| 6goc-pdb | HEADER CARBOHYDRATE 01-JUN-18 6GOC
TITLE METHYLESTERASE BT1017
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DUF3826 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 GENE: BJP75_005780, BTHETA7330_02632;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PECTIN, RHAMNOGALACTURONAN-II, METHYLESTERASE, HUMAN GUT MICROBIOTA,
KEYWDS 2 CARBOHYDRATE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BASLE,D.NDEH,H.GILBERT
REVDAT 1 19-JUN-19 6GOC 0
JRNL AUTH D.NDHE,D.CHENG-JIE,A.BASLE,H.GILBERT
JRNL TITL CHARACTERISATION OF A METHYLESTERASES ESSENTIAL FOR PECTIN
JRNL TITL 2 RHAMNOGALACTURONAN II METABOLISM FROM THE GUT BACTERIUM
JRNL TITL 3 BACTEROIDES THETAIOTAOMICRON
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 48044
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2524
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3478
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.4040
REMARK 3 BIN FREE R VALUE SET COUNT : 197
REMARK 3 BIN FREE R VALUE : 0.3940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3473
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.75000
REMARK 3 B22 (A**2) : -3.76000
REMARK 3 B33 (A**2) : 1.01000
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): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.796
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3549 ; 0.013 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 3159 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4800 ; 1.607 ; 1.672
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7405 ; 1.030 ; 1.666
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 443 ; 6.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 191 ;32.051 ;21.885
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 569 ;13.962 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;19.151 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 454 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4037 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 679 ; 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): 1775 ; 2.776 ; 3.312
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1774 ; 2.773 ; 3.310
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2217 ; 3.647 ; 4.960
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2218 ; 3.646 ; 4.962
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1774 ; 3.634 ; 3.632
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1772 ; 3.622 ; 3.627
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2583 ; 5.191 ; 5.294
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4078 ; 6.018 ;39.596
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4048 ; 5.989 ;39.470
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 : NULL
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 6GOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010201.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97889
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50611
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 66.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM 1,6-HEXANEDIOL; 20 MM 1,2
REMARK 280 -PROPANEDIOL; 20 MM 1,4-BUTANEDIOL; 20 MM 1-BUTANOL; 20 MM 2-
REMARK 280 PROPANOL; 20 MM 1,3-PROPANEDIOL; 100 MM IMIDAZOL/MES PH 6.5; 20 %
REMARK 280 ETHYLENE GLYCOL; 10 % PEG 8000K, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.35450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.35450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.25400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 114.73450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.25400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 114.73450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.35450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.25400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 114.73450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.35450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.25400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 114.73450
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/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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1053 LIES ON A SPECIAL POSITION.
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 -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 SER A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 LEU A 9
REMARK 465 VAL A 10
REMARK 465 PRO A 11
REMARK 465 ARG A 12
REMARK 465 GLY A 13
REMARK 465 SER A 14
REMARK 465 HIS A 15
REMARK 465 MSE A 16
REMARK 465 ALA A 17
REMARK 465 SER A 18
REMARK 465 GLN A 19
REMARK 465 ALA A 463
REMARK 465 SER A 464
REMARK 465 LEU A 465
REMARK 465 GLU A 466
REMARK 465 LYS A 467
REMARK 465 LYS A 468
REMARK 465 ALA A 469
REMARK 465 MSE A 470
REMARK 465 GLU A 471
REMARK 465 TRP A 472
REMARK 465 VAL A 473
REMARK 465 ALA A 474
REMARK 465 SER A 475
REMARK 465 LEU A 476
REMARK 465 ASN A 477
REMARK 465 LEU A 478
REMARK 465 ASP A 479
REMARK 465 ASP A 480
REMARK 465 GLU A 481
REMARK 465 LYS A 482
REMARK 465 LYS A 483
REMARK 465 SER A 484
REMARK 465 GLY A 485
REMARK 465 PHE A 486
REMARK 465 ALA A 487
REMARK 465 VAL A 488
REMARK 465 THR A 489
REMARK 465 THR A 490
REMARK 465 ILE A 491
REMARK 465 TYR A 492
REMARK 465 ASN A 493
REMARK 465 HIS A 494
REMARK 465 LEU A 495
REMARK 465 ARG A 496
REMARK 465 GLN A 497
REMARK 465 VAL A 498
REMARK 465 ARG A 499
REMARK 465 ASP A 500
REMARK 465 TRP A 501
REMARK 465 HIS A 502
REMARK 465 ASN A 503
REMARK 465 ASP A 504
REMARK 465 HIS A 505
REMARK 465 PRO A 506
REMARK 465 TYR A 507
REMARK 465 THR A 508
REMARK 465 THR A 509
REMARK 465 ILE A 510
REMARK 465 PRO A 511
REMARK 465 ALA A 512
REMARK 465 GLY A 513
REMARK 465 ILE A 514
REMARK 465 ASN A 515
REMARK 465 PRO A 516
REMARK 465 THR A 517
REMARK 465 THR A 518
REMARK 465 GLY A 519
REMARK 465 LYS A 520
REMARK 465 PRO A 521
REMARK 465 LEU A 522
REMARK 465 THR A 523
REMARK 465 GLN A 524
REMARK 465 LEU A 525
REMARK 465 GLU A 526
REMARK 465 ARG A 527
REMARK 465 GLU A 528
REMARK 465 ILE A 529
REMARK 465 ILE A 530
REMARK 465 ALA A 531
REMARK 465 ASP A 532
REMARK 465 SER A 533
REMARK 465 ALA A 534
REMARK 465 MSE A 535
REMARK 465 PRO A 536
REMARK 465 LYS A 537
REMARK 465 GLU A 538
REMARK 465 VAL A 539
REMARK 465 HIS A 540
REMARK 465 GLU A 541
REMARK 465 ARG A 542
REMARK 465 LEU A 543
REMARK 465 MSE A 544
REMARK 465 LYS A 545
REMARK 465 GLY A 546
REMARK 465 LEU A 547
REMARK 465 ARG A 548
REMARK 465 ARG A 549
REMARK 465 VAL A 550
REMARK 465 LEU A 551
REMARK 465 THR A 552
REMARK 465 GLU A 553
REMARK 465 GLU A 554
REMARK 465 GLN A 555
REMARK 465 VAL A 556
REMARK 465 GLU A 557
REMARK 465 GLN A 558
REMARK 465 ILE A 559
REMARK 465 LEU A 560
REMARK 465 ASP A 561
REMARK 465 LYS A 562
REMARK 465 TYR A 563
REMARK 465 THR A 564
REMARK 465 VAL A 565
REMARK 465 GLY A 566
REMARK 465 LYS A 567
REMARK 465 VAL A 568
REMARK 465 ALA A 569
REMARK 465 PHE A 570
REMARK 465 THR A 571
REMARK 465 MSE A 572
REMARK 465 LYS A 573
REMARK 465 GLY A 574
REMARK 465 TYR A 575
REMARK 465 GLN A 576
REMARK 465 GLU A 577
REMARK 465 ILE A 578
REMARK 465 VAL A 579
REMARK 465 PRO A 580
REMARK 465 ASP A 581
REMARK 465 MSE A 582
REMARK 465 THR A 583
REMARK 465 GLU A 584
REMARK 465 GLU A 585
REMARK 465 GLU A 586
REMARK 465 THR A 587
REMARK 465 ALA A 588
REMARK 465 PHE A 589
REMARK 465 ILE A 590
REMARK 465 LEU A 591
REMARK 465 GLU A 592
REMARK 465 GLN A 593
REMARK 465 LEU A 594
REMARK 465 LYS A 595
REMARK 465 LEU A 596
REMARK 465 ALA A 597
REMARK 465 ARG A 598
REMARK 465 GLU A 599
REMARK 465 GLN A 600
REMARK 465 ALA A 601
REMARK 465 VAL A 602
REMARK 465 ASP A 603
REMARK 465 TYR A 604
REMARK 465 LYS A 605
REMARK 465 SER A 606
REMARK 465 MSE A 607
REMARK 465 LYS A 608
REMARK 465 GLN A 609
REMARK 465 ILE A 610
REMARK 465 SER A 611
REMARK 465 ALA A 612
REMARK 465 ILE A 613
REMARK 465 PHE A 614
REMARK 465 LYS A 615
REMARK 465 ALA A 616
REMARK 465 TYR A 617
REMARK 465 LYS A 618
REMARK 465 THR A 619
REMARK 465 LYS A 620
REMARK 465 ILE A 621
REMARK 465 GLU A 622
REMARK 465 LEU A 623
REMARK 465 TYR A 624
REMARK 465 PHE A 625
REMARK 465 TYR A 626
REMARK 465 GLU A 627
REMARK 465 HIS A 628
REMARK 465 GLY A 629
REMARK 465 ARG A 630
REMARK 465 ASN A 631
REMARK 465 TRP A 632
REMARK 465 ARG A 633
REMARK 465 GLN A 634
REMARK 465 MSE A 635
REMARK 465 TYR A 636
REMARK 465 LYS A 637
REMARK 465 ASP A 638
REMARK 465 TYR A 639
REMARK 465 ALA A 640
REMARK 465 GLU A 641
REMARK 465 LYS A 642
REMARK 465 ARG A 643
REMARK 465 LYS A 644
REMARK 465 ALA A 645
REMARK 465 GLU A 646
REMARK 465 LYS A 647
REMARK 465 ALA A 648
REMARK 465 LYS A 649
REMARK 465 GLU A 650
REMARK 465 GLY A 651
REMARK 465 LYS A 652
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 ASP A 49 CG OD1 OD2
REMARK 470 LYS A 454 CG CD CE NZ
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 OE1 GLU A 134 O HOH A 801 2.08
REMARK 500 NH1 ARG A 45 OD1 ASN A 90 2.13
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 O HOH A 861 O HOH A 861 3555 0.73
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = -4.5 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 ASP A 81 39.97 72.22
REMARK 500 ARG A 102 -166.07 -118.44
REMARK 500 THR A 173 -97.11 -107.33
REMARK 500 HIS A 201 33.69 -80.79
REMARK 500 SER A 282 -120.13 58.55
REMARK 500 SER A 306 -32.13 -143.38
REMARK 500 PRO A 322 47.63 -84.96
REMARK 500 LEU A 360 -72.75 -123.58
REMARK 500 ALA A 374 36.85 -143.95
REMARK 500 ASP A 414 110.28 -164.64
REMARK 500 GLU A 431 -39.59 -37.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 63 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 701 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 201 NE2
REMARK 620 2 HIS A 244 NE2 107.9
REMARK 620 3 CYS A 315 SG 110.0 98.4
REMARK 620 4 CYS A 317 SG 113.9 113.9 111.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 701
DBREF1 6GOC A 19 652 UNP A0A0P0F0R1_BACT4
DBREF2 6GOC A A0A0P0F0R1 19 653
SEQADV 6GOC MSE A -4 UNP A0A0P0F0R INITIATING METHIONINE
SEQADV 6GOC GLY A -3 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC SER A -2 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC SER A -1 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 0 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 1 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 2 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 3 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 4 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 5 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC SER A 6 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC SER A 7 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC GLY A 8 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC LEU A 9 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC VAL A 10 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC PRO A 11 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC ARG A 12 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC GLY A 13 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC SER A 14 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC HIS A 15 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC MSE A 16 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC ALA A 17 UNP A0A0P0F0R EXPRESSION TAG
SEQADV 6GOC SER A 18 UNP A0A0P0F0R EXPRESSION TAG
SEQRES 1 A 658 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 658 LEU VAL PRO ARG GLY SER HIS MSE ALA SER GLN THR GLN
SEQRES 3 A 658 THR TYR GLU THR GLU PHE ALA ARG PRO LEU ASN GLU VAL
SEQRES 4 A 658 LEU THR ASP ILE GLN ASN ARG PHE GLY ILE ARG LEU LYS
SEQRES 5 A 658 TYR ASP ILE ASP THR VAL GLY LYS ILE LEU PRO TYR ALA
SEQRES 6 A 658 ASP PHE ARG ILE ARG PRO TYR SER VAL GLU GLU SER LEU
SEQRES 7 A 658 THR ASN VAL LEU SER PRO PHE ASP TYR LYS PHE VAL ARG
SEQRES 8 A 658 GLN SER GLY ASN LEU TYR LYS LEU LYS ALA TYR GLU TYR
SEQRES 9 A 658 PRO ARG ARG THR ASP ALA ASP GLY GLU LYS MSE LEU ALA
SEQRES 10 A 658 TYR LEU ASN THR LEU TYR ALA ASP LYS GLN ALA PHE GLU
SEQRES 11 A 658 LEU ARG ALA ASP SER LEU ARG LYS GLU VAL ARG GLN ARG
SEQRES 12 A 658 LEU GLY ILE ASP THR LEU LEU ALA GLN CYS VAL ASN SER
SEQRES 13 A 658 THR PRO ILE LEU SER LYS ILE ARG LYS PHE ASP GLY TYR
SEQRES 14 A 658 THR VAL GLN ASN PHE ALA LEU GLU THR LEU PRO GLY LEU
SEQRES 15 A 658 TYR VAL CYS GLY SER VAL TYR THR PRO GLN SER LYS GLY
SEQRES 16 A 658 LYS HIS ALA LEU ILE ILE CYS PRO ASN GLY HIS PHE GLY
SEQRES 17 A 658 GLY GLY ARG TYR ARG GLU ASP GLN GLN GLN ARG MSE GLY
SEQRES 18 A 658 THR LEU ALA ARG MSE GLY ALA VAL CYS VAL ASP TYR ASP
SEQRES 19 A 658 LEU PHE GLY TRP GLY GLU SER ILE LEU GLN VAL GLY SER
SEQRES 20 A 658 THR ALA HIS ARG SER SER ALA ALA HIS THR ILE GLN ALA
SEQRES 21 A 658 MSE ASN GLY LEU LEU ILE LEU ASP TYR MSE LEU ALA SER
SEQRES 22 A 658 ARG LYS ASP ILE ASP THR LYS ARG ILE GLY ALA ASN GLY
SEQRES 23 A 658 GLY SER GLY GLY GLY THR HIS THR VAL LEU LEU THR THR
SEQRES 24 A 658 LEU ASP ASP ARG PHE THR ALA SER ALA PRO VAL VAL SER
SEQRES 25 A 658 LEU ALA SER HIS PHE ASP GLY GLY CYS PRO CYS GLU SER
SEQRES 26 A 658 GLY MSE PRO ILE GLN LEU SER ALA GLY GLY THR CYS ASN
SEQRES 27 A 658 ALA GLU LEU ALA ALA THR PHE ALA PRO ARG PRO GLN LEU
SEQRES 28 A 658 VAL VAL SER ASP GLY GLY ASP TRP THR ALA SER VAL PRO
SEQRES 29 A 658 ALA LEU GLU PHE PRO TYR LEU GLN ARG ILE TYR GLY PHE
SEQRES 30 A 658 TYR ASP ALA LYS ASP ASN VAL THR ASN VAL HIS LEU PRO
SEQRES 31 A 658 LYS GLU LYS HIS ASP PHE GLY PRO ASN LYS ARG ASN ALA
SEQRES 32 A 658 VAL TYR ASP PHE PHE ALA GLU VAL PHE ASP LEU ASP LYS
SEQRES 33 A 658 LYS MSE LEU ASP GLU SER LYS VAL THR ILE GLU PRO GLU
SEQRES 34 A 658 SER ALA MSE TYR SER PHE GLY GLU LYS GLY GLU LEU LEU
SEQRES 35 A 658 PRO GLU ASN ALA ILE ARG SER PHE ASP LYS VAL ALA ALA
SEQRES 36 A 658 TYR PHE ASP LYS LYS ALA PHE ALA LYS LEU LYS SER ASP
SEQRES 37 A 658 ALA SER LEU GLU LYS LYS ALA MSE GLU TRP VAL ALA SER
SEQRES 38 A 658 LEU ASN LEU ASP ASP GLU LYS LYS SER GLY PHE ALA VAL
SEQRES 39 A 658 THR THR ILE TYR ASN HIS LEU ARG GLN VAL ARG ASP TRP
SEQRES 40 A 658 HIS ASN ASP HIS PRO TYR THR THR ILE PRO ALA GLY ILE
SEQRES 41 A 658 ASN PRO THR THR GLY LYS PRO LEU THR GLN LEU GLU ARG
SEQRES 42 A 658 GLU ILE ILE ALA ASP SER ALA MSE PRO LYS GLU VAL HIS
SEQRES 43 A 658 GLU ARG LEU MSE LYS GLY LEU ARG ARG VAL LEU THR GLU
SEQRES 44 A 658 GLU GLN VAL GLU GLN ILE LEU ASP LYS TYR THR VAL GLY
SEQRES 45 A 658 LYS VAL ALA PHE THR MSE LYS GLY TYR GLN GLU ILE VAL
SEQRES 46 A 658 PRO ASP MSE THR GLU GLU GLU THR ALA PHE ILE LEU GLU
SEQRES 47 A 658 GLN LEU LYS LEU ALA ARG GLU GLN ALA VAL ASP TYR LYS
SEQRES 48 A 658 SER MSE LYS GLN ILE SER ALA ILE PHE LYS ALA TYR LYS
SEQRES 49 A 658 THR LYS ILE GLU LEU TYR PHE TYR GLU HIS GLY ARG ASN
SEQRES 50 A 658 TRP ARG GLN MSE TYR LYS ASP TYR ALA GLU LYS ARG LYS
SEQRES 51 A 658 ALA GLU LYS ALA LYS GLU GLY LYS
MODRES 6GOC MSE A 110 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 215 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 221 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 255 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 264 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 321 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 412 MET MODIFIED RESIDUE
MODRES 6GOC MSE A 426 MET MODIFIED RESIDUE
HET MSE A 110 8
HET MSE A 215 8
HET MSE A 221 8
HET MSE A 255 8
HET MSE A 264 8
HET MSE A 321 8
HET MSE A 412 8
HET MSE A 426 8
HET CU A 701 1
HETNAM MSE SELENOMETHIONINE
HETNAM CU COPPER (II) ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 CU CU 2+
FORMUL 3 HOH *279(H2 O)
HELIX 1 AA1 THR A 22 GLU A 26 5 5
HELIX 2 AA2 LEU A 31 GLY A 43 1 13
HELIX 3 AA3 TYR A 59 ILE A 64 5 6
HELIX 4 AA4 SER A 68 SER A 78 1 11
HELIX 5 AA5 THR A 103 THR A 116 1 14
HELIX 6 AA6 ASP A 120 GLY A 140 1 21
HELIX 7 AA7 GLY A 140 ALA A 146 1 7
HELIX 8 AA8 GLY A 204 TYR A 207 5 4
HELIX 9 AA9 ARG A 208 MSE A 221 1 14
HELIX 10 AB1 TRP A 232 GLU A 234 5 3
HELIX 11 AB2 SER A 235 GLY A 240 1 6
HELIX 12 AB3 SER A 241 ARG A 245 5 5
HELIX 13 AB4 SER A 246 ARG A 268 1 23
HELIX 14 AB5 SER A 282 ASP A 295 1 14
HELIX 15 AB6 CYS A 315 GLY A 320 1 6
HELIX 16 AB7 PRO A 322 GLY A 329 5 8
HELIX 17 AB8 CYS A 331 THR A 338 1 8
HELIX 18 AB9 ASP A 352 VAL A 357 5 6
HELIX 19 AC1 LEU A 360 PHE A 371 1 12
HELIX 20 AC2 TYR A 372 ASP A 373 5 2
HELIX 21 AC3 ALA A 374 ASP A 376 5 3
HELIX 22 AC4 GLY A 391 ASP A 407 1 17
HELIX 23 AC5 ASP A 409 LEU A 413 5 5
HELIX 24 AC6 ASP A 414 VAL A 418 5 5
HELIX 25 AC7 PRO A 422 TYR A 427 5 6
HELIX 26 AC8 SER A 443 ALA A 449 1 7
HELIX 27 AC9 ASP A 452 SER A 461 1 10
SHEET 1 AA1 2 ARG A 29 PRO A 30 0
SHEET 2 AA1 2 ILE A 56 LEU A 57 -1 O LEU A 57 N ARG A 29
SHEET 1 AA2 3 ARG A 45 TYR A 48 0
SHEET 2 AA2 3 LEU A 91 ALA A 96 1 O TYR A 92 N LYS A 47
SHEET 3 AA2 3 TYR A 82 ARG A 86 -1 N VAL A 85 O LYS A 93
SHEET 1 AA3 3 ILE A 154 LEU A 155 0
SHEET 2 AA3 3 TYR A 164 GLU A 172 -1 O ALA A 170 N ILE A 154
SHEET 3 AA3 3 ARG A 159 PHE A 161 -1 N ARG A 159 O VAL A 166
SHEET 1 AA4 7 ILE A 154 LEU A 155 0
SHEET 2 AA4 7 TYR A 164 GLU A 172 -1 O ALA A 170 N ILE A 154
SHEET 3 AA4 7 TYR A 178 PRO A 186 -1 O VAL A 183 N GLN A 167
SHEET 4 AA4 7 ALA A 223 TYR A 227 -1 O CYS A 224 N TYR A 184
SHEET 5 AA4 7 HIS A 192 CYS A 197 1 N ALA A 193 O VAL A 223A
SHEET 6 AA4 7 ILE A 271 GLY A 281 1 O GLY A 277 N LEU A 194
SHEET 7 AA4 7 ALA A 300 VAL A 304 1 O VAL A 304 N GLY A 280
SHEET 1 AA5 2 GLN A 344 ASP A 349 0
SHEET 2 AA5 2 VAL A 378 LEU A 383 1 O THR A 379 N VAL A 346
LINK C LYS A 109 N MSE A 110 1555 1555 1.34
LINK C MSE A 110 N LEU A 111 1555 1555 1.33
LINK NE2 HIS A 201 CU CU A 701 1555 1555 1.99
LINK C ARG A 214 N MSE A 215 1555 1555 1.33
LINK C MSE A 215 N GLY A 216 1555 1555 1.34
LINK C ARG A 220 N MSE A 221 1555 1555 1.34
LINK C MSE A 221 N GLY A 222 1555 1555 1.34
LINK NE2 HIS A 244 CU CU A 701 1555 1555 2.08
LINK C ALA A 254 N MSE A 255 1555 1555 1.33
LINK C MSE A 255 N ASN A 256 1555 1555 1.34
LINK C TYR A 263 N MSE A 264 1555 1555 1.33
LINK C MSE A 264 N LEU A 265 1555 1555 1.33
LINK SG CYS A 315 CU CU A 701 1555 1555 2.41
LINK SG CYS A 317 CU CU A 701 1555 1555 2.25
LINK C GLY A 320 N MSE A 321 1555 1555 1.34
LINK C MSE A 321 N PRO A 322 1555 1555 1.34
LINK C LYS A 411 N MSE A 412 1555 1555 1.35
LINK C MSE A 412 N LEU A 413 1555 1555 1.33
LINK C ALA A 425 N MSE A 426 1555 1555 1.35
LINK C MSE A 426 N TYR A 427 1555 1555 1.34
CISPEP 1 ALA A 340 PRO A 341 0 5.34
SITE 1 AC1 4 HIS A 201 HIS A 244 CYS A 315 CYS A 317
CRYST1 68.508 229.469 80.709 90.00 90.00 90.00 C 2 2 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 0.014597 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004358 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012390 0.00000
TER 3474 ASP A 462
MASTER 606 0 9 27 17 0 1 6 3753 1 85 51
END
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