HEADER LYASE/INHIBITOR 11-OCT-16 5TLH
TITLE FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE IN COMPLEX WITH
TITLE 2 THE INHIBITOR 2-NAPHTHOL 6-BISPHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRUCTOSE-BISPHOSPHATE ALDOLASE A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MUSCLE-TYPE ALDOLASE;
COMPND 5 EC: 4.1.2.13;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 GENE: ALDOA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(SI);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPB14
KEYWDS INHIBITOR, BISPHOSPHONATE, COMPLEX, ALDOLASE, LYASE, LYASE-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.W.HERON,J.SYGUSCH
REVDAT 4 18-OCT-23 5TLH 1 REMARK
REVDAT 3 09-NOV-22 5TLH 1 JRNL
REVDAT 2 08-JAN-20 5TLH 1 REMARK
REVDAT 1 25-OCT-17 5TLH 0
JRNL AUTH P.W.HERON,M.ABELLAN-FLOS,L.SALMON,J.SYGUSCH
JRNL TITL BISPHOSPHONATE INHIBITORS OF MAMMALIAN GLYCOLYTIC ALDOLASE.
JRNL REF J.MED.CHEM. V. 61 10558 2018
JRNL REFN ISSN 0022-2623
JRNL PMID 30418024
JRNL DOI 10.1021/ACS.JMEDCHEM.8B01000
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 69057
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2012
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 43.9362 - 5.3082 1.00 5062 154 0.1584 0.1647
REMARK 3 2 5.3082 - 4.2144 1.00 5027 150 0.1240 0.1577
REMARK 3 3 4.2144 - 3.6820 1.00 4983 151 0.1277 0.1576
REMARK 3 4 3.6820 - 3.3455 1.00 4963 149 0.1455 0.1796
REMARK 3 5 3.3455 - 3.1057 0.99 4924 150 0.1520 0.1888
REMARK 3 6 3.1057 - 2.9227 0.98 4867 145 0.1519 0.2010
REMARK 3 7 2.9227 - 2.7763 0.97 4797 145 0.1511 0.1933
REMARK 3 8 2.7763 - 2.6555 0.95 4721 144 0.1477 0.1948
REMARK 3 9 2.6555 - 2.5533 0.95 4724 137 0.1520 0.2281
REMARK 3 10 2.5533 - 2.4652 0.94 4669 144 0.1578 0.2166
REMARK 3 11 2.4652 - 2.3881 0.94 4681 135 0.1653 0.2283
REMARK 3 12 2.3881 - 2.3198 0.94 4681 139 0.1770 0.2015
REMARK 3 13 2.3198 - 2.2588 0.94 4670 139 0.1957 0.2569
REMARK 3 14 2.2588 - 2.2037 0.86 4276 130 0.2225 0.2771
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.88
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 : 0.005 11009
REMARK 3 ANGLE : 0.858 14943
REMARK 3 CHIRALITY : 0.037 1667
REMARK 3 PLANARITY : 0.004 1921
REMARK 3 DIHEDRAL : 13.038 4132
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 8168
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 8168
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 8168
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TLH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69137
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.204
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.16600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.89600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2QUT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM HEPES, 17.5% PEG 4000, PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
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 51.57050
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A 346
REMARK 465 GLN A 347
REMARK 465 ALA A 348
REMARK 465 GLY A 349
REMARK 465 ALA A 350
REMARK 465 ALA A 351
REMARK 465 ALA A 352
REMARK 465 SER A 353
REMARK 465 GLU A 354
REMARK 465 SER A 355
REMARK 465 LEU A 356
REMARK 465 PHE A 357
REMARK 465 ILE A 358
REMARK 465 SER B 345
REMARK 465 GLY B 346
REMARK 465 GLN B 347
REMARK 465 ALA B 348
REMARK 465 GLY B 349
REMARK 465 ALA B 350
REMARK 465 ALA B 351
REMARK 465 ALA B 352
REMARK 465 SER B 353
REMARK 465 GLU B 354
REMARK 465 SER B 355
REMARK 465 LEU B 356
REMARK 465 PHE B 357
REMARK 465 ILE B 358
REMARK 465 GLN C 347
REMARK 465 ALA C 348
REMARK 465 GLY C 349
REMARK 465 ALA C 350
REMARK 465 ALA C 351
REMARK 465 ALA C 352
REMARK 465 SER C 353
REMARK 465 GLU C 354
REMARK 465 SER C 355
REMARK 465 LEU C 356
REMARK 465 PHE C 357
REMARK 465 ILE C 358
REMARK 465 SER D 345
REMARK 465 GLY D 346
REMARK 465 GLN D 347
REMARK 465 ALA D 348
REMARK 465 GLY D 349
REMARK 465 ALA D 350
REMARK 465 ALA D 351
REMARK 465 ALA D 352
REMARK 465 SER D 353
REMARK 465 GLU D 354
REMARK 465 SER D 355
REMARK 465 LEU D 356
REMARK 465 PHE D 357
REMARK 465 ILE D 358
REMARK 465 SER D 359
REMARK 465 ASN D 360
REMARK 465 HIS D 361
REMARK 465 ALA D 362
REMARK 465 TYR D 363
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 HH12 ARG D 133 O HOH D 502 1.39
REMARK 500 HG SER B 3 O HOH B 513 1.56
REMARK 500 HH21 ARG A 42 O20 RD2 A 401 1.57
REMARK 500 HH TYR C 84 OD2 ASP C 140 1.58
REMARK 500 H HIS A 156 O HOH A 511 1.59
REMARK 500 HH TYR B 84 OD2 ASP B 140 1.59
REMARK 500 O HOH A 642 O HOH D 624 1.87
REMARK 500 O18 RD2 C 401 O HOH C 501 1.89
REMARK 500 O HOH B 530 O HOH C 706 1.96
REMARK 500 O HOH A 648 O HOH D 514 1.99
REMARK 500 O HOH B 656 O HOH B 703 1.99
REMARK 500 O HOH B 681 O HOH B 688 2.01
REMARK 500 O HOH A 510 O HOH A 527 2.02
REMARK 500 O HOH C 567 O HOH C 700 2.02
REMARK 500 O HOH C 646 O HOH D 657 2.03
REMARK 500 O HOH A 604 O HOH A 690 2.03
REMARK 500 O HOH B 533 O HOH B 653 2.03
REMARK 500 O HOH C 622 O HOH C 686 2.03
REMARK 500 O HOH A 670 O HOH B 668 2.04
REMARK 500 O HOH C 679 O HOH C 698 2.04
REMARK 500 O HOH B 571 O HOH C 672 2.04
REMARK 500 O HOH C 537 O HOH C 698 2.04
REMARK 500 O HOH A 523 O HOH A 646 2.05
REMARK 500 OG SER A 271 O HOH A 501 2.07
REMARK 500 O HOH B 557 O HOH B 573 2.07
REMARK 500 O HOH A 664 O HOH A 685 2.08
REMARK 500 O HOH A 580 O HOH A 688 2.08
REMARK 500 O HOH B 704 O HOH C 619 2.08
REMARK 500 O3 MDN C 402 O HOH C 503 2.09
REMARK 500 O HOH D 527 O HOH D 666 2.09
REMARK 500 O HOH B 700 O HOH C 700 2.10
REMARK 500 OD1 ASN A 180 O HOH A 502 2.10
REMARK 500 O HOH B 672 O HOH B 683 2.10
REMARK 500 O HOH A 543 O HOH D 677 2.10
REMARK 500 O HOH B 570 O HOH B 658 2.11
REMARK 500 O HOH C 668 O HOH C 683 2.11
REMARK 500 O HOH C 653 O HOH C 696 2.12
REMARK 500 NH1 ARG D 133 O HOH D 502 2.12
REMARK 500 O HOH A 639 O HOH A 690 2.13
REMARK 500 O HOH A 545 O HOH D 583 2.13
REMARK 500 O HOH B 615 O HOH C 533 2.13
REMARK 500 OG1 THR A 36 O HOH A 503 2.13
REMARK 500 O HOH A 704 O HOH A 706 2.13
REMARK 500 O HOH D 598 O HOH D 605 2.13
REMARK 500 O HOH B 552 O HOH B 692 2.13
REMARK 500 O HOH C 506 O HOH C 677 2.13
REMARK 500 O HOH A 721 O HOH D 519 2.14
REMARK 500 O HOH A 660 O HOH A 705 2.15
REMARK 500 O HOH D 653 O HOH D 657 2.15
REMARK 500 O HOH B 630 O HOH B 696 2.16
REMARK 500
REMARK 500 THIS ENTRY HAS 59 CLOSE CONTACTS
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 701 O HOH B 608 1655 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS B 41 CD LYS B 41 CE 0.151
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 THR A 259 -28.43 -140.78
REMARK 500 THR A 298 -157.33 -135.69
REMARK 500 THR B 259 -29.12 -140.71
REMARK 500 THR B 298 -156.65 -134.64
REMARK 500 THR C 259 -29.48 -140.54
REMARK 500 THR C 298 -156.06 -135.36
REMARK 500 THR D 259 -29.21 -140.17
REMARK 500 THR D 298 -156.19 -135.81
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 B 713 DISTANCE = 5.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RD2 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MDN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RD2 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MDN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RD2 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MDN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RD2 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MDN D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TLE RELATED DB: PDB
REMARK 900 RELATED ID: 5TLW RELATED DB: PDB
REMARK 900 RELATED ID: 5TLZ RELATED DB: PDB
DBREF 5TLH A 1 363 UNP P00883 ALDOA_RABIT 2 364
DBREF 5TLH B 1 363 UNP P00883 ALDOA_RABIT 2 364
DBREF 5TLH C 1 363 UNP P00883 ALDOA_RABIT 2 364
DBREF 5TLH D 1 363 UNP P00883 ALDOA_RABIT 2 364
SEQRES 1 A 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 A 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 A 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 A 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 A 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 A 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 A 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 A 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 A 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 A 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 A 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 A 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 A 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 A 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 A 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 A 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 A 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 A 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 A 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 A 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 A 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 A 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 A 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 A 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 A 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 A 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 A 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 A 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
SEQRES 1 B 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 B 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 B 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 B 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 B 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 B 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 B 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 B 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 B 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 B 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 B 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 B 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 B 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 B 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 B 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 B 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 B 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 B 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 B 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 B 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 B 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 B 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 B 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 B 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 B 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 B 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 B 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 B 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
SEQRES 1 C 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 C 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 C 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 C 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 C 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 C 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 C 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 C 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 C 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 C 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 C 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 C 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 C 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 C 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 C 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 C 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 C 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 C 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 C 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 C 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 C 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 C 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 C 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 C 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 C 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 C 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 C 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 C 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
SEQRES 1 D 363 PRO HIS SER HIS PRO ALA LEU THR PRO GLU GLN LYS LYS
SEQRES 2 D 363 GLU LEU SER ASP ILE ALA HIS ARG ILE VAL ALA PRO GLY
SEQRES 3 D 363 LYS GLY ILE LEU ALA ALA ASP GLU SER THR GLY SER ILE
SEQRES 4 D 363 ALA LYS ARG LEU GLN SER ILE GLY THR GLU ASN THR GLU
SEQRES 5 D 363 GLU ASN ARG ARG PHE TYR ARG GLN LEU LEU LEU THR ALA
SEQRES 6 D 363 ASP ASP ARG VAL ASN PRO CYS ILE GLY GLY VAL ILE LEU
SEQRES 7 D 363 PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY ARG
SEQRES 8 D 363 PRO PHE PRO GLN VAL ILE LYS SER LYS GLY GLY VAL VAL
SEQRES 9 D 363 GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU ALA GLY
SEQRES 10 D 363 THR ASN GLY GLU THR THR THR GLN GLY LEU ASP GLY LEU
SEQRES 11 D 363 SER GLU ARG CYS ALA GLN TYR LYS LYS ASP GLY ALA ASP
SEQRES 12 D 363 PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY GLU HIS
SEQRES 13 D 363 THR PRO SER ALA LEU ALA ILE MET GLU ASN ALA ASN VAL
SEQRES 14 D 363 LEU ALA ARG TYR ALA SER ILE CYS GLN GLN ASN GLY ILE
SEQRES 15 D 363 VAL PRO ILE VAL GLU PRO GLU ILE LEU PRO ASP GLY ASP
SEQRES 16 D 363 HIS ASP LEU LYS ARG CYS GLN TYR VAL THR GLU LYS VAL
SEQRES 17 D 363 LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS ILE
SEQRES 18 D 363 TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL THR
SEQRES 19 D 363 PRO GLY HIS ALA CYS THR GLN LYS TYR SER HIS GLU GLU
SEQRES 20 D 363 ILE ALA MET ALA THR VAL THR ALA LEU ARG ARG THR VAL
SEQRES 21 D 363 PRO PRO ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY
SEQRES 22 D 363 GLN SER GLU GLU GLU ALA SER ILE ASN LEU ASN ALA ILE
SEQRES 23 D 363 ASN LYS CYS PRO LEU LEU LYS PRO TRP ALA LEU THR PHE
SEQRES 24 D 363 SER TYR GLY ARG ALA LEU GLN ALA SER ALA LEU LYS ALA
SEQRES 25 D 363 TRP GLY GLY LYS LYS GLU ASN LEU LYS ALA ALA GLN GLU
SEQRES 26 D 363 GLU TYR VAL LYS ARG ALA LEU ALA ASN SER LEU ALA CYS
SEQRES 27 D 363 GLN GLY LYS TYR THR PRO SER GLY GLN ALA GLY ALA ALA
SEQRES 28 D 363 ALA SER GLU SER LEU PHE ILE SER ASN HIS ALA TYR
HET RD2 A 401 28
HET MDN A 402 11
HET GOL B 403 28
HET RD2 B 401 28
HET MDN B 402 11
HET RD2 C 401 28
HET MDN C 402 11
HET GOL D 403 28
HET RD2 D 401 28
HET MDN D 402 11
HETNAM RD2 [(6-HYDROXYNAPHTHALEN-2-YL)METHYLENE]BIS(PHOSPHONIC
HETNAM 2 RD2 ACID)
HETNAM MDN METHYLENEDIPHOSPHONIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 RD2 4(C11 H12 O7 P2)
FORMUL 6 MDN 4(C H6 O6 P2)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 15 HOH *842(H2 O)
HELIX 1 AA1 THR A 8 VAL A 23 1 16
HELIX 2 AA2 SER A 35 SER A 45 1 11
HELIX 3 AA3 THR A 51 THR A 64 1 14
HELIX 4 AA4 PHE A 79 TYR A 84 1 6
HELIX 5 AA5 PRO A 92 LYS A 100 1 9
HELIX 6 AA6 GLY A 129 ASP A 140 1 12
HELIX 7 AA7 SER A 159 ASN A 180 1 22
HELIX 8 AA8 ASP A 197 HIS A 219 1 23
HELIX 9 AA9 TYR A 222 GLY A 225 5 4
HELIX 10 AB1 SER A 244 ARG A 258 1 15
HELIX 11 AB2 SER A 275 CYS A 289 1 15
HELIX 12 AB3 GLY A 302 GLY A 314 1 13
HELIX 13 AB4 LYS A 316 GLU A 318 5 3
HELIX 14 AB5 ASN A 319 CYS A 338 1 20
HELIX 15 AB6 THR B 8 VAL B 23 1 16
HELIX 16 AB7 SER B 35 ILE B 46 1 12
HELIX 17 AB8 THR B 51 THR B 64 1 14
HELIX 18 AB9 PHE B 79 TYR B 84 1 6
HELIX 19 AC1 PRO B 92 LYS B 100 1 9
HELIX 20 AC2 GLY B 129 ASP B 140 1 12
HELIX 21 AC3 SER B 159 ASN B 180 1 22
HELIX 22 AC4 ASP B 197 HIS B 219 1 23
HELIX 23 AC5 TYR B 222 GLY B 225 5 4
HELIX 24 AC6 SER B 244 ARG B 258 1 15
HELIX 25 AC7 SER B 275 CYS B 289 1 15
HELIX 26 AC8 GLY B 302 GLY B 314 1 13
HELIX 27 AC9 LYS B 316 GLU B 318 5 3
HELIX 28 AD1 ASN B 319 CYS B 338 1 20
HELIX 29 AD2 SER B 359 TYR B 363 5 5
HELIX 30 AD3 THR C 8 VAL C 23 1 16
HELIX 31 AD4 SER C 35 SER C 45 1 11
HELIX 32 AD5 THR C 51 THR C 64 1 14
HELIX 33 AD6 PHE C 79 TYR C 84 1 6
HELIX 34 AD7 PRO C 92 LYS C 100 1 9
HELIX 35 AD8 GLY C 129 ASP C 140 1 12
HELIX 36 AD9 SER C 159 ASN C 180 1 22
HELIX 37 AE1 ASP C 197 HIS C 219 1 23
HELIX 38 AE2 TYR C 222 GLY C 225 5 4
HELIX 39 AE3 SER C 244 ARG C 258 1 15
HELIX 40 AE4 SER C 275 CYS C 289 1 15
HELIX 41 AE5 GLY C 302 GLY C 314 1 13
HELIX 42 AE6 LYS C 316 GLU C 318 5 3
HELIX 43 AE7 ASN C 319 CYS C 338 1 20
HELIX 44 AE8 SER C 359 TYR C 363 5 5
HELIX 45 AE9 THR D 8 VAL D 23 1 16
HELIX 46 AF1 SER D 35 SER D 45 1 11
HELIX 47 AF2 THR D 51 THR D 64 1 14
HELIX 48 AF3 PHE D 79 TYR D 84 1 6
HELIX 49 AF4 PRO D 92 LYS D 100 1 9
HELIX 50 AF5 GLY D 129 ASP D 140 1 12
HELIX 51 AF6 SER D 159 ASN D 180 1 22
HELIX 52 AF7 ASP D 197 HIS D 219 1 23
HELIX 53 AF8 TYR D 222 GLY D 225 5 4
HELIX 54 AF9 SER D 244 ARG D 258 1 15
HELIX 55 AG1 SER D 275 CYS D 289 1 15
HELIX 56 AG2 GLY D 302 GLY D 314 1 13
HELIX 57 AG3 LYS D 316 GLU D 318 5 3
HELIX 58 AG4 ASN D 319 CYS D 338 1 20
SHEET 1 AA1 9 GLY A 28 ALA A 32 0
SHEET 2 AA1 9 ILE A 73 LEU A 78 1 O ILE A 77 N LEU A 30
SHEET 3 AA1 9 VAL A 103 LYS A 107 1 O GLY A 105 N VAL A 76
SHEET 4 AA1 9 PHE A 144 LEU A 151 1 O PHE A 144 N ILE A 106
SHEET 5 AA1 9 VAL A 183 ILE A 190 1 O GLU A 189 N LEU A 151
SHEET 6 AA1 9 LEU A 227 LEU A 228 1 O LEU A 227 N VAL A 186
SHEET 7 AA1 9 GLY A 266 PHE A 269 1 O THR A 268 N LEU A 228
SHEET 8 AA1 9 ALA A 296 TYR A 301 1 O ALA A 296 N VAL A 267
SHEET 9 AA1 9 GLY A 28 ALA A 32 1 N ILE A 29 O PHE A 299
SHEET 1 AA2 2 VAL A 112 PRO A 114 0
SHEET 2 AA2 2 THR A 122 THR A 124 -1 O THR A 123 N VAL A 113
SHEET 1 AA3 9 GLY B 28 ALA B 32 0
SHEET 2 AA3 9 ILE B 73 LEU B 78 1 O ILE B 77 N LEU B 30
SHEET 3 AA3 9 VAL B 103 LYS B 107 1 O GLY B 105 N VAL B 76
SHEET 4 AA3 9 ALA B 142 LEU B 151 1 O ASP B 143 N VAL B 104
SHEET 5 AA3 9 VAL B 183 ILE B 190 1 O GLU B 187 N CYS B 149
SHEET 6 AA3 9 LEU B 227 LEU B 228 1 O LEU B 227 N VAL B 186
SHEET 7 AA3 9 GLY B 266 PHE B 269 1 O THR B 268 N LEU B 228
SHEET 8 AA3 9 ALA B 296 TYR B 301 1 O ALA B 296 N VAL B 267
SHEET 9 AA3 9 GLY B 28 ALA B 32 1 N ILE B 29 O PHE B 299
SHEET 1 AA4 2 VAL B 112 PRO B 114 0
SHEET 2 AA4 2 THR B 122 THR B 124 -1 O THR B 123 N VAL B 113
SHEET 1 AA5 9 GLY C 28 ALA C 32 0
SHEET 2 AA5 9 ILE C 73 LEU C 78 1 O ILE C 77 N LEU C 30
SHEET 3 AA5 9 VAL C 103 LYS C 107 1 O GLY C 105 N VAL C 76
SHEET 4 AA5 9 PHE C 144 LEU C 151 1 O LYS C 146 N ILE C 106
SHEET 5 AA5 9 VAL C 183 ILE C 190 1 O GLU C 187 N CYS C 149
SHEET 6 AA5 9 LEU C 227 LEU C 228 1 O LEU C 227 N VAL C 186
SHEET 7 AA5 9 GLY C 266 PHE C 269 1 O THR C 268 N LEU C 228
SHEET 8 AA5 9 ALA C 296 TYR C 301 1 O ALA C 296 N VAL C 267
SHEET 9 AA5 9 GLY C 28 ALA C 32 1 N ILE C 29 O PHE C 299
SHEET 1 AA6 2 VAL C 112 PRO C 114 0
SHEET 2 AA6 2 THR C 122 THR C 124 -1 O THR C 123 N VAL C 113
SHEET 1 AA7 9 GLY D 28 ALA D 32 0
SHEET 2 AA7 9 ILE D 73 LEU D 78 1 O GLY D 75 N LEU D 30
SHEET 3 AA7 9 VAL D 103 LYS D 107 1 O GLY D 105 N VAL D 76
SHEET 4 AA7 9 ALA D 142 LEU D 151 1 O ASP D 143 N VAL D 104
SHEET 5 AA7 9 VAL D 183 ILE D 190 1 O GLU D 189 N LEU D 151
SHEET 6 AA7 9 LEU D 227 LEU D 228 1 O LEU D 227 N VAL D 186
SHEET 7 AA7 9 GLY D 266 PHE D 269 1 O THR D 268 N LEU D 228
SHEET 8 AA7 9 ALA D 296 TYR D 301 1 O ALA D 296 N VAL D 267
SHEET 9 AA7 9 GLY D 28 ALA D 32 1 N ILE D 29 O PHE D 299
SHEET 1 AA8 2 VAL D 112 PRO D 114 0
SHEET 2 AA8 2 THR D 122 THR D 124 -1 O THR D 123 N VAL D 113
CISPEP 1 THR A 157 PRO A 158 0 -1.41
CISPEP 2 THR B 157 PRO B 158 0 -0.52
CISPEP 3 THR C 157 PRO C 158 0 -0.33
CISPEP 4 THR D 157 PRO D 158 0 -0.65
SITE 1 AC1 5 GLU A 34 ARG A 42 SER A 45 ARG A 303
SITE 2 AC1 5 LYS A 311
SITE 1 AC2 9 ASP A 33 SER A 38 LYS A 107 LYS A 146
SITE 2 AC2 9 ARG A 148 HOH A 507 HOH A 518 HOH A 542
SITE 3 AC2 9 HOH A 568
SITE 1 AC3 12 LEU A 127 GLU A 165 ASN A 168 ARG A 172
SITE 2 AC3 12 HOH A 504 LEU B 127 GLU B 165 ASN B 168
SITE 3 AC3 12 VAL B 169 ARG B 172 HOH B 501 HOH B 546
SITE 1 AC4 6 GLU B 34 ARG B 42 SER B 45 ARG B 303
SITE 2 AC4 6 LYS B 311 HOH B 503
SITE 1 AC5 11 ASP B 33 SER B 35 SER B 38 LYS B 107
SITE 2 AC5 11 LYS B 146 ARG B 148 HOH B 504 HOH B 529
SITE 3 AC5 11 HOH B 591 HOH B 601 HOH B 628
SITE 1 AC6 8 GLU C 34 ARG C 42 SER C 45 ARG C 303
SITE 2 AC6 8 LYS C 311 HOH C 501 HOH C 537 HOH C 572
SITE 1 AC7 10 SER C 38 LYS C 107 LYS C 146 ARG C 148
SITE 2 AC7 10 HOH C 503 HOH C 504 HOH C 509 HOH C 552
SITE 3 AC7 10 HOH C 609 HOH C 613
SITE 1 AC8 10 LEU C 127 GLU C 165 ASN C 168 ARG C 172
SITE 2 AC8 10 HOH C 576 LEU D 127 GLU D 165 ASN D 168
SITE 3 AC8 10 ARG D 172 HOH D 585
SITE 1 AC9 6 GLU D 34 ARG D 42 SER D 45 ARG D 303
SITE 2 AC9 6 LYS D 311 HOH D 501
SITE 1 AD1 7 SER D 38 LYS D 107 LYS D 146 ARG D 148
SITE 2 AD1 7 HOH D 504 HOH D 513 HOH D 545
CRYST1 83.569 103.141 84.865 90.00 98.87 90.00 P 1 21 1 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 0.011966 0.000000 0.001867 0.00000
SCALE2 0.000000 0.009695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011926 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
