HEADER TRANSFERASE 19-FEB-13 4JBF
TITLE CRYSTAL STRUCTURE OF PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FROM ATOPOBIUM
TITLE 2 PARVULUM DSM 20469.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDOGLYCAN GLYCOSYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 505-954;
COMPND 5 EC: 2.4.1.129;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ATOPOBIUM PARVULUM;
SOURCE 3 ORGANISM_COMMON: STREPTOCOCCUS PARVULUS;
SOURCE 4 ORGANISM_TAXID: 521095;
SOURCE 5 STRAIN: DSM 20469;
SOURCE 6 GENE: APAR_1344;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) MAGIC;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG68
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, MCSG, STRUCTURES OF MTB PROTEINS CONFERRING SUSCEPTIBILITY
KEYWDS 3 TO KNOWN MTB INHIBITORS, MTBI, GLYCOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,Z.WAWRZAK,G.MINASOV,L.SHUVALOVA,O.KIRYUKHINA,G.BABNIGG,
AUTHOR 2 E.RUBIN,J.SACCHETTINI,A.JOACHIMIAK,W.F.ANDERSON,MIDWEST CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS (MCSG),STRUCTURES OF MTB PROTEINS CONFERRING
AUTHOR 4 SUSCEPTIBILITY TO KNOWN MTB INHIBITORS (MTBI)
REVDAT 3 24-JAN-18 4JBF 1 AUTHOR JRNL
REVDAT 2 15-NOV-17 4JBF 1 REMARK
REVDAT 1 20-MAR-13 4JBF 0
JRNL AUTH E.V.FILIPPOVA,Z.WAWRZAK,G.MINASOV,L.SHUVALOVA,O.KIRYUKHINA,
JRNL AUTH 2 G.BABNIGG,E.RUBIN,J.SACCHETTINI,A.JOACHIMIAK,W.F.ANDERSON,
JRNL AUTH 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG),
JRNL AUTH 4 STRUCTURES OF MTB PROTEINS CONFERRING SUSCEPTIBILITY TO
JRNL AUTH 5 KNOWN MTB INHIBITORS (MTBI)
JRNL TITL CRYSTAL STRUCTURE OF PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FROM
JRNL TITL 2 ATOPOBIUM PARVULUM DSM 20469.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 75977
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4744
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 254
REMARK 3 BIN FREE R VALUE : 0.4150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5876
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 465
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 57.11000
REMARK 3 B22 (A**2) : -44.57000
REMARK 3 B33 (A**2) : -12.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 19.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.029
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.028
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.349
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6002 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5589 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8183 ; 1.835 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12836 ; 0.840 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 812 ; 3.166 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 217 ;28.309 ;25.115
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 799 ;10.278 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;11.289 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 982 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6971 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1278 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4JBF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000077834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : SI-111 CHANNEL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77602
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.750
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM CHLORIDE, 0.1 M HEPES
REMARK 280 PH 7, 20% PEG 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.08350
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MSE A 473
REMARK 465 HIS A 474
REMARK 465 HIS A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
REMARK 465 HIS A 478
REMARK 465 HIS A 479
REMARK 465 SER A 480
REMARK 465 SER A 481
REMARK 465 GLY A 482
REMARK 465 VAL A 483
REMARK 465 ASP A 484
REMARK 465 LEU A 485
REMARK 465 TRP A 486
REMARK 465 SER A 487
REMARK 465 HIS A 488
REMARK 465 PRO A 489
REMARK 465 GLN A 490
REMARK 465 PHE A 491
REMARK 465 GLU A 492
REMARK 465 LYS A 493
REMARK 465 GLY A 494
REMARK 465 THR A 495
REMARK 465 GLU A 496
REMARK 465 ASN A 497
REMARK 465 LEU A 498
REMARK 465 TYR A 499
REMARK 465 PHE A 500
REMARK 465 GLN A 501
REMARK 465 SER A 502
REMARK 465 ASN A 503
REMARK 465 ALA A 504
REMARK 465 ILE A 505
REMARK 465 ASP A 506
REMARK 465 ALA A 507
REMARK 465 PRO A 508
REMARK 465 ARG A 509
REMARK 465 LEU A 510
REMARK 465 GLN A 511
REMARK 465 ALA A 512
REMARK 465 LEU A 513
REMARK 465 PRO A 514
REMARK 465 THR A 515
REMARK 465 ASN A 516
REMARK 465 ASN A 517
REMARK 465 HIS A 518
REMARK 465 THR A 519
REMARK 465 ILE A 520
REMARK 465 ALA A 521
REMARK 465 LYS A 522
REMARK 465 LYS A 544
REMARK 465 GLY A 548
REMARK 465 GLY A 586
REMARK 465 HIS A 587
REMARK 465 ALA A 588
REMARK 465 ASP A 589
REMARK 465 HIS A 590
REMARK 465 SER A 591
REMARK 465 ILE A 660
REMARK 465 ILE A 661
REMARK 465 GLU A 662
REMARK 465 SER A 663
REMARK 465 GLY A 664
REMARK 465 THR A 665
REMARK 465 GLY A 666
REMARK 465 GLY A 841
REMARK 465 GLU A 897
REMARK 465 GLU A 927
REMARK 465 GLY A 951
REMARK 465 ALA A 952
REMARK 465 ALA A 953
REMARK 465 SER A 954
REMARK 465 MSE B 473
REMARK 465 HIS B 474
REMARK 465 HIS B 475
REMARK 465 HIS B 476
REMARK 465 HIS B 477
REMARK 465 HIS B 478
REMARK 465 HIS B 479
REMARK 465 SER B 480
REMARK 465 SER B 481
REMARK 465 GLY B 482
REMARK 465 VAL B 483
REMARK 465 ASP B 484
REMARK 465 LEU B 485
REMARK 465 TRP B 486
REMARK 465 SER B 487
REMARK 465 HIS B 488
REMARK 465 PRO B 489
REMARK 465 GLN B 490
REMARK 465 PHE B 491
REMARK 465 GLU B 492
REMARK 465 LYS B 493
REMARK 465 GLY B 494
REMARK 465 THR B 495
REMARK 465 GLU B 496
REMARK 465 ASN B 497
REMARK 465 LEU B 498
REMARK 465 TYR B 499
REMARK 465 PHE B 500
REMARK 465 GLN B 501
REMARK 465 SER B 502
REMARK 465 ASN B 503
REMARK 465 ALA B 504
REMARK 465 ILE B 505
REMARK 465 ASP B 506
REMARK 465 ALA B 507
REMARK 465 PRO B 508
REMARK 465 ARG B 509
REMARK 465 LEU B 510
REMARK 465 GLN B 511
REMARK 465 ALA B 512
REMARK 465 LEU B 513
REMARK 465 PRO B 514
REMARK 465 THR B 515
REMARK 465 ASN B 516
REMARK 465 ASN B 517
REMARK 465 HIS B 518
REMARK 465 THR B 519
REMARK 465 ILE B 520
REMARK 465 ALA B 521
REMARK 465 LYS B 522
REMARK 465 LYS B 544
REMARK 465 GLY B 548
REMARK 465 THR B 549
REMARK 465 TYR B 550
REMARK 465 GLY B 586
REMARK 465 HIS B 587
REMARK 465 ALA B 588
REMARK 465 ASP B 589
REMARK 465 HIS B 590
REMARK 465 SER B 591
REMARK 465 ASP B 592
REMARK 465 ASN B 604
REMARK 465 ILE B 661
REMARK 465 GLU B 662
REMARK 465 SER B 663
REMARK 465 GLY B 664
REMARK 465 THR B 665
REMARK 465 GLY B 666
REMARK 465 GLY B 951
REMARK 465 ALA B 952
REMARK 465 ALA B 953
REMARK 465 SER B 954
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 594 CD NE CZ NH1 NH2
REMARK 470 GLU A 711 CG CD OE1 OE2
REMARK 470 PHE A 901 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP B 593 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 593 CZ3 CH2
REMARK 470 ARG B 594 CD NE CZ NH1 NH2
REMARK 470 PHE B 901 CG CD1 CD2 CE1 CE2 CZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 759 NE - CZ - NH1 ANGL. DEV. = 4.2 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 GLU A 541 -158.44 -123.94
REMARK 500 SER A 651 -162.65 -112.77
REMARK 500 ASP A 770 28.05 -144.82
REMARK 500 ASN A 823 33.31 -99.68
REMARK 500 ALA A 894 -158.54 -93.85
REMARK 500 PHE A 901 55.88 -119.91
REMARK 500 GLU B 541 -151.81 -134.48
REMARK 500 SER B 542 143.59 -170.77
REMARK 500 ALA B 560 46.74 38.21
REMARK 500 SER B 651 -164.19 -112.24
REMARK 500 THR B 659 -152.04 -136.64
REMARK 500 ALA B 721 18.50 59.45
REMARK 500 ASP B 770 26.44 -141.01
REMARK 500 ASN B 823 39.58 -98.46
REMARK 500 ALA B 894 -168.92 -105.13
REMARK 500 HIS B 913 70.24 53.58
REMARK 500 ASN B 925 -89.45 -76.26
REMARK 500 GLU B 927 145.92 -38.16
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 PG4 B 1001
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC110119 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: MCSG-APC110119 RELATED DB: TARGETTRACK
DBREF 4JBF A 505 954 UNP C8W8H7 C8W8H7_ATOPD 505 954
DBREF 4JBF B 505 954 UNP C8W8H7 C8W8H7_ATOPD 505 954
SEQADV 4JBF MSE A 473 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 474 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 475 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 476 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 477 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 478 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 479 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER A 480 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER A 481 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLY A 482 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF VAL A 483 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ASP A 484 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF LEU A 485 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF TRP A 486 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER A 487 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS A 488 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF PRO A 489 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLN A 490 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF PHE A 491 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLU A 492 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF LYS A 493 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLY A 494 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF THR A 495 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLU A 496 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ASN A 497 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF LEU A 498 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF TYR A 499 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF PHE A 500 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLN A 501 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER A 502 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ASN A 503 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ALA A 504 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF MSE B 473 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 474 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 475 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 476 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 477 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 478 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 479 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER B 480 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER B 481 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLY B 482 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF VAL B 483 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ASP B 484 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF LEU B 485 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF TRP B 486 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER B 487 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF HIS B 488 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF PRO B 489 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLN B 490 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF PHE B 491 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLU B 492 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF LYS B 493 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLY B 494 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF THR B 495 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLU B 496 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ASN B 497 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF LEU B 498 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF TYR B 499 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF PHE B 500 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF GLN B 501 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF SER B 502 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ASN B 503 UNP C8W8H7 EXPRESSION TAG
SEQADV 4JBF ALA B 504 UNP C8W8H7 EXPRESSION TAG
SEQRES 1 A 482 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 482 TRP SER HIS PRO GLN PHE GLU LYS GLY THR GLU ASN LEU
SEQRES 3 A 482 TYR PHE GLN SER ASN ALA ILE ASP ALA PRO ARG LEU GLN
SEQRES 4 A 482 ALA LEU PRO THR ASN ASN HIS THR ILE ALA LYS SER ALA
SEQRES 5 A 482 TYR VAL GLN ARG GLY ALA ILE ILE THR SER ASP GLY VAL
SEQRES 6 A 482 THR LEU ALA GLU SER VAL LYS GLN ASP ASP GLY THR TYR
SEQRES 7 A 482 VAL ARG ASN TYR PRO HIS ASP GLY MSE ALA SER HIS THR
SEQRES 8 A 482 VAL GLY TYR ILE SER THR GLN TYR GLY THR ALA GLY ILE
SEQRES 9 A 482 GLU SER SER MSE ASN GLU THR LEU THR GLY HIS ALA ASP
SEQRES 10 A 482 HIS SER ASP TRP ARG SER ALA LEU TYR SER MSE ALA GLY
SEQRES 11 A 482 ILE ASN THR THR GLY SER SER VAL VAL LEU THR ILE ASN
SEQRES 12 A 482 SER GLN MSE GLN ALA VAL ALA GLU ALA ALA LEU GLN GLY
SEQRES 13 A 482 TYR SER GLY SER ILE VAL VAL MSE ASP PRO SER THR GLY
SEQRES 14 A 482 ALA VAL LEU ALA LYS ALA SER SER PRO SER TYR THR HIS
SEQRES 15 A 482 ALA GLU LEU GLY THR ILE ILE GLU SER GLY THR GLY SER
SEQRES 16 A 482 GLN LEU VAL ASP ARG THR THR GLN ALA LEU TYR SER PRO
SEQRES 17 A 482 GLY SER SER PHE LYS THR VAL THR LEU ALA ALA GLY ILE
SEQRES 18 A 482 ASP THR HIS LYS THR THR LEU ASP THR THR TYR SER ALA
SEQRES 19 A 482 PRO GLY THR MSE GLU ILE GLY GLY GLY THR ILE HIS ASN
SEQRES 20 A 482 TYR ALA ASN GLU ASP MSE GLY THR ILE PRO LEU ARG GLU
SEQRES 21 A 482 ALA PHE ALA ARG SER SER ASN THR ALA LEU ALA GLN LEU
SEQRES 22 A 482 GLY VAL ALA LEU GLY ALA ASP ASN LEU VAL SER TYR ALA
SEQRES 23 A 482 ARG ALA PHE GLY TYR GLY THR ALA LEU GLY GLN ASP PHE
SEQRES 24 A 482 SER THR THR PRO SER LEU MSE PRO ASN PRO ALA GLU MSE
SEQRES 25 A 482 THR THR TRP GLU LEU ALA TRP ALA SER CYS GLY LEU PRO
SEQRES 26 A 482 VAL GLY GLU HIS ALA SER PRO ALA GLY PRO GLN THR THR
SEQRES 27 A 482 VAL MSE GLN ASN ALA VAL ILE ALA ALA ALA ILE ALA ASN
SEQRES 28 A 482 GLY GLY VAL VAL MSE ASN PRO TYR ILE VAL ASP ARG VAL
SEQRES 29 A 482 LEU SER PRO GLU GLY ALA VAL VAL SER THR THR SER PRO
SEQRES 30 A 482 LYS SER LEU GLY GLN ALA VAL SER ALA ASP THR ALA ALA
SEQRES 31 A 482 GLN VAL ARG GLU ALA MSE LEU GLY VAL VAL GLU SER GLY
SEQRES 32 A 482 THR GLY MSE GLY ALA ARG VAL PRO GLY VAL LYS ILE ALA
SEQRES 33 A 482 GLY LYS THR GLY THR ALA ASP VAL GLU ASN GLY ASN PHE
SEQRES 34 A 482 ASN SER PHE PHE ILE GLY PHE ALA PRO TYR ASP HIS PRO
SEQRES 35 A 482 THR LEU VAL VAL SER VAL VAL ILE GLU GLY ASN GLY GLU
SEQRES 36 A 482 ASN VAL LEU GLY TYR GLY ALA GLN VAL GLY GLY ARG VAL
SEQRES 37 A 482 LEU ALA GLN CYS LEU ASN ILE GLN ALA LEU GLY ALA ALA
SEQRES 38 A 482 SER
SEQRES 1 B 482 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 482 TRP SER HIS PRO GLN PHE GLU LYS GLY THR GLU ASN LEU
SEQRES 3 B 482 TYR PHE GLN SER ASN ALA ILE ASP ALA PRO ARG LEU GLN
SEQRES 4 B 482 ALA LEU PRO THR ASN ASN HIS THR ILE ALA LYS SER ALA
SEQRES 5 B 482 TYR VAL GLN ARG GLY ALA ILE ILE THR SER ASP GLY VAL
SEQRES 6 B 482 THR LEU ALA GLU SER VAL LYS GLN ASP ASP GLY THR TYR
SEQRES 7 B 482 VAL ARG ASN TYR PRO HIS ASP GLY MSE ALA SER HIS THR
SEQRES 8 B 482 VAL GLY TYR ILE SER THR GLN TYR GLY THR ALA GLY ILE
SEQRES 9 B 482 GLU SER SER MSE ASN GLU THR LEU THR GLY HIS ALA ASP
SEQRES 10 B 482 HIS SER ASP TRP ARG SER ALA LEU TYR SER MSE ALA GLY
SEQRES 11 B 482 ILE ASN THR THR GLY SER SER VAL VAL LEU THR ILE ASN
SEQRES 12 B 482 SER GLN MSE GLN ALA VAL ALA GLU ALA ALA LEU GLN GLY
SEQRES 13 B 482 TYR SER GLY SER ILE VAL VAL MSE ASP PRO SER THR GLY
SEQRES 14 B 482 ALA VAL LEU ALA LYS ALA SER SER PRO SER TYR THR HIS
SEQRES 15 B 482 ALA GLU LEU GLY THR ILE ILE GLU SER GLY THR GLY SER
SEQRES 16 B 482 GLN LEU VAL ASP ARG THR THR GLN ALA LEU TYR SER PRO
SEQRES 17 B 482 GLY SER SER PHE LYS THR VAL THR LEU ALA ALA GLY ILE
SEQRES 18 B 482 ASP THR HIS LYS THR THR LEU ASP THR THR TYR SER ALA
SEQRES 19 B 482 PRO GLY THR MSE GLU ILE GLY GLY GLY THR ILE HIS ASN
SEQRES 20 B 482 TYR ALA ASN GLU ASP MSE GLY THR ILE PRO LEU ARG GLU
SEQRES 21 B 482 ALA PHE ALA ARG SER SER ASN THR ALA LEU ALA GLN LEU
SEQRES 22 B 482 GLY VAL ALA LEU GLY ALA ASP ASN LEU VAL SER TYR ALA
SEQRES 23 B 482 ARG ALA PHE GLY TYR GLY THR ALA LEU GLY GLN ASP PHE
SEQRES 24 B 482 SER THR THR PRO SER LEU MSE PRO ASN PRO ALA GLU MSE
SEQRES 25 B 482 THR THR TRP GLU LEU ALA TRP ALA SER CYS GLY LEU PRO
SEQRES 26 B 482 VAL GLY GLU HIS ALA SER PRO ALA GLY PRO GLN THR THR
SEQRES 27 B 482 VAL MSE GLN ASN ALA VAL ILE ALA ALA ALA ILE ALA ASN
SEQRES 28 B 482 GLY GLY VAL VAL MSE ASN PRO TYR ILE VAL ASP ARG VAL
SEQRES 29 B 482 LEU SER PRO GLU GLY ALA VAL VAL SER THR THR SER PRO
SEQRES 30 B 482 LYS SER LEU GLY GLN ALA VAL SER ALA ASP THR ALA ALA
SEQRES 31 B 482 GLN VAL ARG GLU ALA MSE LEU GLY VAL VAL GLU SER GLY
SEQRES 32 B 482 THR GLY MSE GLY ALA ARG VAL PRO GLY VAL LYS ILE ALA
SEQRES 33 B 482 GLY LYS THR GLY THR ALA ASP VAL GLU ASN GLY ASN PHE
SEQRES 34 B 482 ASN SER PHE PHE ILE GLY PHE ALA PRO TYR ASP HIS PRO
SEQRES 35 B 482 THR LEU VAL VAL SER VAL VAL ILE GLU GLY ASN GLY GLU
SEQRES 36 B 482 ASN VAL LEU GLY TYR GLY ALA GLN VAL GLY GLY ARG VAL
SEQRES 37 B 482 LEU ALA GLN CYS LEU ASN ILE GLN ALA LEU GLY ALA ALA
SEQRES 38 B 482 SER
MODRES 4JBF MSE A 559 MET SELENOMETHIONINE
MODRES 4JBF MSE A 580 MET SELENOMETHIONINE
MODRES 4JBF MSE A 600 MET SELENOMETHIONINE
MODRES 4JBF MSE A 618 MET SELENOMETHIONINE
MODRES 4JBF MSE A 636 MET SELENOMETHIONINE
MODRES 4JBF MSE A 710 MET SELENOMETHIONINE
MODRES 4JBF MSE A 725 MET SELENOMETHIONINE
MODRES 4JBF MSE A 778 MET SELENOMETHIONINE
MODRES 4JBF MSE A 784 MET SELENOMETHIONINE
MODRES 4JBF MSE A 812 MET SELENOMETHIONINE
MODRES 4JBF MSE A 828 MET SELENOMETHIONINE
MODRES 4JBF MSE A 868 MET SELENOMETHIONINE
MODRES 4JBF MSE A 878 MET SELENOMETHIONINE
MODRES 4JBF MSE B 559 MET SELENOMETHIONINE
MODRES 4JBF MSE B 580 MET SELENOMETHIONINE
MODRES 4JBF MSE B 600 MET SELENOMETHIONINE
MODRES 4JBF MSE B 618 MET SELENOMETHIONINE
MODRES 4JBF MSE B 636 MET SELENOMETHIONINE
MODRES 4JBF MSE B 710 MET SELENOMETHIONINE
MODRES 4JBF MSE B 725 MET SELENOMETHIONINE
MODRES 4JBF MSE B 778 MET SELENOMETHIONINE
MODRES 4JBF MSE B 784 MET SELENOMETHIONINE
MODRES 4JBF MSE B 812 MET SELENOMETHIONINE
MODRES 4JBF MSE B 828 MET SELENOMETHIONINE
MODRES 4JBF MSE B 868 MET SELENOMETHIONINE
MODRES 4JBF MSE B 878 MET SELENOMETHIONINE
HET MSE A 559 8
HET MSE A 580 8
HET MSE A 600 8
HET MSE A 618 8
HET MSE A 636 8
HET MSE A 710 8
HET MSE A 725 8
HET MSE A 778 8
HET MSE A 784 8
HET MSE A 812 8
HET MSE A 828 8
HET MSE A 868 8
HET MSE A 878 8
HET MSE B 559 8
HET MSE B 580 8
HET MSE B 600 8
HET MSE B 618 8
HET MSE B 636 8
HET MSE B 710 8
HET MSE B 725 8
HET MSE B 778 8
HET MSE B 784 8
HET MSE B 812 8
HET MSE B 828 8
HET MSE B 868 8
HET MSE B 878 8
HET PG4 B1001 7
HETNAM MSE SELENOMETHIONINE
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 1 MSE 26(C5 H11 N O2 SE)
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *465(H2 O)
HELIX 1 1 ALA A 560 GLY A 565 1 6
HELIX 2 2 GLY A 575 MSE A 580 1 6
HELIX 3 3 MSE A 580 THR A 585 1 6
HELIX 4 4 LEU A 597 SER A 599 5 3
HELIX 5 5 MSE A 600 THR A 605 1 6
HELIX 6 6 ASN A 615 GLN A 627 1 13
HELIX 7 7 HIS A 654 THR A 659 5 6
HELIX 8 8 PRO A 680 SER A 683 5 4
HELIX 9 9 PHE A 684 THR A 695 1 12
HELIX 10 10 TYR A 720 GLU A 723 5 4
HELIX 11 11 LEU A 730 ARG A 736 1 7
HELIX 12 12 SER A 738 GLY A 750 1 13
HELIX 13 13 GLY A 750 PHE A 761 1 12
HELIX 14 14 ASN A 780 MSE A 784 5 5
HELIX 15 15 THR A 785 SER A 793 1 9
HELIX 16 16 THR A 810 ASN A 823 1 14
HELIX 17 17 SER A 857 GLY A 875 1 19
HELIX 18 18 GLY A 877 ARG A 881 5 5
HELIX 19 19 GLY A 931 LEU A 950 1 20
HELIX 20 20 ALA B 560 GLY B 565 1 6
HELIX 21 21 GLY B 575 MSE B 580 1 6
HELIX 22 22 MSE B 580 THR B 585 1 6
HELIX 23 23 TRP B 593 ALA B 601 5 9
HELIX 24 24 ASN B 615 GLN B 627 1 13
HELIX 25 25 HIS B 654 THR B 659 5 6
HELIX 26 26 PRO B 680 SER B 683 5 4
HELIX 27 27 PHE B 684 THR B 695 1 12
HELIX 28 28 TYR B 720 GLU B 723 5 4
HELIX 29 29 LEU B 730 ARG B 736 1 7
HELIX 30 30 SER B 738 GLY B 750 1 13
HELIX 31 31 GLY B 750 PHE B 761 1 12
HELIX 32 32 ASN B 780 MSE B 784 5 5
HELIX 33 33 THR B 785 SER B 793 1 9
HELIX 34 34 THR B 810 ASN B 823 1 14
HELIX 35 35 SER B 857 GLY B 875 1 19
HELIX 36 36 GLY B 877 ARG B 881 5 5
HELIX 37 37 ASP B 895 GLY B 899 5 5
HELIX 38 38 GLY B 931 LEU B 950 1 20
SHEET 1 A 5 THR A 538 ALA A 540 0
SHEET 2 A 5 ILE A 531 ILE A 532 -1 N ILE A 531 O LEU A 539
SHEET 3 A 5 SER A 609 LEU A 612 1 O LEU A 612 N ILE A 532
SHEET 4 A 5 VAL A 833 LEU A 837 -1 O ARG A 835 N VAL A 611
SHEET 5 A 5 VAL A 843 THR A 846 -1 O VAL A 844 N VAL A 836
SHEET 1 B 2 TYR A 566 SER A 568 0
SHEET 2 B 2 GLY A 572 ALA A 574 -1 O GLY A 572 N SER A 568
SHEET 1 C 5 VAL A 643 SER A 649 0
SHEET 2 C 5 SER A 630 MSE A 636 -1 N ILE A 633 O ALA A 647
SHEET 3 C 5 LEU A 916 GLU A 923 -1 O GLU A 923 N SER A 630
SHEET 4 C 5 SER A 903 ALA A 909 -1 N SER A 903 O ILE A 922
SHEET 5 C 5 ALA A 888 THR A 893 -1 N LYS A 890 O ILE A 906
SHEET 1 D 2 THR A 703 SER A 705 0
SHEET 2 D 2 THR A 727 PRO A 729 -1 O ILE A 728 N TYR A 704
SHEET 1 E 2 THR A 709 ILE A 712 0
SHEET 2 E 2 GLY A 715 HIS A 718 -1 O GLY A 715 N ILE A 712
SHEET 1 F 2 VAL A 826 MSE A 828 0
SHEET 2 F 2 SER A 851 GLN A 854 -1 O LEU A 852 N VAL A 827
SHEET 1 G 5 THR B 538 ALA B 540 0
SHEET 2 G 5 ILE B 531 ILE B 532 -1 N ILE B 531 O LEU B 539
SHEET 3 G 5 SER B 609 LEU B 612 1 O LEU B 612 N ILE B 532
SHEET 4 G 5 VAL B 833 LEU B 837 -1 O ARG B 835 N VAL B 611
SHEET 5 G 5 VAL B 843 THR B 846 -1 O VAL B 844 N VAL B 836
SHEET 1 H 2 TYR B 566 SER B 568 0
SHEET 2 H 2 GLY B 572 ALA B 574 -1 O GLY B 572 N SER B 568
SHEET 1 I 5 VAL B 643 SER B 649 0
SHEET 2 I 5 GLY B 631 MSE B 636 -1 N ILE B 633 O ALA B 647
SHEET 3 I 5 LEU B 916 ILE B 922 -1 O SER B 919 N VAL B 634
SHEET 4 I 5 SER B 903 ALA B 909 -1 N GLY B 907 O VAL B 918
SHEET 5 I 5 ALA B 888 THR B 893 -1 N LYS B 890 O ILE B 906
SHEET 1 J 2 THR B 703 SER B 705 0
SHEET 2 J 2 THR B 727 PRO B 729 -1 O ILE B 728 N TYR B 704
SHEET 1 K 2 THR B 709 ILE B 712 0
SHEET 2 K 2 GLY B 715 HIS B 718 -1 O GLY B 715 N ILE B 712
SHEET 1 L 2 VAL B 826 ASN B 829 0
SHEET 2 L 2 LYS B 850 GLN B 854 -1 O LYS B 850 N ASN B 829
LINK C GLY A 558 N MSE A 559 1555 1555 1.34
LINK C MSE A 559 N ALA A 560 1555 1555 1.34
LINK C SER A 579 N MSE A 580 1555 1555 1.33
LINK C MSE A 580 N ASN A 581 1555 1555 1.32
LINK C SER A 599 N MSE A 600 1555 1555 1.32
LINK C MSE A 600 N ALA A 601 1555 1555 1.33
LINK C GLN A 617 N MSE A 618 1555 1555 1.31
LINK C MSE A 618 N GLN A 619 1555 1555 1.34
LINK C VAL A 635 N MSE A 636 1555 1555 1.32
LINK C MSE A 636 N ASP A 637 1555 1555 1.33
LINK C THR A 709 N MSE A 710 1555 1555 1.32
LINK C MSE A 710 N GLU A 711 1555 1555 1.33
LINK C ASP A 724 N MSE A 725 1555 1555 1.33
LINK C MSE A 725 N GLY A 726 1555 1555 1.34
LINK C LEU A 777 N MSE A 778 1555 1555 1.32
LINK C MSE A 778 N PRO A 779 1555 1555 1.34
LINK C GLU A 783 N MSE A 784 1555 1555 1.32
LINK C MSE A 784 N THR A 785 1555 1555 1.32
LINK C VAL A 811 N MSE A 812 1555 1555 1.34
LINK C MSE A 812 N GLN A 813 1555 1555 1.34
LINK C VAL A 827 N MSE A 828 1555 1555 1.33
LINK C MSE A 828 N ASN A 829 1555 1555 1.33
LINK C ALA A 867 N MSE A 868 1555 1555 1.34
LINK C MSE A 868 N LEU A 869 1555 1555 1.31
LINK C GLY A 877 N MSE A 878 1555 1555 1.35
LINK C MSE A 878 N GLY A 879 1555 1555 1.32
LINK C GLY B 558 N MSE B 559 1555 1555 1.33
LINK C MSE B 559 N ALA B 560 1555 1555 1.33
LINK C SER B 579 N MSE B 580 1555 1555 1.32
LINK C MSE B 580 N ASN B 581 1555 1555 1.32
LINK C SER B 599 N MSE B 600 1555 1555 1.32
LINK C MSE B 600 N ALA B 601 1555 1555 1.34
LINK C GLN B 617 N MSE B 618 1555 1555 1.32
LINK C MSE B 618 N GLN B 619 1555 1555 1.34
LINK C VAL B 635 N MSE B 636 1555 1555 1.33
LINK C MSE B 636 N ASP B 637 1555 1555 1.33
LINK C THR B 709 N MSE B 710 1555 1555 1.33
LINK C MSE B 710 N GLU B 711 1555 1555 1.33
LINK C ASP B 724 N MSE B 725 1555 1555 1.34
LINK C MSE B 725 N GLY B 726 1555 1555 1.34
LINK C LEU B 777 N MSE B 778 1555 1555 1.33
LINK C MSE B 778 N PRO B 779 1555 1555 1.33
LINK C GLU B 783 N MSE B 784 1555 1555 1.33
LINK C MSE B 784 N THR B 785 1555 1555 1.32
LINK C VAL B 811 N MSE B 812 1555 1555 1.34
LINK C MSE B 812 N GLN B 813 1555 1555 1.33
LINK C VAL B 827 N MSE B 828 1555 1555 1.31
LINK C MSE B 828 N ASN B 829 1555 1555 1.33
LINK C ALA B 867 N MSE B 868 1555 1555 1.33
LINK C MSE B 868 N LEU B 869 1555 1555 1.31
LINK C GLY B 877 N MSE B 878 1555 1555 1.32
LINK C MSE B 878 N GLY B 879 1555 1555 1.33
CISPEP 1 SER A 649 PRO A 650 0 1.22
CISPEP 2 GLY A 806 PRO A 807 0 0.69
CISPEP 3 ALA A 909 PRO A 910 0 -3.97
CISPEP 4 SER B 649 PRO B 650 0 2.45
CISPEP 5 GLY B 806 PRO B 807 0 0.56
CISPEP 6 ALA B 909 PRO B 910 0 -5.47
SITE 1 AC1 2 THR B 785 TRP B 787
CRYST1 66.927 70.167 114.820 90.00 97.35 90.00 P 1 21 1 4
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 0.014942 0.000000 0.001927 0.00000
SCALE2 0.000000 0.014252 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008781 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
