HEADER LIGASE(PEPTIDOGLYCAN SYNTHESIS) 18-JUL-94 2DLN
TITLE VANCOMYCIN RESISTANCE: STRUCTURE OF D-ALANINE:D-ALANINE
TITLE 2 LIGASE AT 2.3 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.3.2.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS LIGASE(PEPTIDOGLYCAN SYNTHESIS)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.KNOX,P.C.MOEWS,C.FAN
REVDAT 3 24-FEB-09 2DLN 1 VERSN
REVDAT 2 01-APR-03 2DLN 1 JRNL
REVDAT 1 01-NOV-95 2DLN 0
JRNL AUTH C.FAN,P.C.MOEWS,C.T.WALSH,J.R.KNOX
JRNL TITL VANCOMYCIN RESISTANCE: STRUCTURE OF
JRNL TITL 2 D-ALANINE:D-ALANINE LIGASE AT 2.3 A RESOLUTION.
JRNL REF SCIENCE V. 266 439 1994
JRNL REFN ISSN 0036-8075
JRNL PMID 7939684
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ, X-PLOR
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 9776
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 292
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 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) : 0.540 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.950 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.470 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.820 ; 1.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THERE IS NO NON-CRYSTALLOGRAPHIC
REMARK 3 SYMMETRY. A CLOSE DIMER IS FORMED BY THE TWO-FOLD DIAD OF THE
REMARK 3 SPACE GROUP (P 21 21 2).
REMARK 4
REMARK 4 2DLN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 49.65000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.70000
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: MONOMERIC
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 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 OG SER A 281 O HOH A 654 1.61
REMARK 500 O2 PHY A 320 O HOH A 654 1.89
REMARK 500 O GLY A 34 O HOH A 613 1.90
REMARK 500 OG1 THR A 247 O HOH A 646 2.08
REMARK 500 CB ALA A 244 O HOH A 677 2.08
REMARK 500 OE1 GLU A 220 O HOH A 665 2.08
REMARK 500 O ASP A 69 NE2 GLN A 73 2.12
REMARK 500 O ASP A 3 O HOH A 462 2.18
REMARK 500 NH1 ARG A 99 OE1 GLU A 176 2.18
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 456 O HOH A 644 3557 1.41
REMARK 500 O HOH A 450 O HOH A 689 3557 1.62
REMARK 500 O HOH A 523 O HOH A 530 3546 1.96
REMARK 500 O HOH A 404 O HOH A 497 2555 2.07
REMARK 500 O HOH A 640 O HOH A 641 1556 2.07
REMARK 500 O HOH A 593 O HOH A 593 2565 2.09
REMARK 500 OE1 GLU A 32 O HOH A 541 3557 2.13
REMARK 500 CD2 LEU A 139 NH1 ARG A 202 3546 2.17
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 16 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 16 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 41 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 65 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 THR A 84 N - CA - C ANGL. DEV. = 18.7 DEGREES
REMARK 500 ARG A 99 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 LEU A 139 CB - CA - C ANGL. DEV. = 13.1 DEGREES
REMARK 500 LEU A 139 CA - CB - CG ANGL. DEV. = 30.4 DEGREES
REMARK 500 ARG A 147 NE - CZ - NH1 ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLU A 176 OE1 - CD - OE2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 LEU A 178 CA - CB - CG ANGL. DEV. = 19.9 DEGREES
REMARK 500 TYR A 210 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR A 210 CB - CG - CD1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 MET A 292 CA - CB - CG ANGL. DEV. = 10.5 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 THR A 2 -52.31 73.25
REMARK 500 LYS A 43 32.57 -87.74
REMARK 500 GLU A 44 -80.14 -160.89
REMARK 500 SER A 52 0.04 -67.72
REMARK 500 THR A 71 -70.42 -52.59
REMARK 500 GLN A 130 -26.26 -141.75
REMARK 500 ALA A 136 2.94 -66.73
REMARK 500 ALA A 159 145.09 70.94
REMARK 500 SER A 274 73.58 -153.15
REMARK 500 MET A 277 42.63 -152.77
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 404 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH A 487 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 502 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH A 513 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH A 518 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A 522 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 536 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH A 543 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH A 549 DISTANCE = 5.08 ANGSTROMS
REMARK 525 HOH A 553 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A 557 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A 561 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 564 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH A 566 DISTANCE = 9.67 ANGSTROMS
REMARK 525 HOH A 575 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH A 587 DISTANCE = 7.94 ANGSTROMS
REMARK 525 HOH A 590 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A 591 DISTANCE = 10.01 ANGSTROMS
REMARK 525 HOH A 592 DISTANCE = 9.17 ANGSTROMS
REMARK 525 HOH A 593 DISTANCE = 8.22 ANGSTROMS
REMARK 525 HOH A 594 DISTANCE = 7.66 ANGSTROMS
REMARK 525 HOH A 595 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH A 596 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A 597 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH A 600 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH A 601 DISTANCE = 10.75 ANGSTROMS
REMARK 525 HOH A 602 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH A 605 DISTANCE = 7.85 ANGSTROMS
REMARK 525 HOH A 615 DISTANCE = 9.22 ANGSTROMS
REMARK 525 HOH A 616 DISTANCE = 9.47 ANGSTROMS
REMARK 525 HOH A 618 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH A 628 DISTANCE = 7.89 ANGSTROMS
REMARK 525 HOH A 629 DISTANCE = 9.76 ANGSTROMS
REMARK 525 HOH A 655 DISTANCE = 9.48 ANGSTROMS
REMARK 525 HOH A 664 DISTANCE = 9.90 ANGSTROMS
REMARK 525 HOH A 673 DISTANCE = 8.33 ANGSTROMS
REMARK 525 HOH A 674 DISTANCE = 9.36 ANGSTROMS
REMARK 525 HOH A 687 DISTANCE = 5.14 ANGSTROMS
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 330 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHY A 320 O4P
REMARK 620 2 GLU A 270 OE2 87.6
REMARK 620 3 ADP A 310 O3B 63.3 71.2
REMARK 620 4 ADP A 310 O2A 134.2 58.3 76.3
REMARK 620 5 ASP A 257 OD2 114.7 74.0 145.2 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 331 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 270 OE2
REMARK 620 2 ADP A 310 O2B 81.6
REMARK 620 3 PHY A 320 O5P 99.8 86.8
REMARK 620 4 HOH A 400 O 177.3 96.3 78.3
REMARK 620 5 ASN A 272 OD1 102.4 167.7 81.2 79.2
REMARK 620 6 GLU A 270 OE1 65.0 104.9 158.5 117.3 87.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ADP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: PHY
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 330
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 331
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 310
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHY A 320
DBREF 2DLN A 2 306 UNP P07862 DDLB_ECOLI 1 305
SEQRES 1 A 306 MET THR ASP LYS ILE ALA VAL LEU LEU GLY GLY THR SER
SEQRES 2 A 306 ALA GLU ARG GLU VAL SER LEU ASN SER GLY ALA ALA VAL
SEQRES 3 A 306 LEU ALA GLY LEU ARG GLU GLY GLY ILE ASP ALA TYR PRO
SEQRES 4 A 306 VAL ASP PRO LYS GLU VAL ASP VAL THR GLN LEU LYS SER
SEQRES 5 A 306 MET GLY PHE GLN LYS VAL PHE ILE ALA LEU HIS GLY ARG
SEQRES 6 A 306 GLY GLY GLU ASP GLY THR LEU GLN GLY MET LEU GLU LEU
SEQRES 7 A 306 MET GLY LEU PRO TYR THR GLY SER GLY VAL MET ALA SER
SEQRES 8 A 306 ALA LEU SER MET ASP LYS LEU ARG SER LYS LEU LEU TRP
SEQRES 9 A 306 GLN GLY ALA GLY LEU PRO VAL ALA PRO TRP VAL ALA LEU
SEQRES 10 A 306 THR ARG ALA GLU PHE GLU LYS GLY LEU SER ASP LYS GLN
SEQRES 11 A 306 LEU ALA GLU ILE SER ALA LEU GLY LEU PRO VAL ILE VAL
SEQRES 12 A 306 LYS PRO SER ARG GLU GLY SER SER VAL GLY MET SER LYS
SEQRES 13 A 306 VAL VAL ALA GLU ASN ALA LEU GLN ASP ALA LEU ARG LEU
SEQRES 14 A 306 ALA PHE GLN HIS ASP GLU GLU VAL LEU ILE GLU LYS TRP
SEQRES 15 A 306 LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY GLU
SEQRES 16 A 306 GLU ILE LEU PRO SER ILE ARG ILE GLN PRO SER GLY THR
SEQRES 17 A 306 PHE TYR ASP TYR GLU ALA LYS TYR LEU SER ASP GLU THR
SEQRES 18 A 306 GLN TYR PHE CYS PRO ALA GLY LEU GLU ALA SER GLN GLU
SEQRES 19 A 306 ALA ASN LEU GLN ALA LEU VAL LEU LYS ALA TRP THR THR
SEQRES 20 A 306 LEU GLY CYS LYS GLY TRP GLY ARG ILE ASP VAL MET LEU
SEQRES 21 A 306 ASP SER ASP GLY GLN PHE TYR LEU LEU GLU ALA ASN THR
SEQRES 22 A 306 SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA
SEQRES 23 A 306 ALA ARG GLN ALA GLY MET SER PHE SER GLN LEU VAL VAL
SEQRES 24 A 306 ARG ILE LEU GLU LEU ALA ASP
HET MG A 330 1
HET MG A 331 1
HET ADP A 310 27
HET PHY A 320 16
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PHY 1(S)-AMINOETHYL-(2-CARBOXYPROPYL)PHOSPHORYL-
HETNAM 2 PHY PHOSPHINIC ACID
FORMUL 2 MG 2(MG 2+)
FORMUL 4 ADP C10 H15 N5 O10 P2
FORMUL 5 PHY C6 H15 N O7 P2
FORMUL 6 HOH *292(H2 O)
HELIX 1 H1 GLU A 15 GLY A 34 1 20
HELIX 2 H2 THR A 48 SER A 52 1 5
HELIX 3 H3 THR A 71 MET A 79 1 9
HELIX 4 H4 GLY A 87 ASP A 96 1 10
HELIX 5 H5 LEU A 98 ALA A 107 1 10
HELIX 6 H6 ARG A 119 GLY A 125 1 7
HELIX 7 H7 ASP A 128 LEU A 137 1 10
HELIX 8 H8 LEU A 163 HIS A 173 1 11
HELIX 9 H9 TYR A 212 LEU A 217 1 6
HELIX 10 H10 ALA A 231 THR A 247 1 17
HELIX 11 H11 LEU A 282 GLN A 289 1 8
HELIX 12 H12 PHE A 294 GLU A 303 1 10
SHEET 1 SN 4 ASP A 36 ASP A 41 0
SHEET 2 SN 4 LYS A 4 GLY A 11 1 N VAL A 7 O TYR A 38
SHEET 3 SN 4 LYS A 57 ALA A 61 1 N PHE A 59 O ALA A 6
SHEET 4 SN 4 TYR A 83 GLY A 85 1 N THR A 84 O VAL A 58
SHEET 1 CEN 4 PRO A 113 LEU A 117 0
SHEET 2 CEN 4 GLU A 176 LYS A 181 -1 N ILE A 179 O VAL A 115
SHEET 3 CEN 4 VAL A 141 PRO A 145 -1 N LYS A 144 O LEU A 178
SHEET 4 CEN 4 MET A 154 VAL A 158 -1 N SER A 155 O VAL A 143
SHEET 1 SC 5 GLN A 265 ASN A 272 0
SHEET 2 SC 5 TRP A 253 LEU A 260 -1 N ASP A 257 O GLU A 270
SHEET 3 SC 5 PRO A 186 ILE A 192 -1 N VAL A 190 O ILE A 256
SHEET 4 SC 5 ILE A 197 SER A 206 -1 N ILE A 201 O THR A 189
SHEET 5 SC 5 THR A 221 CYS A 225 -1 N PHE A 224 O ARG A 202
LINK O4P PHY A 320 MG MG A 330 1555 1555 1.88
LINK MG MG A 330 OE2 GLU A 270 1555 1555 2.72
LINK MG MG A 330 O3B ADP A 310 1555 1555 2.63
LINK MG MG A 330 O2A ADP A 310 1555 1555 2.42
LINK MG MG A 330 OD2 ASP A 257 1555 1555 1.98
LINK MG MG A 331 OE2 GLU A 270 1555 1555 1.93
LINK MG MG A 331 O2B ADP A 310 1555 1555 2.28
LINK MG MG A 331 O5P PHY A 320 1555 1555 2.29
LINK MG MG A 331 O HOH A 400 1555 1555 1.87
LINK MG MG A 331 OD1 ASN A 272 1555 1555 2.10
LINK MG MG A 331 OE1 GLU A 270 1555 1555 2.08
CISPEP 1 LEU A 139 PRO A 140 0 3.29
CISPEP 2 CYS A 225 PRO A 226 0 -2.34
SITE 1 ADP 15 LYS A 97 ILE A 142 LYS A 144 SER A 150
SITE 2 ADP 15 SER A 151 GLU A 180 TRP A 182 GLU A 187
SITE 3 ADP 15 PHE A 209 LYS A 215 MET A 259 GLU A 270
SITE 4 ADP 15 ASN A 272 MG A 330 MG A 331
SITE 1 PHY 6 GLU A 15 VAL A 18 HIS A 63 SER A 150
SITE 2 PHY 6 TYR A 216 SER A 281
SITE 1 AC1 5 LYS A 215 ASP A 257 GLU A 270 ADP A 310
SITE 2 AC1 5 PHY A 320
SITE 1 AC2 5 GLU A 270 ASN A 272 ADP A 310 PHY A 320
SITE 2 AC2 5 HOH A 400
SITE 1 AC3 22 LYS A 97 ILE A 142 LYS A 144 GLU A 148
SITE 2 AC3 22 GLY A 149 SER A 150 SER A 151 MET A 154
SITE 3 AC3 22 GLU A 180 LYS A 181 TRP A 182 LEU A 183
SITE 4 AC3 22 GLU A 187 TYR A 210 LYS A 215 ASP A 257
SITE 5 AC3 22 LEU A 269 GLU A 270 PHY A 320 MG A 330
SITE 6 AC3 22 MG A 331 HOH A 413
SITE 1 AC4 21 GLU A 15 GLY A 149 SER A 150 LYS A 215
SITE 2 AC4 21 TYR A 216 ARG A 255 ASP A 257 GLU A 270
SITE 3 AC4 21 ASN A 272 PRO A 275 GLY A 276 SER A 281
SITE 4 AC4 21 LEU A 282 ADP A 310 MG A 330 MG A 331
SITE 5 AC4 21 HOH A 400 HOH A 430 HOH A 531 HOH A 637
SITE 6 AC4 21 HOH A 654
CRYST1 99.300 51.400 51.200 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010070 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019455 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019531 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
