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HEADER HYDROLASE 13-JUN-19 6RZN
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL CARBOHYDRATE BINDING MODULE FAMILY
TITLE 2 48 AND FERULIC ACID ESTERASE FROM THE MULTI-ENZYME CE1-GH62-GH10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULIC ACID ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.73;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THE ELECTRON DENSITY IS LACKING FOR THE N-TERMINAL AND
COMPND 7 TWO LOOPS.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FERULIC ACID ESTEREASE, CARBOHYDRATE ESTERASE FAMILY 1, CE1, CBM48,
KEYWDS 2 CARBOHYDRATE BINDING MODULE FAMILY 48, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FREDSLUND,D.H.WELNER,C.WILKENS
REVDAT 1 25-SEP-19 6RZN 0
JRNL AUTH J.HOLCK,F.FREDSLUND,M.S.MOELLER,J.BRASK,K.B.R.M.KROGH,
JRNL AUTH 2 L.LANGE,D.H.WELNER,B.SVENSSON,S.JANECEK,C.WILKENS
JRNL TITL CARBOHYDRATE BINDING MODULE OF FAMILY 48 ENABLES ACTION OF
JRNL TITL 2 FERULIC ACID ESTERASES ON POLYMERIC ARABINOXYLAN
JRNL REF J.BIOL.CHEM. 2019
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.310
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 68019
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 3488
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 54.8864 - 5.5738 0.96 2703 155 0.1944 0.1975
REMARK 3 2 5.5738 - 4.4247 0.99 2685 142 0.1545 0.1529
REMARK 3 3 4.4247 - 3.8656 0.99 2643 135 0.1493 0.1544
REMARK 3 4 3.8656 - 3.5122 0.99 2637 147 0.1578 0.1774
REMARK 3 5 3.5122 - 3.2605 0.99 2604 169 0.1631 0.2011
REMARK 3 6 3.2605 - 3.0683 0.97 2568 119 0.1786 0.1901
REMARK 3 7 3.0683 - 2.9146 0.93 2453 149 0.1728 0.2554
REMARK 3 8 2.9146 - 2.7878 0.98 2569 133 0.1749 0.1922
REMARK 3 9 2.7878 - 2.6804 0.98 2578 136 0.1677 0.2076
REMARK 3 10 2.6804 - 2.5880 0.98 2573 151 0.1659 0.2096
REMARK 3 11 2.5880 - 2.5070 0.99 2554 137 0.1725 0.1932
REMARK 3 12 2.5070 - 2.4354 0.99 2557 135 0.1714 0.2276
REMARK 3 13 2.4354 - 2.3713 0.98 2593 139 0.1762 0.2237
REMARK 3 14 2.3713 - 2.3134 0.98 2550 161 0.1706 0.2319
REMARK 3 15 2.3134 - 2.2608 0.98 2517 122 0.1759 0.2095
REMARK 3 16 2.2608 - 2.2127 0.98 2569 136 0.1801 0.2301
REMARK 3 17 2.2127 - 2.1684 0.99 2590 125 0.1845 0.2074
REMARK 3 18 2.1684 - 2.1275 0.99 2559 119 0.1841 0.2188
REMARK 3 19 2.1275 - 2.0895 0.99 2598 128 0.1908 0.2385
REMARK 3 20 2.0895 - 2.0541 0.99 2583 135 0.1994 0.2533
REMARK 3 21 2.0541 - 2.0210 0.99 2567 156 0.2155 0.2531
REMARK 3 22 2.0210 - 1.9899 1.00 2540 142 0.2182 0.2733
REMARK 3 23 1.9899 - 1.9606 1.00 2599 132 0.2240 0.2579
REMARK 3 24 1.9606 - 1.9330 1.00 2571 138 0.2251 0.2649
REMARK 3 25 1.9330 - 1.9069 1.00 2571 147 0.2275 0.2471
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 5500
REMARK 3 ANGLE : 0.623 7447
REMARK 3 CHIRALITY : 0.046 788
REMARK 3 PLANARITY : 0.004 965
REMARK 3 DIHEDRAL : 11.239 3225
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6RZN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-19.
REMARK 100 THE DEPOSITION ID IS D_1292102768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-AUG-18
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68057
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.907
REMARK 200 RESOLUTION RANGE LOW (A) : 54.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.7300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.1
REMARK 200 STARTING MODEL: 1JT2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM SULFATE, 50 MM BIS
REMARK 280 -TRIS/HCL 6.5,30 % (V/V) PENTAERYTHRITOL ETHOXYLATE (15/4_EO/OH,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.82500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.64000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.64000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.82500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.95000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLN A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 PRO A 10
REMARK 465 GLY A 11
REMARK 465 ALA A 12
REMARK 465 ARG A 13
REMARK 465 PRO A 14
REMARK 465 GLY A 15
REMARK 465 PHE A 16
REMARK 465 ARG A 17
REMARK 465 ALA A 18
REMARK 465 PRO A 19
REMARK 465 ALA A 20
REMARK 465 ARG A 21
REMARK 465 PRO A 223
REMARK 465 VAL A 224
REMARK 465 THR A 225
REMARK 465 GLN A 226
REMARK 465 GLY A 227
REMARK 465 GLN A 228
REMARK 465 GLN A 229
REMARK 465 GLY A 230
REMARK 465 ILE A 231
REMARK 465 PRO A 232
REMARK 465 SER A 233
REMARK 465 GLY A 234
REMARK 465 SER A 235
REMARK 465 GLY A 236
REMARK 465 MET A 237
REMARK 465 MET A 300
REMARK 465 ALA A 301
REMARK 465 GLY A 302
REMARK 465 ARG A 303
REMARK 465 GLN A 304
REMARK 465 GLN A 305
REMARK 465 GLY A 306
REMARK 465 ALA A 307
REMARK 465 ASP A 308
REMARK 465 ALA A 309
REMARK 465 GLU A 310
REMARK 465 LYS A 311
REMARK 465 GLN B 1
REMARK 465 VAL B 2
REMARK 465 THR B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 PRO B 6
REMARK 465 GLU B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 PRO B 10
REMARK 465 GLY B 11
REMARK 465 ALA B 12
REMARK 465 ARG B 13
REMARK 465 PRO B 14
REMARK 465 GLY B 15
REMARK 465 PHE B 16
REMARK 465 ARG B 17
REMARK 465 ALA B 18
REMARK 465 PRO B 19
REMARK 465 ALA B 20
REMARK 465 ARG B 21
REMARK 465 PRO B 223
REMARK 465 VAL B 224
REMARK 465 THR B 225
REMARK 465 GLN B 226
REMARK 465 GLY B 227
REMARK 465 GLN B 228
REMARK 465 GLN B 229
REMARK 465 GLY B 230
REMARK 465 ILE B 231
REMARK 465 PRO B 232
REMARK 465 SER B 233
REMARK 465 GLY B 234
REMARK 465 SER B 235
REMARK 465 GLY B 236
REMARK 465 MET B 237
REMARK 465 MET B 300
REMARK 465 ALA B 301
REMARK 465 GLY B 302
REMARK 465 ARG B 303
REMARK 465 GLN B 304
REMARK 465 GLN B 305
REMARK 465 GLY B 306
REMARK 465 ALA B 307
REMARK 465 ASP B 308
REMARK 465 ALA B 309
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 OE2 GLU B 321 HD1 HIS B 355 1.57
REMARK 500 O HOH B 823 O HOH B 836 1.98
REMARK 500 OG1 THR A 238 O HOH A 401 2.00
REMARK 500 O HOH B 664 O HOH B 774 2.01
REMARK 500 O HOH A 768 O HOH A 834 2.02
REMARK 500 O HOH B 625 O HOH B 674 2.02
REMARK 500 O HOH A 570 O HOH A 734 2.02
REMARK 500 O HOH B 786 O HOH B 828 2.04
REMARK 500 O HOH B 747 O HOH B 831 2.04
REMARK 500 O HOH B 691 O HOH B 739 2.04
REMARK 500 O HOH A 597 O HOH A 669 2.05
REMARK 500 O HOH A 420 O HOH B 582 2.06
REMARK 500 O HOH A 806 O HOH A 831 2.06
REMARK 500 O HOH B 537 O HOH B 813 2.07
REMARK 500 O HOH A 702 O HOH A 771 2.07
REMARK 500 O HOH B 413 O HOH B 739 2.08
REMARK 500 O HOH B 516 O HOH B 558 2.08
REMARK 500 O HOH A 855 O HOH A 857 2.10
REMARK 500 O HOH B 582 O HOH B 602 2.12
REMARK 500 O HOH B 728 O HOH B 754 2.13
REMARK 500 O HOH B 755 O HOH B 782 2.15
REMARK 500 O HOH A 423 O HOH A 433 2.15
REMARK 500 O HOH A 438 O HOH A 578 2.16
REMARK 500 O HOH B 796 O HOH B 854 2.19
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 708 O HOH B 402 3656 2.00
REMARK 500 O HOH A 837 O HOH B 772 1455 2.16
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 79 168.50 177.80
REMARK 500 SER A 272 -116.44 49.89
REMARK 500 SER B 39 118.81 -166.69
REMARK 500 GLU B 79 168.02 177.68
REMARK 500 SER B 272 -117.75 52.87
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 859 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 860 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A 861 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 862 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A 863 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A 864 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A 865 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 866 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 867 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH A 868 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH B 868 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B 869 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B 870 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH B 871 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 872 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B 873 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH B 874 DISTANCE = 7.55 ANGSTROMS
DBREF 6RZN A 1 386 PDB 6RZN 6RZN 1 386
DBREF 6RZN B 1 386 PDB 6RZN 6RZN 1 386
SEQRES 1 A 386 GLN VAL THR PRO ARG PRO GLU ALA ALA PRO GLY ALA ARG
SEQRES 2 A 386 PRO GLY PHE ARG ALA PRO ALA ARG ILE ILE SER PRO GLU
SEQRES 3 A 386 ILE MET PRO ASP ASN LYS VAL THR PHE ARG VAL TYR SER
SEQRES 4 A 386 LYS ASP ALA SER LYS VAL THR ILE THR GLY GLU TRP GLN
SEQRES 5 A 386 THR GLY PRO GLY GLY VAL GLU GLU LEU VAL LYS ASN ASP
SEQRES 6 A 386 THR GLY MET PHE SER ILE THR VAL GLY PRO LEU LYS PRO
SEQRES 7 A 386 GLU LEU TYR ALA TYR ASN PHE THR VAL ASP GLY VAL LYS
SEQRES 8 A 386 ALA LEU ASP ALA ASN ASN VAL GLN VAL ARG ARG ASP GLY
SEQRES 9 A 386 THR ASN TYR GLN ASN PHE PHE ILE ILE PRO GLY PRO GLU
SEQRES 10 A 386 SER ASP LEU TYR PHE HIS LYS ASN ASN VAL PRO HIS GLY
SEQRES 11 A 386 THR VAL THR LYS VAL TRP TYR LYS SER SER VAL ILE GLY
SEQRES 12 A 386 PHE ASP ARG ARG MET TYR VAL TYR THR PRO ALA GLY TYR
SEQRES 13 A 386 GLU GLY ASP THR GLN ARG TYR PRO VAL PHE TYR LEU LEU
SEQRES 14 A 386 HIS GLY ALA GLY GLY ASP GLU ASP ALA TRP THR ASN MET
SEQRES 15 A 386 GLY ARG THR ALA GLN ILE MET ASP ASN LEU ILE ALA GLN
SEQRES 16 A 386 GLY LYS ALA LYS PRO MET ILE VAL VAL MET THR ASN GLY
SEQRES 17 A 386 ASN ALA ASN GLN ALA GLY ALA GLN ASN GLU VAL PRO PRO
SEQRES 18 A 386 VAL PRO VAL THR GLN GLY GLN GLN GLY ILE PRO SER GLY
SEQRES 19 A 386 SER GLY MET THR GLY LYS PHE GLU GLU HIS LEU VAL LYS
SEQRES 20 A 386 ASP VAL VAL PRO PHE ILE GLU LYS ASN PHE ARG ALA LEU
SEQRES 21 A 386 THR GLY LYS ASP ASN ARG ALA ILE ALA GLY LEU SER MET
SEQRES 22 A 386 GLY GLY GLY HIS THR GLN THR ILE THR ASN ASP ASN PRO
SEQRES 23 A 386 GLY MET PHE SER TYR ILE GLY VAL PHE SER MET GLY ILE
SEQRES 24 A 386 MET ALA GLY ARG GLN GLN GLY ALA ASP ALA GLU LYS ILE
SEQRES 25 A 386 GLU LYS GLU ARG ASP ALA LYS ILE GLU ALA LEU LYS LYS
SEQRES 26 A 386 SER GLY TYR LYS LEU TYR TRP ILE ALA CYS GLY LYS ASP
SEQRES 27 A 386 ASP PHE VAL TYR GLN SER ALA LEU THR LEU ARG ASN THR
SEQRES 28 A 386 LEU ASP LYS HIS ASN PHE LYS TYR VAL TYR ARG GLU SER
SEQRES 29 A 386 THR GLY GLY HIS THR TRP ALA ASN TRP ARG ILE TYR LEU
SEQRES 30 A 386 SER GLU PHE ALA PRO MET LEU PHE LYS
SEQRES 1 B 386 GLN VAL THR PRO ARG PRO GLU ALA ALA PRO GLY ALA ARG
SEQRES 2 B 386 PRO GLY PHE ARG ALA PRO ALA ARG ILE ILE SER PRO GLU
SEQRES 3 B 386 ILE MET PRO ASP ASN LYS VAL THR PHE ARG VAL TYR SER
SEQRES 4 B 386 LYS ASP ALA SER LYS VAL THR ILE THR GLY GLU TRP GLN
SEQRES 5 B 386 THR GLY PRO GLY GLY VAL GLU GLU LEU VAL LYS ASN ASP
SEQRES 6 B 386 THR GLY MET PHE SER ILE THR VAL GLY PRO LEU LYS PRO
SEQRES 7 B 386 GLU LEU TYR ALA TYR ASN PHE THR VAL ASP GLY VAL LYS
SEQRES 8 B 386 ALA LEU ASP ALA ASN ASN VAL GLN VAL ARG ARG ASP GLY
SEQRES 9 B 386 THR ASN TYR GLN ASN PHE PHE ILE ILE PRO GLY PRO GLU
SEQRES 10 B 386 SER ASP LEU TYR PHE HIS LYS ASN ASN VAL PRO HIS GLY
SEQRES 11 B 386 THR VAL THR LYS VAL TRP TYR LYS SER SER VAL ILE GLY
SEQRES 12 B 386 PHE ASP ARG ARG MET TYR VAL TYR THR PRO ALA GLY TYR
SEQRES 13 B 386 GLU GLY ASP THR GLN ARG TYR PRO VAL PHE TYR LEU LEU
SEQRES 14 B 386 HIS GLY ALA GLY GLY ASP GLU ASP ALA TRP THR ASN MET
SEQRES 15 B 386 GLY ARG THR ALA GLN ILE MET ASP ASN LEU ILE ALA GLN
SEQRES 16 B 386 GLY LYS ALA LYS PRO MET ILE VAL VAL MET THR ASN GLY
SEQRES 17 B 386 ASN ALA ASN GLN ALA GLY ALA GLN ASN GLU VAL PRO PRO
SEQRES 18 B 386 VAL PRO VAL THR GLN GLY GLN GLN GLY ILE PRO SER GLY
SEQRES 19 B 386 SER GLY MET THR GLY LYS PHE GLU GLU HIS LEU VAL LYS
SEQRES 20 B 386 ASP VAL VAL PRO PHE ILE GLU LYS ASN PHE ARG ALA LEU
SEQRES 21 B 386 THR GLY LYS ASP ASN ARG ALA ILE ALA GLY LEU SER MET
SEQRES 22 B 386 GLY GLY GLY HIS THR GLN THR ILE THR ASN ASP ASN PRO
SEQRES 23 B 386 GLY MET PHE SER TYR ILE GLY VAL PHE SER MET GLY ILE
SEQRES 24 B 386 MET ALA GLY ARG GLN GLN GLY ALA ASP ALA GLU LYS ILE
SEQRES 25 B 386 GLU LYS GLU ARG ASP ALA LYS ILE GLU ALA LEU LYS LYS
SEQRES 26 B 386 SER GLY TYR LYS LEU TYR TRP ILE ALA CYS GLY LYS ASP
SEQRES 27 B 386 ASP PHE VAL TYR GLN SER ALA LEU THR LEU ARG ASN THR
SEQRES 28 B 386 LEU ASP LYS HIS ASN PHE LYS TYR VAL TYR ARG GLU SER
SEQRES 29 B 386 THR GLY GLY HIS THR TRP ALA ASN TRP ARG ILE TYR LEU
SEQRES 30 B 386 SER GLU PHE ALA PRO MET LEU PHE LYS
FORMUL 3 HOH *942(H2 O)
HELIX 1 AA1 GLY A 54 VAL A 58 5 5
HELIX 2 AA2 GLY A 115 PHE A 122 5 8
HELIX 3 AA3 ASP A 177 MET A 182 1 6
HELIX 4 AA4 ARG A 184 GLN A 195 1 12
HELIX 5 AA5 GLY A 239 ASP A 248 1 10
HELIX 6 AA6 ASP A 248 PHE A 257 1 10
HELIX 7 AA7 GLY A 262 ASP A 264 5 3
HELIX 8 AA8 SER A 272 ASN A 285 1 14
HELIX 9 AA9 GLU A 313 LYS A 325 1 13
HELIX 10 AB1 VAL A 341 HIS A 355 1 15
HELIX 11 AB2 THR A 369 ALA A 381 1 13
HELIX 12 AB3 PRO A 382 LEU A 384 5 3
HELIX 13 AB4 GLY B 115 PHE B 122 5 8
HELIX 14 AB5 ASP B 177 MET B 182 1 6
HELIX 15 AB6 ARG B 184 GLN B 195 1 12
HELIX 16 AB7 GLY B 239 ASP B 248 1 10
HELIX 17 AB8 ASP B 248 PHE B 257 1 10
HELIX 18 AB9 GLY B 262 ASP B 264 5 3
HELIX 19 AC1 SER B 272 ASN B 285 1 14
HELIX 20 AC2 LYS B 311 LYS B 325 1 15
HELIX 21 AC3 VAL B 341 HIS B 355 1 15
HELIX 22 AC4 THR B 369 ALA B 381 1 13
HELIX 23 AC5 PRO B 382 LEU B 384 5 3
SHEET 1 AA1 4 GLU A 26 ILE A 27 0
SHEET 2 AA1 4 VAL A 33 TYR A 38 -1 O THR A 34 N GLU A 26
SHEET 3 AA1 4 MET A 68 VAL A 73 -1 O PHE A 69 N VAL A 37
SHEET 4 AA1 4 VAL A 62 LYS A 63 -1 N VAL A 62 O SER A 70
SHEET 1 AA2 4 GLU A 59 GLU A 60 0
SHEET 2 AA2 4 VAL A 45 GLY A 49 -1 N ILE A 47 O GLU A 59
SHEET 3 AA2 4 LEU A 80 VAL A 87 -1 O ASN A 84 N THR A 48
SHEET 4 AA2 4 VAL A 90 ALA A 92 -1 O VAL A 90 N VAL A 87
SHEET 1 AA3 5 GLU A 59 GLU A 60 0
SHEET 2 AA3 5 VAL A 45 GLY A 49 -1 N ILE A 47 O GLU A 59
SHEET 3 AA3 5 LEU A 80 VAL A 87 -1 O ASN A 84 N THR A 48
SHEET 4 AA3 5 ASN A 106 ILE A 112 -1 O PHE A 111 N TYR A 81
SHEET 5 AA3 5 VAL A 100 ASP A 103 -1 N ARG A 101 O GLN A 108
SHEET 1 AA416 VAL A 360 SER A 364 0
SHEET 2 AA416 LEU A 330 GLY A 336 1 N ILE A 333 O ARG A 362
SHEET 3 AA416 TYR A 291 PHE A 295 1 N ILE A 292 O TRP A 332
SHEET 4 AA416 ARG A 266 LEU A 271 1 N GLY A 270 O PHE A 295
SHEET 5 AA416 VAL A 165 LEU A 169 1 N TYR A 167 O ALA A 267
SHEET 6 AA416 ILE A 202 MET A 205 1 O ILE A 202 N PHE A 166
SHEET 7 AA416 ARG A 146 THR A 152 -1 N TYR A 151 O VAL A 203
SHEET 8 AA416 THR A 131 TYR A 137 -1 N THR A 133 O VAL A 150
SHEET 9 AA416 THR B 131 TYR B 137 -1 O VAL B 132 N LYS A 134
SHEET 10 AA416 ARG B 146 THR B 152 -1 O VAL B 150 N THR B 133
SHEET 11 AA416 ILE B 202 MET B 205 -1 O MET B 205 N TYR B 149
SHEET 12 AA416 VAL B 165 LEU B 169 1 N PHE B 166 O ILE B 202
SHEET 13 AA416 ARG B 266 LEU B 271 1 O ALA B 267 N TYR B 167
SHEET 14 AA416 TYR B 291 PHE B 295 1 O PHE B 295 N GLY B 270
SHEET 15 AA416 LEU B 330 GLY B 336 1 O TRP B 332 N ILE B 292
SHEET 16 AA416 VAL B 360 SER B 364 1 O VAL B 360 N ILE B 333
SHEET 1 AA5 4 GLU B 26 ILE B 27 0
SHEET 2 AA5 4 VAL B 33 TYR B 38 -1 O THR B 34 N GLU B 26
SHEET 3 AA5 4 MET B 68 VAL B 73 -1 O PHE B 69 N VAL B 37
SHEET 4 AA5 4 VAL B 62 LYS B 63 -1 N VAL B 62 O SER B 70
SHEET 1 AA6 4 GLU B 59 GLU B 60 0
SHEET 2 AA6 4 VAL B 45 GLY B 49 -1 N ILE B 47 O GLU B 59
SHEET 3 AA6 4 GLU B 79 VAL B 87 -1 O ASN B 84 N THR B 48
SHEET 4 AA6 4 VAL B 90 ALA B 92 -1 O VAL B 90 N VAL B 87
SHEET 1 AA7 5 GLU B 59 GLU B 60 0
SHEET 2 AA7 5 VAL B 45 GLY B 49 -1 N ILE B 47 O GLU B 59
SHEET 3 AA7 5 GLU B 79 VAL B 87 -1 O ASN B 84 N THR B 48
SHEET 4 AA7 5 ASN B 106 ILE B 113 -1 O PHE B 111 N TYR B 81
SHEET 5 AA7 5 VAL B 100 ASP B 103 -1 N ARG B 101 O GLN B 108
CISPEP 1 SER A 24 PRO A 25 0 -1.83
CISPEP 2 GLY A 74 PRO A 75 0 5.49
CISPEP 3 SER B 24 PRO B 25 0 -1.79
CISPEP 4 GLY B 74 PRO B 75 0 4.05
CRYST1 65.650 99.900 133.280 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015232 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007503 0.00000
TER 5274 LYS A 386
TER 10592 LYS B 386
MASTER 422 0 0 23 42 0 0 6 6308 2 0 60
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