HEADER TRANSFERASE 01-AUG-06 2HWG
TITLE STRUCTURE OF PHOSPHORYLATED ENZYME I OF THE PHOSPHOENOLPYRUVATE:SUGAR
TITLE 2 PHOSPHOTRANSFERASE SYSTEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE-PROTEIN PHOSPHOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHOTRANSFERASE SYSTEM, ENZYME I;
COMPND 5 EC: 2.7.3.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PTSI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PRE1
KEYWDS ENZYME I, PHOSPHOENOLPYRUVATE:SUGAR PHOSPHOTRANSFERASE SYSTEM, PTS,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.LIM,A.TEPLYAKOV,O.HERZBERG
REVDAT 6 15-NOV-23 2HWG 1 REMARK
REVDAT 5 30-AUG-23 2HWG 1 REMARK SEQADV LINK
REVDAT 4 14-AUG-19 2HWG 1 REMARK
REVDAT 3 24-JUL-19 2HWG 1 REMARK LINK
REVDAT 2 24-FEB-09 2HWG 1 VERSN
REVDAT 1 14-NOV-06 2HWG 0
JRNL AUTH A.TEPLYAKOV,K.LIM,P.P.ZHU,G.KAPADIA,C.C.CHEN,J.SCHWARTZ,
JRNL AUTH 2 A.HOWARD,P.T.REDDY,A.PETERKOFSKY,O.HERZBERG
JRNL TITL STRUCTURE OF PHOSPHORYLATED ENZYME I, THE
JRNL TITL 2 PHOSPHOENOLPYRUVATE:SUGAR PHOSPHOTRANSFERASE SYSTEM SUGAR
JRNL TITL 3 TRANSLOCATION SIGNAL PROTEIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 16218 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 17053069
JRNL DOI 10.1073/PNAS.0607587103
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 36205
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1798
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8874
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.00
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HWG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000038838.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36262
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.32600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1ZYM,2BG5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN SAMPLE (10 MG/ML) WAS
REMARK 280 MIXED WITH MGCL2 AND PEP TO BRING EACH ADDITIVE TO A FINAL
REMARK 280 CONCENTRATION OF 10 MM. AFTER ~5 MIN, SODIUM OXALATE WAS ADDED
REMARK 280 TO A FINAL CONCENTRATION OF 10 MM. DROPS CONTAINING 1:1 PROTEIN
REMARK 280 AND RESERVOIR SOLUTION WERE EQUILIBRATED AGAINST RESERVOIR
REMARK 280 SOLUTION CONTAINING 22% W/V POLYETHYLENE GLYCOL 6000, 2%
REMARK 280 SATURATED AMMONIUM SULFATE, AND 100 MM NA+HEPES., PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 42.74350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.50350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.04200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.50350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.74350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.04200
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 300 REMARK: THE DIMER IN THE ASYMMETRIC UNIT IS THE BIOLOGICAL ASSEMBLY.
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: 4640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 MSE A 1
REMARK 465 ILE A 574
REMARK 465 CYS A 575
REMARK 465 MSE B 1
REMARK 465 ILE B 574
REMARK 465 CYS B 575
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 NH1 ARG B 371 OE1 GLU B 412 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),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 A 60 CE LYS A 60 NZ 0.155
REMARK 500 GLU B 285 CG GLU B 285 CD 0.107
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 LEU A 561 CA - CB - CG ANGL. DEV. = 24.1 DEGREES
REMARK 500 ILE B 219 CG1 - CB - CG2 ANGL. DEV. = -14.0 DEGREES
REMARK 500 ILE B 262 CG1 - CB - CG2 ANGL. DEV. = -17.1 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 ALA A 7 -47.79 -131.60
REMARK 500 ASP A 22 108.71 -32.63
REMARK 500 GLN A 35 1.93 -52.43
REMARK 500 PHE A 65 -47.29 -134.57
REMARK 500 ASP A 82 128.06 -36.98
REMARK 500 ALA A 151 58.42 -113.50
REMARK 500 GLN A 153 -73.60 -50.28
REMARK 500 GLU A 155 105.88 -43.83
REMARK 500 ASN A 172 98.69 -44.61
REMARK 500 SER A 207 82.06 -155.21
REMARK 500 ASN A 225 70.61 69.75
REMARK 500 LYS A 257 -47.24 -26.18
REMARK 500 THR A 277 135.29 -171.56
REMARK 500 VAL A 278 -39.46 -29.48
REMARK 500 LEU A 294 119.93 -164.05
REMARK 500 ARG A 296 96.95 -66.46
REMARK 500 ALA A 359 -113.84 60.65
REMARK 500 MSE A 477 55.75 -102.94
REMARK 500 GLU A 509 -19.97 -46.94
REMARK 500 LYS B 20 108.95 -46.79
REMARK 500 GLU B 63 -85.33 -126.37
REMARK 500 THR B 64 7.25 -59.97
REMARK 500 PHE B 65 -13.21 -144.93
REMARK 500 GLN B 87 -74.48 -61.56
REMARK 500 LYS B 96 15.73 -140.91
REMARK 500 ASP B 119 55.20 -102.08
REMARK 500 ALA B 151 51.20 -106.86
REMARK 500 ALA B 183 -167.32 -102.07
REMARK 500 ALA B 194 -33.26 -38.30
REMARK 500 SER B 207 50.38 -142.84
REMARK 500 ALA B 222 34.63 -96.63
REMARK 500 ASN B 225 63.24 64.61
REMARK 500 ASP B 303 -14.02 -38.87
REMARK 500 TYR B 344 6.53 -46.35
REMARK 500 ALA B 359 -107.62 52.92
REMARK 500 GLU B 368 -55.35 -27.68
REMARK 500 MSE B 477 46.42 -103.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 338 ASP B 339 149.75
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 MG A 901 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NEP A 189 O2P
REMARK 620 2 GLU A 431 OE1 166.3
REMARK 620 3 ASP A 455 OD2 81.2 90.5
REMARK 620 4 OXL A 903 O2 92.7 91.9 162.0
REMARK 620 5 OXL A 903 O1 91.6 76.9 86.3 76.9
REMARK 620 6 HOH A1001 O 99.4 93.0 102.4 95.2 166.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 NEP B 189 O2P
REMARK 620 2 GLU B 431 OE1 170.3
REMARK 620 3 ASP B 455 OD2 90.1 87.7
REMARK 620 4 OXL B 904 O1 106.7 82.6 87.4
REMARK 620 5 OXL B 904 O2 89.3 95.9 160.9 74.5
REMARK 620 6 HOH B1002 O 88.1 84.7 118.6 150.5 80.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL B 904
DBREF 2HWG A 1 575 UNP P08839 PT1_ECOLI 1 575
DBREF 2HWG B 1 575 UNP P08839 PT1_ECOLI 1 575
SEQADV 2HWG MSE A 1 UNP P08839 MET 1 MODIFIED RESIDUE
SEQADV 2HWG MSE A 78 UNP P08839 MET 78 MODIFIED RESIDUE
SEQADV 2HWG MSE A 98 UNP P08839 MET 98 MODIFIED RESIDUE
SEQADV 2HWG NEP A 189 UNP P08839 HIS 189 MODIFIED RESIDUE
SEQADV 2HWG MSE A 193 UNP P08839 MET 193 MODIFIED RESIDUE
SEQADV 2HWG MSE A 239 UNP P08839 MET 239 MODIFIED RESIDUE
SEQADV 2HWG MSE A 302 UNP P08839 MET 302 MODIFIED RESIDUE
SEQADV 2HWG MSE A 334 UNP P08839 MET 334 MODIFIED RESIDUE
SEQADV 2HWG MSE A 345 UNP P08839 MET 345 MODIFIED RESIDUE
SEQADV 2HWG MSE A 364 UNP P08839 MET 364 MODIFIED RESIDUE
SEQADV 2HWG MSE A 389 UNP P08839 MET 389 MODIFIED RESIDUE
SEQADV 2HWG MSE A 392 UNP P08839 MET 392 MODIFIED RESIDUE
SEQADV 2HWG MSE A 429 UNP P08839 MET 429 MODIFIED RESIDUE
SEQADV 2HWG MSE A 469 UNP P08839 MET 469 MODIFIED RESIDUE
SEQADV 2HWG MSE A 477 UNP P08839 MET 477 MODIFIED RESIDUE
SEQADV 2HWG MSE A 501 UNP P08839 MET 501 MODIFIED RESIDUE
SEQADV 2HWG MSE A 518 UNP P08839 MET 518 MODIFIED RESIDUE
SEQADV 2HWG MSE A 525 UNP P08839 MET 525 MODIFIED RESIDUE
SEQADV 2HWG MSE A 562 UNP P08839 MET 562 MODIFIED RESIDUE
SEQADV 2HWG MSE B 1 UNP P08839 MET 1 MODIFIED RESIDUE
SEQADV 2HWG MSE B 78 UNP P08839 MET 78 MODIFIED RESIDUE
SEQADV 2HWG MSE B 98 UNP P08839 MET 98 MODIFIED RESIDUE
SEQADV 2HWG NEP B 189 UNP P08839 HIS 189 MODIFIED RESIDUE
SEQADV 2HWG MSE B 193 UNP P08839 MET 193 MODIFIED RESIDUE
SEQADV 2HWG MSE B 239 UNP P08839 MET 239 MODIFIED RESIDUE
SEQADV 2HWG MSE B 302 UNP P08839 MET 302 MODIFIED RESIDUE
SEQADV 2HWG MSE B 334 UNP P08839 MET 334 MODIFIED RESIDUE
SEQADV 2HWG MSE B 345 UNP P08839 MET 345 MODIFIED RESIDUE
SEQADV 2HWG MSE B 364 UNP P08839 MET 364 MODIFIED RESIDUE
SEQADV 2HWG MSE B 389 UNP P08839 MET 389 MODIFIED RESIDUE
SEQADV 2HWG MSE B 392 UNP P08839 MET 392 MODIFIED RESIDUE
SEQADV 2HWG MSE B 429 UNP P08839 MET 429 MODIFIED RESIDUE
SEQADV 2HWG MSE B 469 UNP P08839 MET 469 MODIFIED RESIDUE
SEQADV 2HWG MSE B 477 UNP P08839 MET 477 MODIFIED RESIDUE
SEQADV 2HWG MSE B 501 UNP P08839 MET 501 MODIFIED RESIDUE
SEQADV 2HWG MSE B 518 UNP P08839 MET 518 MODIFIED RESIDUE
SEQADV 2HWG MSE B 525 UNP P08839 MET 525 MODIFIED RESIDUE
SEQADV 2HWG MSE B 562 UNP P08839 MET 562 MODIFIED RESIDUE
SEQRES 1 A 575 MSE ILE SER GLY ILE LEU ALA SER PRO GLY ILE ALA PHE
SEQRES 2 A 575 GLY LYS ALA LEU LEU LEU LYS GLU ASP GLU ILE VAL ILE
SEQRES 3 A 575 ASP ARG LYS LYS ILE SER ALA ASP GLN VAL ASP GLN GLU
SEQRES 4 A 575 VAL GLU ARG PHE LEU SER GLY ARG ALA LYS ALA SER ALA
SEQRES 5 A 575 GLN LEU GLU THR ILE LYS THR LYS ALA GLY GLU THR PHE
SEQRES 6 A 575 GLY GLU GLU LYS GLU ALA ILE PHE GLU GLY HIS ILE MSE
SEQRES 7 A 575 LEU LEU GLU ASP GLU GLU LEU GLU GLN GLU ILE ILE ALA
SEQRES 8 A 575 LEU ILE LYS ASP LYS HIS MSE THR ALA ASP ALA ALA ALA
SEQRES 9 A 575 HIS GLU VAL ILE GLU GLY GLN ALA SER ALA LEU GLU GLU
SEQRES 10 A 575 LEU ASP ASP GLU TYR LEU LYS GLU ARG ALA ALA ASP VAL
SEQRES 11 A 575 ARG ASP ILE GLY LYS ARG LEU LEU ARG ASN ILE LEU GLY
SEQRES 12 A 575 LEU LYS ILE ILE ASP LEU SER ALA ILE GLN ASP GLU VAL
SEQRES 13 A 575 ILE LEU VAL ALA ALA ASP LEU THR PRO SER GLU THR ALA
SEQRES 14 A 575 GLN LEU ASN LEU LYS LYS VAL LEU GLY PHE ILE THR ASP
SEQRES 15 A 575 ALA GLY GLY ARG THR SER NEP THR SER ILE MSE ALA ARG
SEQRES 16 A 575 SER LEU GLU LEU PRO ALA ILE VAL GLY THR GLY SER VAL
SEQRES 17 A 575 THR SER GLN VAL LYS ASN ASP ASP TYR LEU ILE LEU ASP
SEQRES 18 A 575 ALA VAL ASN ASN GLN VAL TYR VAL ASN PRO THR ASN GLU
SEQRES 19 A 575 VAL ILE ASP LYS MSE ARG ALA VAL GLN GLU GLN VAL ALA
SEQRES 20 A 575 SER GLU LYS ALA GLU LEU ALA LYS LEU LYS ASP LEU PRO
SEQRES 21 A 575 ALA ILE THR LEU ASP GLY HIS GLN VAL GLU VAL CYS ALA
SEQRES 22 A 575 ASN ILE GLY THR VAL ARG ASP VAL GLU GLY ALA GLU ARG
SEQRES 23 A 575 ASN GLY ALA GLU GLY VAL GLY LEU TYR ARG THR GLU PHE
SEQRES 24 A 575 LEU PHE MSE ASP ARG ASP ALA LEU PRO THR GLU GLU GLU
SEQRES 25 A 575 GLN PHE ALA ALA TYR LYS ALA VAL ALA GLU ALA CYS GLY
SEQRES 26 A 575 SER GLN ALA VAL ILE VAL ARG THR MSE ASP ILE GLY GLY
SEQRES 27 A 575 ASP LYS GLU LEU PRO TYR MSE ASN PHE PRO LYS GLU GLU
SEQRES 28 A 575 ASN PRO PHE LEU GLY TRP ARG ALA ILE ARG ILE ALA MSE
SEQRES 29 A 575 ASP ARG ARG GLU ILE LEU ARG ASP GLN LEU ARG ALA ILE
SEQRES 30 A 575 LEU ARG ALA SER ALA PHE GLY LYS LEU ARG ILE MSE PHE
SEQRES 31 A 575 PRO MSE ILE ILE SER VAL GLU GLU VAL ARG ALA LEU ARG
SEQRES 32 A 575 LYS GLU ILE GLU ILE TYR LYS GLN GLU LEU ARG ASP GLU
SEQRES 33 A 575 GLY LYS ALA PHE ASP GLU SER ILE GLU ILE GLY VAL MSE
SEQRES 34 A 575 VAL GLU THR PRO ALA ALA ALA THR ILE ALA ARG HIS LEU
SEQRES 35 A 575 ALA LYS GLU VAL ASP PHE PHE SER ILE GLY THR ASN ASP
SEQRES 36 A 575 LEU THR GLN TYR THR LEU ALA VAL ASP ARG GLY ASN ASP
SEQRES 37 A 575 MSE ILE SER HIS LEU TYR GLN PRO MSE SER PRO SER VAL
SEQRES 38 A 575 LEU ASN LEU ILE LYS GLN VAL ILE ASP ALA SER HIS ALA
SEQRES 39 A 575 GLU GLY LYS TRP THR GLY MSE CYS GLY GLU LEU ALA GLY
SEQRES 40 A 575 ASP GLU ARG ALA THR LEU LEU LEU LEU GLY MSE GLY LEU
SEQRES 41 A 575 ASP GLU PHE SER MSE SER ALA ILE SER ILE PRO ARG ILE
SEQRES 42 A 575 LYS LYS ILE ILE ARG ASN THR ASN PHE GLU ASP ALA LYS
SEQRES 43 A 575 VAL LEU ALA GLU GLN ALA LEU ALA GLN PRO THR THR ASP
SEQRES 44 A 575 GLU LEU MSE THR LEU VAL ASN LYS PHE ILE GLU GLU LYS
SEQRES 45 A 575 THR ILE CYS
SEQRES 1 B 575 MSE ILE SER GLY ILE LEU ALA SER PRO GLY ILE ALA PHE
SEQRES 2 B 575 GLY LYS ALA LEU LEU LEU LYS GLU ASP GLU ILE VAL ILE
SEQRES 3 B 575 ASP ARG LYS LYS ILE SER ALA ASP GLN VAL ASP GLN GLU
SEQRES 4 B 575 VAL GLU ARG PHE LEU SER GLY ARG ALA LYS ALA SER ALA
SEQRES 5 B 575 GLN LEU GLU THR ILE LYS THR LYS ALA GLY GLU THR PHE
SEQRES 6 B 575 GLY GLU GLU LYS GLU ALA ILE PHE GLU GLY HIS ILE MSE
SEQRES 7 B 575 LEU LEU GLU ASP GLU GLU LEU GLU GLN GLU ILE ILE ALA
SEQRES 8 B 575 LEU ILE LYS ASP LYS HIS MSE THR ALA ASP ALA ALA ALA
SEQRES 9 B 575 HIS GLU VAL ILE GLU GLY GLN ALA SER ALA LEU GLU GLU
SEQRES 10 B 575 LEU ASP ASP GLU TYR LEU LYS GLU ARG ALA ALA ASP VAL
SEQRES 11 B 575 ARG ASP ILE GLY LYS ARG LEU LEU ARG ASN ILE LEU GLY
SEQRES 12 B 575 LEU LYS ILE ILE ASP LEU SER ALA ILE GLN ASP GLU VAL
SEQRES 13 B 575 ILE LEU VAL ALA ALA ASP LEU THR PRO SER GLU THR ALA
SEQRES 14 B 575 GLN LEU ASN LEU LYS LYS VAL LEU GLY PHE ILE THR ASP
SEQRES 15 B 575 ALA GLY GLY ARG THR SER NEP THR SER ILE MSE ALA ARG
SEQRES 16 B 575 SER LEU GLU LEU PRO ALA ILE VAL GLY THR GLY SER VAL
SEQRES 17 B 575 THR SER GLN VAL LYS ASN ASP ASP TYR LEU ILE LEU ASP
SEQRES 18 B 575 ALA VAL ASN ASN GLN VAL TYR VAL ASN PRO THR ASN GLU
SEQRES 19 B 575 VAL ILE ASP LYS MSE ARG ALA VAL GLN GLU GLN VAL ALA
SEQRES 20 B 575 SER GLU LYS ALA GLU LEU ALA LYS LEU LYS ASP LEU PRO
SEQRES 21 B 575 ALA ILE THR LEU ASP GLY HIS GLN VAL GLU VAL CYS ALA
SEQRES 22 B 575 ASN ILE GLY THR VAL ARG ASP VAL GLU GLY ALA GLU ARG
SEQRES 23 B 575 ASN GLY ALA GLU GLY VAL GLY LEU TYR ARG THR GLU PHE
SEQRES 24 B 575 LEU PHE MSE ASP ARG ASP ALA LEU PRO THR GLU GLU GLU
SEQRES 25 B 575 GLN PHE ALA ALA TYR LYS ALA VAL ALA GLU ALA CYS GLY
SEQRES 26 B 575 SER GLN ALA VAL ILE VAL ARG THR MSE ASP ILE GLY GLY
SEQRES 27 B 575 ASP LYS GLU LEU PRO TYR MSE ASN PHE PRO LYS GLU GLU
SEQRES 28 B 575 ASN PRO PHE LEU GLY TRP ARG ALA ILE ARG ILE ALA MSE
SEQRES 29 B 575 ASP ARG ARG GLU ILE LEU ARG ASP GLN LEU ARG ALA ILE
SEQRES 30 B 575 LEU ARG ALA SER ALA PHE GLY LYS LEU ARG ILE MSE PHE
SEQRES 31 B 575 PRO MSE ILE ILE SER VAL GLU GLU VAL ARG ALA LEU ARG
SEQRES 32 B 575 LYS GLU ILE GLU ILE TYR LYS GLN GLU LEU ARG ASP GLU
SEQRES 33 B 575 GLY LYS ALA PHE ASP GLU SER ILE GLU ILE GLY VAL MSE
SEQRES 34 B 575 VAL GLU THR PRO ALA ALA ALA THR ILE ALA ARG HIS LEU
SEQRES 35 B 575 ALA LYS GLU VAL ASP PHE PHE SER ILE GLY THR ASN ASP
SEQRES 36 B 575 LEU THR GLN TYR THR LEU ALA VAL ASP ARG GLY ASN ASP
SEQRES 37 B 575 MSE ILE SER HIS LEU TYR GLN PRO MSE SER PRO SER VAL
SEQRES 38 B 575 LEU ASN LEU ILE LYS GLN VAL ILE ASP ALA SER HIS ALA
SEQRES 39 B 575 GLU GLY LYS TRP THR GLY MSE CYS GLY GLU LEU ALA GLY
SEQRES 40 B 575 ASP GLU ARG ALA THR LEU LEU LEU LEU GLY MSE GLY LEU
SEQRES 41 B 575 ASP GLU PHE SER MSE SER ALA ILE SER ILE PRO ARG ILE
SEQRES 42 B 575 LYS LYS ILE ILE ARG ASN THR ASN PHE GLU ASP ALA LYS
SEQRES 43 B 575 VAL LEU ALA GLU GLN ALA LEU ALA GLN PRO THR THR ASP
SEQRES 44 B 575 GLU LEU MSE THR LEU VAL ASN LYS PHE ILE GLU GLU LYS
SEQRES 45 B 575 THR ILE CYS
MODRES 2HWG MSE A 78 MET SELENOMETHIONINE
MODRES 2HWG MSE A 98 MET SELENOMETHIONINE
MODRES 2HWG NEP A 189 HIS N1-PHOSPHONOHISTIDINE
MODRES 2HWG MSE A 193 MET SELENOMETHIONINE
MODRES 2HWG MSE A 239 MET SELENOMETHIONINE
MODRES 2HWG MSE A 302 MET SELENOMETHIONINE
MODRES 2HWG MSE A 334 MET SELENOMETHIONINE
MODRES 2HWG MSE A 345 MET SELENOMETHIONINE
MODRES 2HWG MSE A 364 MET SELENOMETHIONINE
MODRES 2HWG MSE A 389 MET SELENOMETHIONINE
MODRES 2HWG MSE A 392 MET SELENOMETHIONINE
MODRES 2HWG MSE A 429 MET SELENOMETHIONINE
MODRES 2HWG MSE A 469 MET SELENOMETHIONINE
MODRES 2HWG MSE A 477 MET SELENOMETHIONINE
MODRES 2HWG MSE A 501 MET SELENOMETHIONINE
MODRES 2HWG MSE A 518 MET SELENOMETHIONINE
MODRES 2HWG MSE A 525 MET SELENOMETHIONINE
MODRES 2HWG MSE A 562 MET SELENOMETHIONINE
MODRES 2HWG MSE B 78 MET SELENOMETHIONINE
MODRES 2HWG MSE B 98 MET SELENOMETHIONINE
MODRES 2HWG NEP B 189 HIS N1-PHOSPHONOHISTIDINE
MODRES 2HWG MSE B 193 MET SELENOMETHIONINE
MODRES 2HWG MSE B 239 MET SELENOMETHIONINE
MODRES 2HWG MSE B 302 MET SELENOMETHIONINE
MODRES 2HWG MSE B 334 MET SELENOMETHIONINE
MODRES 2HWG MSE B 345 MET SELENOMETHIONINE
MODRES 2HWG MSE B 364 MET SELENOMETHIONINE
MODRES 2HWG MSE B 389 MET SELENOMETHIONINE
MODRES 2HWG MSE B 392 MET SELENOMETHIONINE
MODRES 2HWG MSE B 429 MET SELENOMETHIONINE
MODRES 2HWG MSE B 469 MET SELENOMETHIONINE
MODRES 2HWG MSE B 477 MET SELENOMETHIONINE
MODRES 2HWG MSE B 501 MET SELENOMETHIONINE
MODRES 2HWG MSE B 518 MET SELENOMETHIONINE
MODRES 2HWG MSE B 525 MET SELENOMETHIONINE
MODRES 2HWG MSE B 562 MET SELENOMETHIONINE
HET MSE A 78 8
HET MSE A 98 8
HET NEP A 189 14
HET MSE A 193 8
HET MSE A 239 8
HET MSE A 302 8
HET MSE A 334 8
HET MSE A 345 8
HET MSE A 364 8
HET MSE A 389 8
HET MSE A 392 8
HET MSE A 429 8
HET MSE A 469 8
HET MSE A 477 8
HET MSE A 501 8
HET MSE A 518 8
HET MSE A 525 8
HET MSE A 562 8
HET MSE B 78 8
HET MSE B 98 8
HET NEP B 189 14
HET MSE B 193 8
HET MSE B 239 8
HET MSE B 302 8
HET MSE B 334 8
HET MSE B 345 8
HET MSE B 364 8
HET MSE B 389 8
HET MSE B 392 8
HET MSE B 429 8
HET MSE B 469 8
HET MSE B 477 8
HET MSE B 501 8
HET MSE B 518 8
HET MSE B 525 8
HET MSE B 562 8
HET MG A 901 1
HET OXL A 903 6
HET MG B 902 1
HET OXL B 904 6
HETNAM MSE SELENOMETHIONINE
HETNAM NEP N1-PHOSPHONOHISTIDINE
HETNAM MG MAGNESIUM ION
HETNAM OXL OXALATE ION
FORMUL 1 MSE 34(C5 H11 N O2 SE)
FORMUL 1 NEP 2(C6 H10 N3 O5 P)
FORMUL 3 MG 2(MG 2+)
FORMUL 4 OXL 2(C2 O4 2-)
FORMUL 7 HOH *214(H2 O)
HELIX 1 1 ASP A 34 LYS A 60 1 27
HELIX 2 2 LYS A 60 PHE A 65 1 6
HELIX 3 3 GLY A 66 ASP A 82 1 17
HELIX 4 4 ASP A 82 ASP A 95 1 14
HELIX 5 5 THR A 99 LEU A 118 1 20
HELIX 6 6 ASP A 120 LEU A 142 1 23
HELIX 7 7 ASP A 148 ILE A 152 5 5
HELIX 8 8 THR A 164 GLN A 170 1 7
HELIX 9 9 SER A 188 LEU A 197 1 10
HELIX 10 10 SER A 207 VAL A 212 1 6
HELIX 11 11 THR A 232 ALA A 254 1 23
HELIX 12 12 LYS A 255 LYS A 257 5 3
HELIX 13 13 VAL A 278 ASN A 287 1 10
HELIX 14 14 THR A 297 MSE A 302 1 6
HELIX 15 15 THR A 309 CYS A 324 1 16
HELIX 16 16 LEU A 342 ASN A 346 5 5
HELIX 17 17 ASN A 352 GLY A 356 5 5
HELIX 18 18 ALA A 359 MSE A 364 1 6
HELIX 19 19 ARG A 366 SER A 381 1 16
HELIX 20 20 SER A 395 GLU A 416 1 22
HELIX 21 21 THR A 432 ILE A 438 1 7
HELIX 22 22 ILE A 438 LYS A 444 1 7
HELIX 23 23 GLY A 452 ALA A 462 1 11
HELIX 24 24 ASN A 467 TYR A 474 5 8
HELIX 25 25 SER A 478 GLU A 495 1 18
HELIX 26 26 ALA A 511 MSE A 518 1 8
HELIX 27 27 SER A 526 ILE A 528 5 3
HELIX 28 28 SER A 529 ASN A 539 1 11
HELIX 29 29 ASN A 541 GLN A 555 1 15
HELIX 30 30 THR A 557 THR A 573 1 17
HELIX 31 31 ASP B 34 THR B 59 1 26
HELIX 32 32 LYS B 60 GLU B 63 5 4
HELIX 33 33 GLU B 68 GLU B 81 1 14
HELIX 34 34 ASP B 82 HIS B 97 1 16
HELIX 35 35 THR B 99 GLU B 117 1 19
HELIX 36 36 ASP B 120 GLY B 143 1 24
HELIX 37 37 THR B 164 LEU B 171 1 8
HELIX 38 38 SER B 188 LEU B 197 1 10
HELIX 39 39 SER B 207 GLN B 211 5 5
HELIX 40 40 THR B 232 ALA B 254 1 23
HELIX 41 41 LYS B 255 LYS B 257 5 3
HELIX 42 42 ARG B 279 ASN B 287 1 9
HELIX 43 43 THR B 297 ARG B 304 1 8
HELIX 44 44 THR B 309 CYS B 324 1 16
HELIX 45 45 LEU B 342 ASN B 346 5 5
HELIX 46 46 ASN B 352 GLY B 356 5 5
HELIX 47 47 ALA B 359 ARG B 366 1 8
HELIX 48 48 ARG B 366 SER B 381 1 16
HELIX 49 49 SER B 395 GLU B 416 1 22
HELIX 50 50 THR B 432 ILE B 438 1 7
HELIX 51 51 ILE B 438 ALA B 443 1 6
HELIX 52 52 GLY B 452 LEU B 461 1 10
HELIX 53 53 ASN B 467 TYR B 474 5 8
HELIX 54 54 SER B 478 GLU B 495 1 18
HELIX 55 55 GLY B 503 ARG B 510 5 8
HELIX 56 56 ALA B 511 MSE B 518 1 8
HELIX 57 57 SER B 526 ILE B 528 5 3
HELIX 58 58 SER B 529 ASN B 539 1 11
HELIX 59 59 ASN B 541 LEU B 553 1 13
HELIX 60 60 THR B 557 THR B 573 1 17
SHEET 1 A 7 ILE A 5 SER A 8 0
SHEET 2 A 7 ALA A 201 VAL A 203 -1 O VAL A 203 N ILE A 5
SHEET 3 A 7 VAL A 176 THR A 181 1 N PHE A 179 O ILE A 202
SHEET 4 A 7 VAL A 156 ALA A 160 1 N VAL A 156 O LEU A 177
SHEET 5 A 7 ILE A 11 LEU A 18 1 N LEU A 17 O ILE A 157
SHEET 6 A 7 TYR A 217 ASP A 221 -1 O LEU A 218 N GLY A 14
SHEET 7 A 7 GLN A 226 VAL A 229 -1 O GLN A 226 N ASP A 221
SHEET 1 B 9 GLU A 270 ILE A 275 0
SHEET 2 B 9 VAL A 292 ARG A 296 1 O LEU A 294 N ILE A 275
SHEET 3 B 9 VAL A 329 ARG A 332 1 O ILE A 330 N TYR A 295
SHEET 4 B 9 LEU A 386 PHE A 390 1 O ARG A 387 N VAL A 331
SHEET 5 B 9 GLU A 425 VAL A 430 1 O MSE A 429 N PHE A 390
SHEET 6 B 9 PHE A 448 ILE A 451 1 O SER A 450 N VAL A 430
SHEET 7 B 9 TRP A 498 MSE A 501 1 O GLY A 500 N PHE A 449
SHEET 8 B 9 GLU A 522 MSE A 525 1 O SER A 524 N MSE A 501
SHEET 9 B 9 GLU A 270 ILE A 275 1 N CYS A 272 O PHE A 523
SHEET 1 C 7 LEU B 6 SER B 8 0
SHEET 2 C 7 ALA B 201 ILE B 202 -1 O ALA B 201 N SER B 8
SHEET 3 C 7 VAL B 176 THR B 181 1 N THR B 181 O ILE B 202
SHEET 4 C 7 VAL B 156 ALA B 160 1 N LEU B 158 O ILE B 180
SHEET 5 C 7 GLY B 10 LEU B 18 1 N LEU B 17 O VAL B 159
SHEET 6 C 7 TYR B 217 ALA B 222 -1 O LEU B 218 N GLY B 14
SHEET 7 C 7 GLN B 226 VAL B 229 -1 O GLN B 226 N ASP B 221
SHEET 1 D 9 GLU B 270 ILE B 275 0
SHEET 2 D 9 VAL B 292 ARG B 296 1 O LEU B 294 N ILE B 275
SHEET 3 D 9 VAL B 329 ARG B 332 1 O ILE B 330 N VAL B 292
SHEET 4 D 9 LEU B 386 PHE B 390 1 O ARG B 387 N VAL B 329
SHEET 5 D 9 GLU B 425 VAL B 430 1 O GLY B 427 N ILE B 388
SHEET 6 D 9 PHE B 448 ILE B 451 1 O SER B 450 N VAL B 430
SHEET 7 D 9 TRP B 498 MSE B 501 1 O GLY B 500 N PHE B 449
SHEET 8 D 9 GLU B 522 MSE B 525 1 O SER B 524 N MSE B 501
SHEET 9 D 9 GLU B 270 ILE B 275 1 N CYS B 272 O PHE B 523
LINK C ILE A 77 N MSE A 78 1555 1555 1.33
LINK C MSE A 78 N LEU A 79 1555 1555 1.33
LINK C HIS A 97 N MSE A 98 1555 1555 1.32
LINK C MSE A 98 N THR A 99 1555 1555 1.33
LINK C SER A 188 N NEP A 189 1555 1555 1.31
LINK C NEP A 189 N THR A 190 1555 1555 1.33
LINK C ILE A 192 N MSE A 193 1555 1555 1.31
LINK C MSE A 193 N ALA A 194 1555 1555 1.33
LINK C LYS A 238 N MSE A 239 1555 1555 1.34
LINK C MSE A 239 N ARG A 240 1555 1555 1.33
LINK C PHE A 301 N MSE A 302 1555 1555 1.33
LINK C MSE A 302 N ASP A 303 1555 1555 1.33
LINK C THR A 333 N MSE A 334 1555 1555 1.32
LINK C MSE A 334 N ASP A 335 1555 1555 1.33
LINK C TYR A 344 N MSE A 345 1555 1555 1.34
LINK C MSE A 345 N ASN A 346 1555 1555 1.33
LINK C ALA A 363 N MSE A 364 1555 1555 1.33
LINK C MSE A 364 N ASP A 365 1555 1555 1.32
LINK C ILE A 388 N MSE A 389 1555 1555 1.32
LINK C MSE A 389 N PHE A 390 1555 1555 1.33
LINK C PRO A 391 N MSE A 392 1555 1555 1.34
LINK C MSE A 392 N ILE A 393 1555 1555 1.32
LINK C VAL A 428 N MSE A 429 1555 1555 1.32
LINK C MSE A 429 N VAL A 430 1555 1555 1.32
LINK C ASP A 468 N MSE A 469 1555 1555 1.32
LINK C MSE A 469 N ILE A 470 1555 1555 1.33
LINK C PRO A 476 N MSE A 477 1555 1555 1.33
LINK C MSE A 477 N SER A 478 1555 1555 1.32
LINK C GLY A 500 N MSE A 501 1555 1555 1.33
LINK C MSE A 501 N CYS A 502 1555 1555 1.33
LINK C GLY A 517 N MSE A 518 1555 1555 1.33
LINK C MSE A 518 N GLY A 519 1555 1555 1.34
LINK C SER A 524 N MSE A 525 1555 1555 1.32
LINK C MSE A 525 N SER A 526 1555 1555 1.33
LINK C LEU A 561 N MSE A 562 1555 1555 1.34
LINK C MSE A 562 N THR A 563 1555 1555 1.33
LINK C ILE B 77 N MSE B 78 1555 1555 1.34
LINK C MSE B 78 N LEU B 79 1555 1555 1.33
LINK C HIS B 97 N MSE B 98 1555 1555 1.34
LINK C MSE B 98 N THR B 99 1555 1555 1.33
LINK C SER B 188 N NEP B 189 1555 1555 1.32
LINK C NEP B 189 N THR B 190 1555 1555 1.32
LINK C ILE B 192 N MSE B 193 1555 1555 1.34
LINK C MSE B 193 N ALA B 194 1555 1555 1.34
LINK C LYS B 238 N MSE B 239 1555 1555 1.34
LINK C MSE B 239 N ARG B 240 1555 1555 1.32
LINK C PHE B 301 N MSE B 302 1555 1555 1.34
LINK C MSE B 302 N ASP B 303 1555 1555 1.34
LINK C THR B 333 N MSE B 334 1555 1555 1.32
LINK C MSE B 334 N ASP B 335 1555 1555 1.34
LINK C TYR B 344 N MSE B 345 1555 1555 1.34
LINK C MSE B 345 N ASN B 346 1555 1555 1.33
LINK C ALA B 363 N MSE B 364 1555 1555 1.32
LINK C MSE B 364 N ASP B 365 1555 1555 1.32
LINK C ILE B 388 N MSE B 389 1555 1555 1.32
LINK C MSE B 389 N PHE B 390 1555 1555 1.33
LINK C PRO B 391 N MSE B 392 1555 1555 1.34
LINK C MSE B 392 N ILE B 393 1555 1555 1.33
LINK C VAL B 428 N MSE B 429 1555 1555 1.33
LINK C MSE B 429 N VAL B 430 1555 1555 1.31
LINK C ASP B 468 N MSE B 469 1555 1555 1.33
LINK C MSE B 469 N ILE B 470 1555 1555 1.33
LINK C PRO B 476 N MSE B 477 1555 1555 1.31
LINK C MSE B 477 N SER B 478 1555 1555 1.31
LINK C GLY B 500 N MSE B 501 1555 1555 1.32
LINK C MSE B 501 N CYS B 502 1555 1555 1.33
LINK C GLY B 517 N MSE B 518 1555 1555 1.34
LINK C MSE B 518 N GLY B 519 1555 1555 1.34
LINK C SER B 524 N MSE B 525 1555 1555 1.33
LINK C MSE B 525 N SER B 526 1555 1555 1.33
LINK C LEU B 561 N MSE B 562 1555 1555 1.34
LINK C MSE B 562 N THR B 563 1555 1555 1.32
LINK O2P NEP A 189 MG MG A 901 1555 1555 1.99
LINK OE1 GLU A 431 MG MG A 901 1555 1555 2.01
LINK OD2 ASP A 455 MG MG A 901 1555 1555 2.05
LINK MG MG A 901 O2 OXL A 903 1555 1555 2.20
LINK MG MG A 901 O1 OXL A 903 1555 1555 2.22
LINK MG MG A 901 O HOH A1001 1555 1555 1.89
LINK O2P NEP B 189 MG MG B 902 1555 1555 2.10
LINK OE1 GLU B 431 MG MG B 902 1555 1555 2.04
LINK OD2 ASP B 455 MG MG B 902 1555 1555 1.86
LINK MG MG B 902 O1 OXL B 904 1555 1555 2.05
LINK MG MG B 902 O2 OXL B 904 1555 1555 2.29
LINK MG MG B 902 O HOH B1002 1555 1555 1.90
SITE 1 AC1 6 NEP A 189 ARG A 358 GLU A 431 ASP A 455
SITE 2 AC1 6 OXL A 903 HOH A1001
SITE 1 AC2 7 NEP B 189 ARG B 358 GLU B 431 ASP B 455
SITE 2 AC2 7 ARG B 465 OXL B 904 HOH B1002
SITE 1 AC3 14 NEP A 189 ARG A 296 ARG A 332 MSE A 429
SITE 2 AC3 14 GLU A 431 GLY A 452 THR A 453 ASN A 454
SITE 3 AC3 14 ASP A 455 ARG A 465 CYS A 502 GLY A 503
SITE 4 AC3 14 MG A 901 HOH A1001
SITE 1 AC4 13 NEP B 189 ARG B 296 ARG B 332 MSE B 429
SITE 2 AC4 13 GLU B 431 GLY B 452 THR B 453 ASN B 454
SITE 3 AC4 13 ASP B 455 ARG B 465 GLY B 503 MG B 902
SITE 4 AC4 13 HOH B1002
CRYST1 85.487 94.084 161.007 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 0.011698 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006211 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
