| content |
HEADER HYDROLASE 23-JUL-16 5LKR
TITLE HUMAN BUTYRYLCHOLINESTERASE COMPLEXED WITH N-PROPARGYLIPERIDINES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 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: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS ALZHEIMER DISEASE AD BUTYRYLCHOLINESTERASE N-PROPARGYLIPERIDINES,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,D.KNEZ,J.P.COLLETIER,S.GOBEC
REVDAT 1 14-DEC-16 5LKR 0
JRNL AUTH U.KOSAK,D.KNEZ,N.COQUELLE,B.BRUS,A.PISLAR,F.NACHON,
JRNL AUTH 2 X.BRAZZOLOTTO,J.KOS,J.P.COLLETIER,S.GOBEC
JRNL TITL N-PROPARGYLPIPERIDINES WITH NAPHTHALENE-2-CARBOXAMIDE OR
JRNL TITL 2 NAPHTHALENE-2-SULFONAMIDE MOIETIES: POTENTIAL
JRNL TITL 3 MULTIFUNCTIONAL ANTI-ALZHEIMER'S AGENTS.
JRNL REF BIOORG. MED. CHEM. 2016
JRNL REFN ESSN 1464-3391
JRNL PMID 27908752
JRNL DOI 10.1016/J.BMC.2016.11.032
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 45908
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2327
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 48.8663 - 6.4749 0.99 2757 157 0.1716 0.2400
REMARK 3 2 6.4749 - 5.1411 1.00 2663 125 0.1778 0.2205
REMARK 3 3 5.1411 - 4.4918 1.00 2609 140 0.1390 0.1752
REMARK 3 4 4.4918 - 4.0813 0.99 2549 156 0.1384 0.1776
REMARK 3 5 4.0813 - 3.7889 1.00 2580 144 0.1546 0.2280
REMARK 3 6 3.7889 - 3.5656 1.00 2586 139 0.1794 0.2170
REMARK 3 7 3.5656 - 3.3871 1.00 2561 141 0.1916 0.2316
REMARK 3 8 3.3871 - 3.2397 1.00 2585 126 0.2098 0.2601
REMARK 3 9 3.2397 - 3.1150 1.00 2551 154 0.2259 0.2926
REMARK 3 10 3.1150 - 3.0075 1.00 2589 113 0.2276 0.3291
REMARK 3 11 3.0075 - 2.9135 0.99 2528 141 0.2455 0.2778
REMARK 3 12 2.9135 - 2.8302 0.99 2515 116 0.2499 0.3318
REMARK 3 13 2.8302 - 2.7557 0.99 2556 140 0.2775 0.3333
REMARK 3 14 2.7557 - 2.6885 0.99 2527 152 0.3137 0.3757
REMARK 3 15 2.6885 - 2.6274 0.99 2502 138 0.3354 0.3813
REMARK 3 16 2.6274 - 2.5714 0.98 2495 119 0.3410 0.4147
REMARK 3 17 2.5714 - 2.5200 0.95 2428 126 0.3707 0.4356
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) : 0.430
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.850
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 : 0.007 8985
REMARK 3 ANGLE : 0.917 12253
REMARK 3 CHIRALITY : 0.057 1366
REMARK 3 PLANARITY : 0.005 1546
REMARK 3 DIHEDRAL : 12.924 5198
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5LKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000882.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.966
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45918
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 48.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 18% PEG 4000,
REMARK 280 20 MM TRIS PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.0K
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 36.84050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 114.43450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.73150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 114.43450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.84050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.73150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1
REMARK 465 ASP A 2
REMARK 465 GLU A 531
REMARK 465 MET A 532
REMARK 465 THR A 533
REMARK 465 GLY A 534
REMARK 465 ASN A 535
REMARK 465 ILE A 536
REMARK 465 ASP A 537
REMARK 465 GLU A 538
REMARK 465 ALA A 539
REMARK 465 GLU A 540
REMARK 465 TRP A 541
REMARK 465 GLU A 542
REMARK 465 TRP A 543
REMARK 465 LYS A 544
REMARK 465 ALA A 545
REMARK 465 GLY A 546
REMARK 465 PHE A 547
REMARK 465 HIS A 548
REMARK 465 ARG A 549
REMARK 465 TRP A 550
REMARK 465 ASN A 551
REMARK 465 ASN A 552
REMARK 465 TYR A 553
REMARK 465 MET A 554
REMARK 465 MET A 555
REMARK 465 ASP A 556
REMARK 465 TRP A 557
REMARK 465 LYS A 558
REMARK 465 ASN A 559
REMARK 465 GLN A 560
REMARK 465 PHE A 561
REMARK 465 ASN A 562
REMARK 465 ASP A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 SER A 566
REMARK 465 LYS A 567
REMARK 465 LYS A 568
REMARK 465 GLU A 569
REMARK 465 SER A 570
REMARK 465 CYS A 571
REMARK 465 VAL A 572
REMARK 465 GLY A 573
REMARK 465 LEU A 574
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 ASN B 485
REMARK 465 ASN B 486
REMARK 465 GLU B 531
REMARK 465 MET B 532
REMARK 465 THR B 533
REMARK 465 GLY B 534
REMARK 465 ASN B 535
REMARK 465 ILE B 536
REMARK 465 ASP B 537
REMARK 465 GLU B 538
REMARK 465 ALA B 539
REMARK 465 GLU B 540
REMARK 465 TRP B 541
REMARK 465 GLU B 542
REMARK 465 TRP B 543
REMARK 465 LYS B 544
REMARK 465 ALA B 545
REMARK 465 GLY B 546
REMARK 465 PHE B 547
REMARK 465 HIS B 548
REMARK 465 ARG B 549
REMARK 465 TRP B 550
REMARK 465 ASN B 551
REMARK 465 ASN B 552
REMARK 465 TYR B 553
REMARK 465 MET B 554
REMARK 465 MET B 555
REMARK 465 ASP B 556
REMARK 465 TRP B 557
REMARK 465 LYS B 558
REMARK 465 ASN B 559
REMARK 465 GLN B 560
REMARK 465 PHE B 561
REMARK 465 ASN B 562
REMARK 465 ASP B 563
REMARK 465 TYR B 564
REMARK 465 THR B 565
REMARK 465 SER B 566
REMARK 465 LYS B 567
REMARK 465 LYS B 568
REMARK 465 GLU B 569
REMARK 465 SER B 570
REMARK 465 CYS B 571
REMARK 465 VAL B 572
REMARK 465 GLY B 573
REMARK 465 LEU B 574
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 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 105 CG CD CE NZ
REMARK 470 LYS A 248 CD CE NZ
REMARK 470 GLU A 255 CG CD OE1 OE2
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 LYS A 366 CG CD CE NZ
REMARK 470 ARG A 452 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 453 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 506 CG CD OE1 OE2
REMARK 470 LEU A 530 CA C O CB CG CD1 CD2
REMARK 470 ILE B 4 CG1 CG2 CD1
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LYS B 44 CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 SER B 53 OG
REMARK 470 LYS B 190 CG CD CE NZ
REMARK 470 GLU B 257 CG CD OE1 OE2
REMARK 470 ASP B 268 CG OD1 OD2
REMARK 470 GLU B 276 CG CD OE1 OE2
REMARK 470 TYR B 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 454 CG OD1 OD2
REMARK 470 GLN B 484 CG CD OE1 NE2
REMARK 470 SER B 507 CB OG
REMARK 470 LEU B 530 CA C O CB CG CD1 CD2
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 O4 NAG B 607 O HOH B 701 2.09
REMARK 500 NH1 ARG B 465 O HOH B 702 2.09
REMARK 500 OG SER A 198 O HOH A 701 2.14
REMARK 500 NH1 ARG B 240 O HOH B 703 2.17
REMARK 500 O3 GOL A 617 O4 PEG A 618 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE B 364 CB PHE B 364 CG -0.138
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 PHE A 43 -3.19 86.71
REMARK 500 THR A 50 -89.73 -81.28
REMARK 500 SER A 53 68.96 -116.25
REMARK 500 ASP A 54 -147.36 -177.34
REMARK 500 CYS A 92 -2.97 -142.46
REMARK 500 PRO A 160 -7.54 -59.63
REMARK 500 ALA A 162 72.59 -157.61
REMARK 500 SER A 198 -124.52 64.33
REMARK 500 TYR A 282 -105.07 -71.38
REMARK 500 ASP A 297 -73.08 -98.75
REMARK 500 TYR A 332 35.63 -92.51
REMARK 500 ARG A 381 74.45 51.37
REMARK 500 PHE A 398 -52.43 -129.48
REMARK 500 GLU A 482 -79.68 -95.94
REMARK 500 GLU A 506 -75.48 -73.85
REMARK 500 PHE A 525 -35.73 -130.18
REMARK 500 LYS B 9 14.65 -69.93
REMARK 500 PHE B 43 -11.00 82.71
REMARK 500 ASP B 54 -136.51 -87.30
REMARK 500 ALA B 58 66.30 -102.13
REMARK 500 ASN B 106 32.43 -152.85
REMARK 500 ALA B 162 70.94 -165.64
REMARK 500 ASN B 181 -15.72 -142.01
REMARK 500 SER B 198 -118.67 66.19
REMARK 500 THR B 218 -66.14 -96.74
REMARK 500 TYR B 282 75.55 -110.45
REMARK 500 ASP B 297 -66.78 -126.82
REMARK 500 THR B 315 -175.30 -172.37
REMARK 500 PHE B 398 -54.78 -132.55
REMARK 500 PRO B 431 171.06 -59.65
REMARK 500 ASP B 454 30.43 -141.13
REMARK 500 GLU B 482 -138.67 -105.97
REMARK 500 THR B 496 -66.69 -94.86
REMARK 500 GLN B 498 73.88 57.15
REMARK 500 GLU B 506 -99.12 -68.07
REMARK 500 ARG B 515 43.19 36.98
REMARK 500 PRO B 527 10.65 -65.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 FUL A 604
REMARK 610 NAG B 606
REMARK 610 NAG B 612
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 6YC A 616
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6YC A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6YC B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 602 through NAG A 603 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through NAG A 606 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through FUC A 608 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 609 through NAG A 610 bound to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 611 through NAG A 612 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 613 through NAG A 614 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 613 bound
REMARK 800 to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 602 through NAG B 603 bound to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 604 through FUL B 605 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 607 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 609 bound
REMARK 800 to ASN B 481
DBREF 5LKR A 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 5LKR B 1 574 UNP P06276 CHLE_HUMAN 29 602
SEQRES 1 A 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 A 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 A 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 A 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 A 574 GLY LEU
SEQRES 1 B 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 B 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 B 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 B 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 B 574 GLY LEU
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET FUL A 604 10
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET FUC A 608 10
HET NAG A 609 14
HET NAG A 610 14
HET NAG A 611 14
HET NAG A 612 14
HET NAG A 613 14
HET NAG A 614 14
HET GOL A 615 6
HET 6YC A 616 27
HET GOL A 617 6
HET PEG A 618 7
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET FUL B 605 10
HET NAG B 606 14
HET NAG B 607 14
HET NAG B 608 14
HET NAG B 609 14
HET GOL B 610 6
HET 6YC B 611 27
HET NAG B 612 14
HET NAG B 613 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUL BETA-L-FUCOSE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM GOL GLYCEROL
HETNAM 6YC ~{N}-(2-METHOXYETHYL)-~{N}-[[(3~{S})-1-PROP-2-
HETNAM 2 6YC YNYLPIPERIDIN-3-YL]METHYL]NAPHTHALENE-2-CARBOXAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 22(C8 H15 N O6)
FORMUL 5 FUL 2(C6 H12 O5)
FORMUL 7 FUC C6 H12 O5
FORMUL 11 GOL 3(C3 H8 O3)
FORMUL 12 6YC 2(C23 H28 N2 O2)
FORMUL 14 PEG C4 H10 O3
FORMUL 26 HOH *36(H2 O)
HELIX 1 AA1 PHE A 76 MET A 81 1 6
HELIX 2 AA2 LEU A 125 ASP A 129 5 5
HELIX 3 AA3 GLY A 130 ARG A 138 1 9
HELIX 4 AA4 GLY A 149 LEU A 154 1 6
HELIX 5 AA5 ASN A 165 ILE A 182 1 18
HELIX 6 AA6 ALA A 183 PHE A 185 5 3
HELIX 7 AA7 SER A 198 LEU A 208 1 11
HELIX 8 AA8 SER A 235 THR A 250 1 16
HELIX 9 AA9 ASN A 256 ARG A 265 1 10
HELIX 10 AB1 ASP A 268 GLU A 276 1 9
HELIX 11 AB2 ALA A 277 VAL A 279 5 3
HELIX 12 AB3 MET A 302 LEU A 309 1 8
HELIX 13 AB4 GLY A 326 VAL A 331 1 6
HELIX 14 AB5 THR A 346 PHE A 358 1 13
HELIX 15 AB6 SER A 362 TYR A 373 1 12
HELIX 16 AB7 GLU A 383 PHE A 398 1 16
HELIX 17 AB8 PHE A 398 GLU A 411 1 14
HELIX 18 AB9 PRO A 431 GLY A 435 5 5
HELIX 19 AC1 GLU A 441 PHE A 446 1 6
HELIX 20 AC2 GLY A 447 ASN A 455 5 9
HELIX 21 AC3 THR A 457 GLY A 478 1 22
HELIX 22 AC4 ARG A 515 PHE A 525 1 11
HELIX 23 AC5 PHE A 526 VAL A 529 5 4
HELIX 24 AC6 LEU B 38 ARG B 42 5 5
HELIX 25 AC7 PHE B 76 MET B 81 1 6
HELIX 26 AC8 LEU B 125 ASP B 129 5 5
HELIX 27 AC9 GLY B 130 ARG B 138 1 9
HELIX 28 AD1 GLY B 149 LEU B 154 1 6
HELIX 29 AD2 ASN B 165 ILE B 182 1 18
HELIX 30 AD3 ALA B 183 PHE B 185 5 3
HELIX 31 AD4 SER B 198 SER B 210 1 13
HELIX 32 AD5 PRO B 211 PHE B 217 5 7
HELIX 33 AD6 SER B 235 THR B 250 1 16
HELIX 34 AD7 ASN B 256 ARG B 265 1 10
HELIX 35 AD8 ASP B 268 LEU B 274 1 7
HELIX 36 AD9 ASN B 275 VAL B 279 5 5
HELIX 37 AE1 MET B 302 LEU B 309 1 8
HELIX 38 AE2 GLY B 326 GLY B 333 5 8
HELIX 39 AE3 THR B 346 PHE B 358 1 13
HELIX 40 AE4 SER B 362 TYR B 373 1 12
HELIX 41 AE5 GLU B 383 PHE B 398 1 16
HELIX 42 AE6 PHE B 398 GLU B 411 1 14
HELIX 43 AE7 PRO B 431 GLY B 435 5 5
HELIX 44 AE8 GLU B 441 PHE B 446 1 6
HELIX 45 AE9 THR B 457 TYR B 477 1 21
HELIX 46 AF1 ARG B 515 PHE B 525 1 11
HELIX 47 AF2 PHE B 526 VAL B 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 AA211 TYR A 94 PRO A 100 -1 O VAL A 97 N PHE A 28
SHEET 4 AA211 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA211 ALA A 107 ILE A 113 1 N TRP A 112 O VAL A 142
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O ARG A 219 N LEU A 194
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 503 N TYR A 420
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 2 SER A 64 CYS A 65 0
SHEET 2 AA3 2 LEU A 88 SER A 89 1 O SER A 89 N SER A 64
SHEET 1 AA4 3 ILE B 5 THR B 8 0
SHEET 2 AA4 3 GLY B 11 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 AA4 3 ILE B 55 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 AA511 MET B 16 VAL B 20 0
SHEET 2 AA511 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 AA511 TYR B 94 ALA B 101 -1 O LEU B 95 N ILE B 31
SHEET 4 AA511 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA511 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA511 GLY B 187 GLU B 197 1 O THR B 193 N VAL B 109
SHEET 7 AA511 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 AA511 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA511 ALA B 416 PHE B 421 1 O PHE B 421 N VAL B 321
SHEET 10 AA511 LYS B 499 LEU B 503 1 O LEU B 501 N PHE B 418
SHEET 11 AA511 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.04
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.05
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.06
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 57 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 605 1555 1555 1.46
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A 609 1555 1555 1.45
LINK ND2 ASN A 481 C1 NAG A 611 1555 1555 1.45
LINK ND2 ASN A 486 C1 NAG A 613 1555 1555 1.44
LINK ND2 ASN B 17 C1 NAG B 613 1555 1555 1.44
LINK ND2 ASN B 57 C1 NAG B 601 1555 1555 1.45
LINK ND2 ASN B 106 C1 NAG B 602 1555 1555 1.45
LINK ND2 ASN B 241 C1 NAG B 604 1555 1555 1.43
LINK ND2 ASN B 256 C1 NAG B 607 1555 1555 1.45
LINK ND2 ASN B 341 C1 NAG B 608 1555 1555 1.45
LINK ND2 ASN B 481 C1 NAG B 609 1555 1555 1.45
LINK C1 NAG A 602 O4 NAG A 603 1555 1555 1.45
LINK O4 NAG A 605 C1 NAG A 606 1555 1555 1.48
LINK O6 NAG A 607 C1 FUC A 608 1555 1555 1.45
LINK O4 NAG A 609 C1 NAG A 610 1555 1555 1.43
LINK O4 NAG A 611 C1 NAG A 612 1555 1555 1.44
LINK O4 NAG A 613 C1 NAG A 614 1555 1555 1.44
LINK O4 NAG B 602 C1 NAG B 603 1555 1555 1.44
LINK O6 NAG B 604 C1 FUL B 605 1555 1555 1.45
CISPEP 1 ALA A 101 PRO A 102 0 0.51
CISPEP 2 GLN A 380 ARG A 381 0 -6.06
CISPEP 3 ALA B 101 PRO B 102 0 3.73
SITE 1 AC1 1 NAG A 603
SITE 1 AC2 3 ASN A 228 TRP A 522 THR A 523
SITE 1 AC3 4 GLY A 117 THR A 120 SER A 198 HOH A 701
SITE 1 AC4 2 ASN A 455 PEG A 618
SITE 1 AC5 1 GOL A 617
SITE 1 AC6 3 GLN B 380 NAG B 604 HOH B 714
SITE 1 AC7 5 LEU B 18 TYR B 61 TRP B 98 ASP B 129
SITE 2 AC7 5 LYS B 131
SITE 1 AC8 6 ASN B 68 ASP B 70 GLY B 117 THR B 120
SITE 2 AC8 6 SER B 198 TRP B 231
SITE 1 AC9 3 TYR A 237 NAG A 607 ASN B 455
SITE 1 AD1 2 ASN A 17 THR A 24
SITE 1 AD2 3 ILE A 55 ASN A 57 FUL A 604
SITE 1 AD3 3 ASN A 106 ASN A 188 LYS A 190
SITE 1 AD4 5 SER A 53 ASN A 241 ASN A 245 PHE A 278
SITE 2 AD4 5 NAG B 612
SITE 1 AD5 4 PRO A 335 GLY A 336 SER A 338 ASN A 341
SITE 1 AD6 6 TYR A 477 ASN A 481 GLU A 482 GLN A 484
SITE 2 AD6 6 LEU B 88 GLN B 270
SITE 1 AD7 3 ASN A 486 HOH A 702 HOH B 708
SITE 1 AD8 2 ASN B 17 ALA B 101
SITE 1 AD9 1 ASN B 57
SITE 1 AE1 2 ASN B 106 ASN B 188
SITE 1 AE2 5 TYR B 237 ASN B 241 ASN B 245 PHE B 278
SITE 2 AE2 5 NAG B 606
SITE 1 AE3 4 ASN B 256 GLU B 259 HOH B 701 HOH B 716
SITE 1 AE4 3 SER B 338 ASN B 341 HOH B 706
SITE 1 AE5 4 TYR B 477 ASN B 481 GLU B 482 THR B 483
CRYST1 73.681 79.463 228.869 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 0.013572 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012584 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004369 0.00000
TER 4169 LEU A 530
TER 8300 LEU B 530
MASTER 556 0 31 47 30 0 28 6 8733 2 443 90
END |