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HEADER HYDROLASE 20-APR-07 2PM8
TITLE CRYSTAL STRUCTURE OF RECOMBINANT FULL LENGTH HUMAN
TITLE 2 BUTYRYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 5 BUTYRYLCHOLINE ESTERASE, 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 GENE: BCHE, CHE1;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER
KEYWDS CHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.N.NGAMELUE,K.HOMMA,O.LOCKRIDGE,O.A.ASOJO
REVDAT 1 25-SEP-07 2PM8 0
JRNL AUTH M.N.NGAMELUE,K.HOMMA,O.LOCKRIDGE,O.A.ASOJO
JRNL TITL CRYSTALLIZATION AND X-RAY STRUCTURE OF FULL-LENGTH
JRNL TITL 2 RECOMBINANT HUMAN BUTYRYLCHOLINESTERASE
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 63 723 2007
JRNL REFN DK ESSN 1744-3091
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 38439
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2027
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2638
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.3020
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 8699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.36000
REMARK 3 B22 (A**2) : -0.36000
REMARK 3 B33 (A**2) : 0.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.980
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.398
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.313
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.960
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.839
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8843 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12003 ; 1.536 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1056 ; 6.835 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 404 ;35.308 ;24.059
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1416 ;19.668 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;18.461 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1281 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6714 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4385 ; 0.233 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5956 ; 0.319 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 348 ; 0.205 ; 0.200
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): 77 ; 0.243 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.316 ; 0.200
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): 5371 ; 0.600 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8502 ; 1.070 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3970 ; 1.230 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3500 ; 2.038 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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: NULL
REMARK 4
REMARK 4 2PM8 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB042531.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38439
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : 0.11600
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54500
REMARK 200 R SYM FOR SHELL (I) : 0.52900
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1XLW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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 1/2-Y,1/2+X,Z
REMARK 290 4555 1/2+Y,1/2-X,Z
REMARK 290 5555 1/2-X,1/2+Y,-Z
REMARK 290 6555 1/2+X,1/2-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 75.40150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 75.40150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 75.40150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 75.40150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 75.40150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.40150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 75.40150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.40150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: TETRAMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 -75.40150
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -75.40150
REMARK 350 BIOMT3 2 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 GLN A 455
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 GLN B 455
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 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
REMARK 500 O HOH B 820 O HOH B 828 1.29
REMARK 500 OD1 ASN A 485 C1 NDG A 678 1.39
REMARK 500 CG ASN A 485 C1 NDG A 678 1.53
REMARK 500 NZ LYS B 103 O HOH B 827 1.70
REMARK 500 NH2 ARG A 509 O HOH A 1038 2.09
REMARK 500 OE1 GLU B 443 O HOH B 822 2.16
REMARK 500 O PHE B 21 NH1 ARG B 135 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS B 528 O2 SO4 A 603 4545 2.18
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 304 CB ASP A 304 CG 0.162
REMARK 500 GLU A 352 CG GLU A 352 CD 0.093
REMARK 500 GLU A 352 CD GLU A 352 OE2 0.081
REMARK 500 GLU B 352 CD GLU B 352 OE2 0.082
REMARK 500
REMARK 500 REMARK: NULL
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU B 49 CA - CB - CG ANGL. DEV. = 14.6 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 LYS A 9 -11.14 -47.96
REMARK 500 ARG A 42 128.06 -39.51
REMARK 500 PHE A 43 -26.85 84.91
REMARK 500 ASP A 54 -142.12 -78.71
REMARK 500 ASP A 87 122.91 -33.85
REMARK 500 LEU A 93 82.88 -67.89
REMARK 500 LYS A 103 114.16 -38.13
REMARK 500 LYS A 105 -116.46 118.40
REMARK 500 ASN A 106 60.97 -152.38
REMARK 500 PHE A 118 2.52 58.50
REMARK 500 PHE A 153 24.63 -140.47
REMARK 500 ALA A 162 65.53 -155.13
REMARK 500 SER A 198 -111.98 61.28
REMARK 500 GLU A 255 -59.91 -128.29
REMARK 500 ASN A 256 99.00 -51.31
REMARK 500 VAL A 294 99.75 -64.85
REMARK 500 ASP A 297 -65.47 -99.82
REMARK 500 PHE A 298 -81.19 -66.41
REMARK 500 ASN A 342 12.26 -64.27
REMARK 500 SER A 343 25.71 44.27
REMARK 500 ASP A 379 52.15 -56.57
REMARK 500 GLN A 380 -73.29 -103.78
REMARK 500 ARG A 381 112.02 -32.74
REMARK 500 ASN A 384 -66.75 -29.31
REMARK 500 PHE A 398 -51.43 -131.37
REMARK 500 TRP A 412 31.06 -95.64
REMARK 500 GLU A 422 17.45 -147.06
REMARK 500 PRO A 449 0.34 -63.89
REMARK 500 GLU A 451 90.20 -62.46
REMARK 500 PRO A 480 47.84 -82.79
REMARK 500 GLN A 484 -88.77 -81.32
REMARK 500 ASN A 485 97.60 -43.79
REMARK 500 GLN A 486 99.36 -30.29
REMARK 500 SER A 487 -169.98 -100.05
REMARK 500 THR A 496 -72.54 -73.68
REMARK 500 GLN A 498 62.74 65.57
REMARK 500 GLU A 506 13.03 -144.08
REMARK 500 SER A 507 100.97 172.91
REMARK 500 SER A 524 -62.33 -136.61
REMARK 500 PHE B 21 70.52 33.92
REMARK 500 PHE B 43 -20.52 65.12
REMARK 500 ALA B 58 61.23 -109.52
REMARK 500 ALA B 62 -167.18 -102.67
REMARK 500 MET B 81 -15.48 -48.87
REMARK 500 SER B 89 148.98 168.26
REMARK 500 LEU B 93 76.93 -61.95
REMARK 500 LYS B 105 -69.18 109.53
REMARK 500 ASN B 106 49.80 142.63
REMARK 500 PHE B 118 16.31 57.07
REMARK 500 ALA B 150 -36.52 -36.35
REMARK 500 ASN B 159 108.40 -56.45
REMARK 500 ASN B 181 -50.36 -129.47
REMARK 500 SER B 198 -107.09 24.67
REMARK 500 SER B 215 74.46 -118.62
REMARK 500 LEU B 216 -2.50 -146.74
REMARK 500 CYS B 252 -2.63 -36.67
REMARK 500 ARG B 254 -165.94 -121.80
REMARK 500 GLU B 255 -68.04 -104.92
REMARK 500 ASP B 268 135.68 -36.09
REMARK 500 TYR B 282 -99.39 -118.77
REMARK 500 ILE B 344 92.22 -68.68
REMARK 500 ARG B 347 -47.41 -27.00
REMARK 500 SER B 362 152.06 -46.20
REMARK 500 ASP B 379 32.95 -81.24
REMARK 500 GLN B 380 -83.98 -81.51
REMARK 500 ARG B 381 118.15 -26.45
REMARK 500 ASN B 384 -74.41 -46.55
REMARK 500 PHE B 398 -61.02 -127.31
REMARK 500 LEU B 428 116.90 -39.47
REMARK 500 GLU B 451 102.51 -53.76
REMARK 500 ARG B 452 1.43 -62.43
REMARK 500 PRO B 480 58.61 -93.73
REMARK 500 GLN B 484 -93.09 -93.78
REMARK 500 ASN B 485 94.66 -35.82
REMARK 500 GLN B 486 83.58 -38.96
REMARK 500 THR B 496 -81.78 -74.29
REMARK 500 GLU B 506 -113.91 -124.07
REMARK 500 SER B 507 90.89 -63.11
REMARK 500 THR B 533 -63.57 -17.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XLW RELATED DB: PDB
REMARK 900 RELATED ID: 1VZJ RELATED DB: PDB
REMARK 900 RELATED ID: 1XLU RELATED DB: PDB
REMARK 900 RELATED ID: 1P01 RELATED DB: PDB
REMARK 900 RELATED ID: 1XLV RELATED DB: PDB
REMARK 900 RELATED ID: 2CEK RELATED DB: PDB
DBREF 2PM8 A 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 2PM8 B 1 574 UNP P06276 CHLE_HUMAN 29 602
SEQADV 2PM8 GLN A 17 UNP P06276 ASN 45 CONFLICT
SEQADV 2PM8 GLN A 455 UNP P06276 ASN 483 CONFLICT
SEQADV 2PM8 GLN A 481 UNP P06276 ASN 509 CONFLICT
SEQADV 2PM8 GLN A 486 UNP P06276 ASN 514 CONFLICT
SEQADV 2PM8 GLN B 17 UNP P06276 ASN 45 CONFLICT
SEQADV 2PM8 GLN B 455 UNP P06276 ASN 483 CONFLICT
SEQADV 2PM8 GLN B 481 UNP P06276 ASN 509 CONFLICT
SEQADV 2PM8 GLN B 486 UNP P06276 ASN 514 CONFLICT
SEQRES 1 A 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 574 ARG GLY MET GLN 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 GLN
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 GLN
SEQRES 38 A 574 GLU THR GLN ASN GLN 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 GLN 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 GLN
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 GLN
SEQRES 38 B 574 GLU THR GLN ASN GLN 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
MODRES 2PM8 ASN A 57 ASN GLYCOSYLATION SITE
MODRES 2PM8 ASN A 106 ASN GLYCOSYLATION SITE
MODRES 2PM8 ASN A 341 ASN GLYCOSYLATION SITE
MODRES 2PM8 ASN B 106 ASN GLYCOSYLATION SITE
MODRES 2PM8 ASN A 485 ASN GLYCOSYLATION SITE
HET NAG C 781 14
HET NAG C 782 14
HET NAG A 791 14
HET NDG A 678 14
HET NAG A 798 14
HET NAG B 781 14
HET NAG B 791 14
HET SO4 A 601 5
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 606 5
HET SO4 B 601 5
HET SO4 B 602 5
HET GOL A 999 6
HET GOL A 774 6
HET GOL A 777 6
HET GOL B 774 6
HET GOL B 777 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN NAG NAG
FORMUL 3 NAG 6(C8 H15 N O6)
FORMUL 5 NDG C8 H15 N O6
FORMUL 9 SO4 7(O4 S 2-)
FORMUL 16 GOL 5(C3 H8 O3)
FORMUL 21 HOH *94(H2 O)
HELIX 1 1 PHE A 76 MET A 81 1 6
HELIX 2 2 LEU A 125 ASP A 129 5 5
HELIX 3 3 GLY A 130 ARG A 138 1 9
HELIX 4 4 GLY A 149 LEU A 154 1 6
HELIX 5 5 ASN A 165 ILE A 182 1 18
HELIX 6 6 ALA A 183 PHE A 185 5 3
HELIX 7 7 SER A 198 LEU A 208 1 11
HELIX 8 8 SER A 235 THR A 250 1 16
HELIX 9 9 ASN A 256 ASN A 266 1 11
HELIX 10 10 ASP A 268 ALA A 277 1 10
HELIX 11 11 MET A 302 LEU A 309 1 8
HELIX 12 12 GLY A 326 GLY A 333 5 8
HELIX 13 13 THR A 346 PHE A 358 1 13
HELIX 14 14 SER A 362 THR A 374 1 13
HELIX 15 15 GLU A 383 PHE A 398 1 16
HELIX 16 16 PHE A 398 GLU A 411 1 14
HELIX 17 17 PRO A 431 GLY A 435 5 5
HELIX 18 18 GLU A 441 PHE A 446 1 6
HELIX 19 19 GLY A 447 GLU A 451 5 5
HELIX 20 20 THR A 457 GLY A 478 1 22
HELIX 21 21 ARG A 515 SER A 524 1 10
HELIX 22 22 SER A 524 MET A 532 1 9
HELIX 23 23 LEU B 38 ARG B 42 5 5
HELIX 24 24 PHE B 76 MET B 81 1 6
HELIX 25 25 LEU B 125 ASP B 129 5 5
HELIX 26 26 GLY B 130 ARG B 138 1 9
HELIX 27 27 GLY B 149 LEU B 154 1 6
HELIX 28 28 ASN B 165 ILE B 182 1 18
HELIX 29 29 ALA B 183 PHE B 185 5 3
HELIX 30 30 GLU B 197 LEU B 208 1 12
HELIX 31 31 SER B 210 HIS B 214 5 5
HELIX 32 32 SER B 235 THR B 250 1 16
HELIX 33 33 GLU B 257 ARG B 265 1 9
HELIX 34 34 ASP B 268 ALA B 277 1 10
HELIX 35 35 MET B 302 LEU B 309 1 8
HELIX 36 36 ASP B 324 GLY B 333 5 10
HELIX 37 37 THR B 346 PHE B 358 1 13
HELIX 38 38 SER B 362 THR B 374 1 13
HELIX 39 39 GLU B 383 PHE B 398 1 16
HELIX 40 40 PHE B 398 GLU B 411 1 14
HELIX 41 41 PRO B 431 GLY B 435 5 5
HELIX 42 42 GLU B 441 PHE B 446 1 6
HELIX 43 43 GLY B 447 GLU B 451 5 5
HELIX 44 44 THR B 457 GLY B 478 1 22
HELIX 45 45 ARG B 515 SER B 524 1 10
HELIX 46 46 PHE B 526 GLY B 534 1 9
SHEET 1 A 3 ILE A 5 THR A 8 0
SHEET 2 A 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 A 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 B11 MET A 16 VAL A 20 0
SHEET 2 B11 GLY A 23 PRO A 32 -1 O GLY A 23 N VAL A 20
SHEET 3 B11 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 B11 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 B11 ALA A 107 ILE A 113 1 N TRP A 112 O VAL A 142
SHEET 6 B11 GLY A 187 GLU A 197 1 O PHE A 195 N ILE A 111
SHEET 7 B11 ARG A 219 GLN A 223 1 O ILE A 221 N LEU A 194
SHEET 8 B11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 B11 ALA A 416 PHE A 421 1 O PHE A 417 N ILE A 317
SHEET 10 B11 LYS A 499 LEU A 503 1 O LEU A 503 N TYR A 420
SHEET 11 B11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 C 3 ILE B 5 THR B 8 0
SHEET 2 C 3 GLY B 11 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 C 3 ILE B 55 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 D11 MET B 16 VAL B 20 0
SHEET 2 D11 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 D11 TYR B 94 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 4 D11 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 D11 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 D11 GLY B 187 GLY B 196 1 O THR B 193 N ILE B 111
SHEET 7 D11 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 D11 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 D11 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 D11 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 11 D11 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 2.09
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 2.08
LINK ND2 ASN A 57 C1 NAG A 798 1555 1555 1.45
LINK ND2 ASN A 106 C1 NAG A 791 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG C 781 1555 1555 1.44
LINK ND2 ASN B 106 C1 NAG B 791 1555 1555 1.46
LINK O4 NAG C 781 C1 NAG C 782 1555 1555 1.45
LINK ND2 ASN A 485 C1 NDG A 678 1555 1555 1.43
CISPEP 1 ALA A 101 PRO A 102 0 4.11
CISPEP 2 PRO A 104 LYS A 105 0 14.70
CISPEP 3 ALA B 101 PRO B 102 0 5.90
CISPEP 4 PRO B 104 LYS B 105 0 27.05
CRYST1 150.803 150.803 142.120 90.00 90.00 90.00 P 4 21 2 16
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 0.006631 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006631 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007036 0.00000
TER 4222 GLY A 534
TER 8444 GLY B 534
MASTER 519 0 19 46 28 0 0 6 8699 2 180 90
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