEET 2 C 2 GLN A 358 ILE A 361 -1 O VAL A 359 N PHE A 352
SHEET 1 D 5 ARG B 53 ASP B 60 0
SHEET 2 D 5 LYS B 7 LEU B 14 1 N VAL B 10 O GLN B 55
SHEET 3 D 5 LEU B 85 LEU B 87 1 O LEU B 87 N LEU B 13
SHEET 4 D 5 MET B 109 SER B 111 1 O LEU B 110 N ILE B 86
SHEET 5 D 5 LEU B 129 ARG B 131 1 O THR B 130 N MET B 109
SHEET 1 E 8 HIS B 185 PHE B 191 0
SHEET 2 E 8 ARG B 154 SER B 160 1 N LEU B 157 O SER B 187
SHEET 3 E 8 VAL B 212 CYS B 216 1 O ILE B 214 N ALA B 156
SHEET 4 E 8 ALA B 240 ILE B 244 1 O ALA B 240 N VAL B 213
SHEET 5 E 8 LEU B 274 LEU B 279 1 O VAL B 277 N ASN B 243
SHEET 6 E 8 ASP B 370 ASP B 378 -1 O ILE B 374 N THR B 276
SHEET 7 E 8 THR B 383 PHE B 391 -1 O THR B 383 N THR B 377
SHEET 8 E 8 ARG B 396 MET B 399 -1 O GLU B 398 N ASP B 389
SHEET 1 F 2 ARG B 350 GLY B 354 0
SHEET 2 F 2 GLY B 357 ILE B 361 -1 O VAL B 359 N PHE B 352
SSBOND 1 CYS A 63 CYS A 91 1555 1555 2.04
SSBOND 2 CYS A 168 CYS A 216 1555 1555 2.05
SSBOND 3 CYS B 63 CYS B 91 1555 1555 2.04
SSBOND 4 CYS B 168 CYS B 216 1555 1555 2.06
SSBOND 5 CYS E 7 CYS E 23 1555 1555 2.05
LINK ND2 ASN A 248 C1 NAG A 511 1555 1555 1.46
LINK ND2 ASN A 349 C1 NAG A 512 1555 1555 1.45
LINK ND2 ASN B 248 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN B 349 C1 NAG B 511 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
CISPEP 1 GLY A 88 PRO A 89 1 -0.05
CISPEP 2 GLY B 88 PRO B 89 1 -0.02
CISPEP 3 GLY A 88 PRO A 89 2 -0.05
CISPEP 4 GLY B 88 PRO B 89 2 -0.02
CRYST1 56.866 135.468 137.698 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017585 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007262 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END