HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 18-MAY-15 4ZVV
TITLE LACTATE DEHYDROGENASE A IN COMPLEX WITH A TRISUBSTITUTED PIPERIDINE-2,
TITLE 2 4-DIONE INHIBITOR GNE-140
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-LACTATE DEHYDROGENASE A CHAIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: LDH-A,CELL PROLIFERATION-INDUCING GENE 19 PROTEIN,LDH MUSCLE
COMPND 5 SUBUNIT,LDH-M,RENAL CARCINOMA ANTIGEN NY-REN-59;
COMPND 6 EC: 1.1.1.27;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LDHA, PIG19;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE INHIBITOR COMPLEX, LDHA-G02792140, OXIDOREDUCTASE-
KEYWDS 2 OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LI,Z.CHEN,C.EIGENBROT
REVDAT 4 27-SEP-23 4ZVV 1 REMARK
REVDAT 3 28-SEP-16 4ZVV 1 JRNL
REVDAT 2 10-AUG-16 4ZVV 1 JRNL
REVDAT 1 18-MAY-16 4ZVV 0
JRNL AUTH A.BOUDREAU,H.E.PURKEY,A.HITZ,K.ROBARGE,D.PETERSON,S.LABADIE,
JRNL AUTH 2 M.KWONG,R.HONG,M.GAO,C.DEL NAGRO,R.PUSAPATI,S.MA,L.SALPHATI,
JRNL AUTH 3 J.PANG,A.ZHOU,T.LAI,Y.LI,Z.CHEN,B.WEI,I.YEN,S.SIDERIS,
JRNL AUTH 4 M.MCCLELAND,R.FIRESTEIN,L.CORSON,A.VANDERBILT,S.WILLIAMS,
JRNL AUTH 5 A.DAEMEN,M.BELVIN,C.EIGENBROT,P.K.JACKSON,S.MALEK,
JRNL AUTH 6 G.HATZIVASSILIOU,D.SAMPATH,M.EVANGELISTA,T.O'BRIEN
JRNL TITL METABOLIC PLASTICITY UNDERPINS INNATE AND ACQUIRED
JRNL TITL 2 RESISTANCE TO LDHA INHIBITION.
JRNL REF NAT.CHEM.BIOL. V. 12 779 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 27479743
JRNL DOI 10.1038/NCHEMBIO.2143
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 56050
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.232
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1152
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1656
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 35.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.3140
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 343
REMARK 3 SOLVENT ATOMS : 309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.68000
REMARK 3 B33 (A**2) : -0.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.86000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.534
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.270
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.210
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.437
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10803 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14668 ; 1.136 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1321 ; 4.655 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 407 ;38.921 ;25.086
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1945 ;14.827 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;18.909 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1700 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8088 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6560 ; 0.455 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10616 ; 0.739 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4243 ; 1.080 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4051 ; 1.589 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ZVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209984.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
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 : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56050
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 38.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1I10
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, MALONATE PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 40.64400
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: 28010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -275.0 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 MET A 0
REMARK 465 MET B 0
REMARK 465 MET C 0
REMARK 465 MET D 0
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS D 13 O
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 NE2 GLN A 99 OE2 GLU A 103 1.91
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 80 CE LYS A 80 NZ 0.163
REMARK 500 GLN A 99 CG GLN A 99 CD 0.139
REMARK 500 GLN A 99 CD GLN A 99 NE2 0.170
REMARK 500 GLU A 101 CG GLU A 101 CD -0.157
REMARK 500 GLU A 101 CD GLU A 101 OE1 0.115
REMARK 500 ARG A 105 CG ARG A 105 CD 0.177
REMARK 500 LYS B 13 CB LYS B 13 CG -0.298
REMARK 500 GLU C 15 CB GLU C 15 CG -0.119
REMARK 500 LYS C 242 CE LYS C 242 NZ 0.251
REMARK 500 LYS C 283 CE LYS C 283 NZ 0.227
REMARK 500 LYS D 13 CB LYS D 13 CG -0.294
REMARK 500 LYS D 13 CA LYS D 13 C 0.430
REMARK 500 ARG D 98 CZ ARG D 98 NH2 0.108
REMARK 500 GLU D 101 CB GLU D 101 CG 0.122
REMARK 500 GLU D 103 CD GLU D 103 OE1 0.089
REMARK 500 LYS D 117 CE LYS D 117 NZ 0.163
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 105 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LYS D 13 CB - CA - C ANGL. DEV. = 25.8 DEGREES
REMARK 500 LYS D 13 CB - CG - CD ANGL. DEV. = 25.2 DEGREES
REMARK 500 ARG D 98 NE - CZ - NH1 ANGL. DEV. = -4.4 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 LEU A 189 -169.58 -118.40
REMARK 500 SER A 248 -61.56 -126.89
REMARK 500 SER B 248 -61.21 -138.38
REMARK 500 ASP B 285 83.41 -67.26
REMARK 500 SER C 248 -60.93 -138.62
REMARK 500 LYS D 13 49.05 -103.85
REMARK 500 ASN D 20 57.50 -146.27
REMARK 500 SER D 248 -61.58 -143.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GN0 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GN0 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GN0 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GN0 D 403
DBREF 4ZVV A 0 331 UNP P00338 LDHA_HUMAN 30 361
DBREF 4ZVV B 0 331 UNP P00338 LDHA_HUMAN 30 361
DBREF 4ZVV C 0 331 UNP P00338 LDHA_HUMAN 30 361
DBREF 4ZVV D 0 331 UNP P00338 LDHA_HUMAN 30 361
SEQRES 1 A 332 MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU
SEQRES 2 A 332 LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL
SEQRES 3 A 332 GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE
SEQRES 4 A 332 LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP
SEQRES 5 A 332 VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU
SEQRES 6 A 332 GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL
SEQRES 7 A 332 SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU
SEQRES 8 A 332 VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU
SEQRES 9 A 332 SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE
SEQRES 10 A 332 LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN
SEQRES 11 A 332 CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU
SEQRES 12 A 332 THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN
SEQRES 13 A 332 ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG
SEQRES 14 A 332 PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO
SEQRES 15 A 332 LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP
SEQRES 16 A 332 SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY
SEQRES 17 A 332 VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP
SEQRES 18 A 332 LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL
SEQRES 19 A 332 VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR
SEQRES 20 A 332 THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA
SEQRES 21 A 332 GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL
SEQRES 22 A 332 SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP
SEQRES 23 A 332 VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY
SEQRES 24 A 332 ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU
SEQRES 25 A 332 GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY
SEQRES 26 A 332 ILE GLN LYS GLU LEU GLN PHE
SEQRES 1 B 332 MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU
SEQRES 2 B 332 LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL
SEQRES 3 B 332 GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE
SEQRES 4 B 332 LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP
SEQRES 5 B 332 VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU
SEQRES 6 B 332 GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL
SEQRES 7 B 332 SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU
SEQRES 8 B 332 VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU
SEQRES 9 B 332 SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE
SEQRES 10 B 332 LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN
SEQRES 11 B 332 CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU
SEQRES 12 B 332 THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN
SEQRES 13 B 332 ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG
SEQRES 14 B 332 PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO
SEQRES 15 B 332 LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP
SEQRES 16 B 332 SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY
SEQRES 17 B 332 VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP
SEQRES 18 B 332 LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL
SEQRES 19 B 332 VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR
SEQRES 20 B 332 THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA
SEQRES 21 B 332 GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL
SEQRES 22 B 332 SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP
SEQRES 23 B 332 VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY
SEQRES 24 B 332 ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU
SEQRES 25 B 332 GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY
SEQRES 26 B 332 ILE GLN LYS GLU LEU GLN PHE
SEQRES 1 C 332 MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU
SEQRES 2 C 332 LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL
SEQRES 3 C 332 GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE
SEQRES 4 C 332 LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP
SEQRES 5 C 332 VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU
SEQRES 6 C 332 GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL
SEQRES 7 C 332 SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU
SEQRES 8 C 332 VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU
SEQRES 9 C 332 SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE
SEQRES 10 C 332 LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN
SEQRES 11 C 332 CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU
SEQRES 12 C 332 THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN
SEQRES 13 C 332 ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG
SEQRES 14 C 332 PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO
SEQRES 15 C 332 LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP
SEQRES 16 C 332 SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY
SEQRES 17 C 332 VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP
SEQRES 18 C 332 LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL
SEQRES 19 C 332 VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR
SEQRES 20 C 332 THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA
SEQRES 21 C 332 GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL
SEQRES 22 C 332 SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP
SEQRES 23 C 332 VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY
SEQRES 24 C 332 ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU
SEQRES 25 C 332 GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY
SEQRES 26 C 332 ILE GLN LYS GLU LEU GLN PHE
SEQRES 1 D 332 MET ALA THR LEU LYS ASP GLN LEU ILE TYR ASN LEU LEU
SEQRES 2 D 332 LYS GLU GLU GLN THR PRO GLN ASN LYS ILE THR VAL VAL
SEQRES 3 D 332 GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE
SEQRES 4 D 332 LEU MET LYS ASP LEU ALA ASP GLU LEU ALA LEU VAL ASP
SEQRES 5 D 332 VAL ILE GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU
SEQRES 6 D 332 GLN HIS GLY SER LEU PHE LEU ARG THR PRO LYS ILE VAL
SEQRES 7 D 332 SER GLY LYS ASP TYR ASN VAL THR ALA ASN SER LYS LEU
SEQRES 8 D 332 VAL ILE ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU
SEQRES 9 D 332 SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE
SEQRES 10 D 332 LYS PHE ILE ILE PRO ASN VAL VAL LYS TYR SER PRO ASN
SEQRES 11 D 332 CYS LYS LEU LEU ILE VAL SER ASN PRO VAL ASP ILE LEU
SEQRES 12 D 332 THR TYR VAL ALA TRP LYS ILE SER GLY PHE PRO LYS ASN
SEQRES 13 D 332 ARG VAL ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG
SEQRES 14 D 332 PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS PRO
SEQRES 15 D 332 LEU SER CYS HIS GLY TRP VAL LEU GLY GLU HIS GLY ASP
SEQRES 16 D 332 SER SER VAL PRO VAL TRP SER GLY MET ASN VAL ALA GLY
SEQRES 17 D 332 VAL SER LEU LYS THR LEU HIS PRO ASP LEU GLY THR ASP
SEQRES 18 D 332 LYS ASP LYS GLU GLN TRP LYS GLU VAL HIS LYS GLN VAL
SEQRES 19 D 332 VAL GLU SER ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR
SEQRES 20 D 332 THR SER TRP ALA ILE GLY LEU SER VAL ALA ASP LEU ALA
SEQRES 21 D 332 GLU SER ILE MET LYS ASN LEU ARG ARG VAL HIS PRO VAL
SEQRES 22 D 332 SER THR MET ILE LYS GLY LEU TYR GLY ILE LYS ASP ASP
SEQRES 23 D 332 VAL PHE LEU SER VAL PRO CYS ILE LEU GLY GLN ASN GLY
SEQRES 24 D 332 ILE SER ASP LEU VAL LYS VAL THR LEU THR SER GLU GLU
SEQRES 25 D 332 GLU ALA ARG LEU LYS LYS SER ALA ASP THR LEU TRP GLY
SEQRES 26 D 332 ILE GLN LYS GLU LEU GLN PHE
HET NAD A 401 44
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET GN0 A 405 33
HET NAD B 401 44
HET SO4 B 402 5
HET SO4 B 403 5
HET GN0 B 404 33
HET NAD C 401 44
HET SO4 C 402 5
HET GN0 C 403 33
HET NAD D 401 44
HET SO4 D 402 5
HET GN0 D 403 33
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM SO4 SULFATE ION
HETNAM GN0 (2~{R})-5-(2-CHLOROPHENYL)SULFANYL-2-(4-MORPHOLIN-4-
HETNAM 2 GN0 YLPHENYL)-4-OXIDANYL-2-THIOPHEN-3-YL-1,3-
HETNAM 3 GN0 DIHYDROPYRIDIN-6-ONE
HETSYN GN0 INHIBITOR GNE-140
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 6 SO4 7(O4 S 2-)
FORMUL 9 GN0 4(C25 H23 CL N2 O3 S2)
FORMUL 20 HOH *309(H2 O)
HELIX 1 AA1 THR A 2 LEU A 7 1 6
HELIX 2 AA2 GLY A 28 ASP A 42 1 15
HELIX 3 AA3 ILE A 53 HIS A 66 1 14
HELIX 4 AA4 GLY A 67 LEU A 71 5 5
HELIX 5 AA5 ASP A 81 ALA A 86 5 6
HELIX 6 AA6 SER A 104 SER A 127 1 24
HELIX 7 AA7 PRO A 138 GLY A 151 1 14
HELIX 8 AA8 PRO A 153 ASN A 155 5 3
HELIX 9 AA9 CYS A 162 GLY A 178 1 17
HELIX 10 AB1 HIS A 180 CYS A 184 5 5
HELIX 11 AB2 TRP A 200 GLY A 202 5 3
HELIX 12 AB3 LEU A 210 HIS A 214 1 5
HELIX 13 AB4 LYS A 227 GLY A 245 1 19
HELIX 14 AB5 SER A 248 LYS A 264 1 17
HELIX 15 AB6 THR A 308 LYS A 327 1 20
HELIX 16 AB7 THR B 2 LEU B 7 1 6
HELIX 17 AB8 GLY B 28 LYS B 41 1 14
HELIX 18 AB9 ILE B 53 HIS B 66 1 14
HELIX 19 AC1 GLY B 67 LEU B 71 5 5
HELIX 20 AC2 ASP B 81 THR B 85 5 5
HELIX 21 AC3 SER B 104 SER B 127 1 24
HELIX 22 AC4 PRO B 138 GLY B 151 1 14
HELIX 23 AC5 PRO B 153 ASN B 155 5 3
HELIX 24 AC6 CYS B 162 GLY B 178 1 17
HELIX 25 AC7 HIS B 180 LEU B 182 5 3
HELIX 26 AC8 TRP B 200 GLY B 202 5 3
HELIX 27 AC9 LEU B 210 HIS B 214 1 5
HELIX 28 AD1 TRP B 226 GLY B 245 1 20
HELIX 29 AD2 SER B 248 ASN B 265 1 18
HELIX 30 AD3 THR B 308 LYS B 327 1 20
HELIX 31 AD4 THR C 2 LEU C 7 1 6
HELIX 32 AD5 GLY C 28 LYS C 41 1 14
HELIX 33 AD6 ILE C 53 GLY C 67 1 15
HELIX 34 AD7 SER C 68 LEU C 71 5 4
HELIX 35 AD8 ASP C 81 ALA C 86 5 6
HELIX 36 AD9 SER C 104 SER C 127 1 24
HELIX 37 AE1 PRO C 138 GLY C 151 1 14
HELIX 38 AE2 PRO C 153 ASN C 155 5 3
HELIX 39 AE3 CYS C 162 GLY C 178 1 17
HELIX 40 AE4 HIS C 180 LEU C 182 5 3
HELIX 41 AE5 LEU C 210 HIS C 214 1 5
HELIX 42 AE6 TRP C 226 GLY C 245 1 20
HELIX 43 AE7 SER C 248 LYS C 264 1 17
HELIX 44 AE8 THR C 308 LYS C 327 1 20
HELIX 45 AE9 THR D 2 LEU D 7 1 6
HELIX 46 AF1 GLY D 28 LYS D 41 1 14
HELIX 47 AF2 ILE D 53 HIS D 66 1 14
HELIX 48 AF3 GLY D 67 LEU D 71 5 5
HELIX 49 AF4 ASP D 81 ALA D 86 5 6
HELIX 50 AF5 ASN D 107 SER D 127 1 21
HELIX 51 AF6 PRO D 138 GLY D 151 1 14
HELIX 52 AF7 PRO D 153 ASN D 155 5 3
HELIX 53 AF8 CYS D 162 GLY D 178 1 17
HELIX 54 AF9 HIS D 180 CYS D 184 5 5
HELIX 55 AG1 VAL D 199 GLY D 202 5 4
HELIX 56 AG2 LEU D 210 HIS D 214 1 5
HELIX 57 AG3 LYS D 227 GLY D 245 1 19
HELIX 58 AG4 SER D 248 LYS D 264 1 17
HELIX 59 AG5 THR D 308 LYS D 327 1 20
SHEET 1 AA1 4 ILE A 8 ASN A 10 0
SHEET 2 AA1 4 GLY D 298 VAL D 303 -1 O LEU D 302 N TYR A 9
SHEET 3 AA1 4 PHE D 287 GLY D 295 -1 N PRO D 291 O VAL D 303
SHEET 4 AA1 4 ARG D 268 MET D 275 -1 N HIS D 270 O CYS D 292
SHEET 1 AA2 6 LYS A 75 SER A 78 0
SHEET 2 AA2 6 GLU A 46 VAL A 50 1 N LEU A 47 O VAL A 77
SHEET 3 AA2 6 LYS A 21 VAL A 25 1 N ILE A 22 O ALA A 48
SHEET 4 AA2 6 LEU A 90 ILE A 93 1 O ILE A 92 N VAL A 25
SHEET 5 AA2 6 LYS A 131 ILE A 134 1 O LEU A 133 N VAL A 91
SHEET 6 AA2 6 VAL A 157 GLY A 159 1 O ILE A 158 N LEU A 132
SHEET 1 AA3 2 VAL A 188 LEU A 189 0
SHEET 2 AA3 2 VAL A 197 PRO A 198 -1 O VAL A 197 N LEU A 189
SHEET 1 AA4 2 ASN A 204 VAL A 205 0
SHEET 2 AA4 2 VAL A 208 SER A 209 -1 O VAL A 208 N VAL A 205
SHEET 1 AA5 4 ARG A 268 MET A 275 0
SHEET 2 AA5 4 PHE A 287 GLY A 295 -1 O CYS A 292 N HIS A 270
SHEET 3 AA5 4 GLY A 298 VAL A 303 -1 O VAL A 303 N PRO A 291
SHEET 4 AA5 4 ILE D 8 ASN D 10 -1 O TYR D 9 N LEU A 302
SHEET 1 AA6 4 ILE B 8 ASN B 10 0
SHEET 2 AA6 4 GLY C 298 VAL C 303 -1 O LEU C 302 N TYR B 9
SHEET 3 AA6 4 PHE C 287 GLY C 295 -1 N GLY C 295 O GLY C 298
SHEET 4 AA6 4 ARG C 268 MET C 275 -1 N HIS C 270 O CYS C 292
SHEET 1 AA7 6 ILE B 76 SER B 78 0
SHEET 2 AA7 6 GLU B 46 VAL B 50 1 N LEU B 47 O VAL B 77
SHEET 3 AA7 6 LYS B 21 VAL B 25 1 N VAL B 24 O ALA B 48
SHEET 4 AA7 6 LEU B 90 ILE B 93 1 O ILE B 92 N VAL B 25
SHEET 5 AA7 6 LYS B 131 ILE B 134 1 O LYS B 131 N VAL B 91
SHEET 6 AA7 6 VAL B 157 GLY B 159 1 O ILE B 158 N LEU B 132
SHEET 1 AA8 3 CYS B 184 HIS B 185 0
SHEET 2 AA8 3 ASN B 204 VAL B 205 -1 O ASN B 204 N HIS B 185
SHEET 3 AA8 3 VAL B 208 SER B 209 -1 O VAL B 208 N VAL B 205
SHEET 1 AA9 2 VAL B 188 GLY B 190 0
SHEET 2 AA9 2 SER B 196 PRO B 198 -1 O VAL B 197 N LEU B 189
SHEET 1 AB1 4 ARG B 268 MET B 275 0
SHEET 2 AB1 4 PHE B 287 GLY B 295 -1 O CYS B 292 N HIS B 270
SHEET 3 AB1 4 GLY B 298 VAL B 303 -1 O VAL B 303 N PRO B 291
SHEET 4 AB1 4 ILE C 8 ASN C 10 -1 O TYR C 9 N LEU B 302
SHEET 1 AB2 6 ILE C 76 SER C 78 0
SHEET 2 AB2 6 GLU C 46 VAL C 50 1 N LEU C 47 O VAL C 77
SHEET 3 AB2 6 LYS C 21 VAL C 25 1 N VAL C 24 O ALA C 48
SHEET 4 AB2 6 SER C 88 ILE C 93 1 O ILE C 92 N THR C 23
SHEET 5 AB2 6 LYS C 131 ILE C 134 1 O LEU C 133 N VAL C 91
SHEET 6 AB2 6 VAL C 157 GLY C 159 1 O ILE C 158 N LEU C 132
SHEET 1 AB3 3 CYS C 184 HIS C 185 0
SHEET 2 AB3 3 ASN C 204 VAL C 205 -1 O ASN C 204 N HIS C 185
SHEET 3 AB3 3 VAL C 208 SER C 209 -1 O VAL C 208 N VAL C 205
SHEET 1 AB4 2 VAL C 188 LEU C 189 0
SHEET 2 AB4 2 VAL C 197 PRO C 198 -1 O VAL C 197 N LEU C 189
SHEET 1 AB5 6 LYS D 75 SER D 78 0
SHEET 2 AB5 6 GLU D 46 VAL D 50 1 N LEU D 47 O VAL D 77
SHEET 3 AB5 6 LYS D 21 VAL D 25 1 N VAL D 24 O ALA D 48
SHEET 4 AB5 6 LEU D 90 ILE D 93 1 O ILE D 92 N VAL D 25
SHEET 5 AB5 6 LYS D 131 ILE D 134 1 O LEU D 133 N VAL D 91
SHEET 6 AB5 6 VAL D 157 GLY D 159 1 O ILE D 158 N LEU D 132
SHEET 1 AB6 2 ASN D 204 VAL D 205 0
SHEET 2 AB6 2 VAL D 208 SER D 209 -1 O VAL D 208 N VAL D 205
CISPEP 1 ASN A 137 PRO A 138 0 -4.91
CISPEP 2 ASN B 137 PRO B 138 0 0.05
CISPEP 3 ASN C 137 PRO C 138 0 -5.02
CISPEP 4 ASN D 137 PRO D 138 0 -1.91
SITE 1 AC1 22 GLY A 28 ALA A 29 VAL A 30 ASP A 51
SITE 2 AC1 22 VAL A 52 ILE A 53 THR A 94 ALA A 95
SITE 3 AC1 22 GLY A 96 ARG A 98 ILE A 115 VAL A 135
SITE 4 AC1 22 ASN A 137 LEU A 164 HIS A 192 ILE A 251
SITE 5 AC1 22 GN0 A 405 HOH A 506 HOH A 511 HOH A 515
SITE 6 AC1 22 HOH A 524 HOH A 528
SITE 1 AC2 4 HIS A 185 ARG C 170 HIS C 185 HOH C 561
SITE 1 AC3 7 ARG A 170 HIS A 185 HOH A 508 HOH A 529
SITE 2 AC3 7 HOH A 549 LEU C 182 HIS C 185
SITE 1 AC4 3 TRP A 147 PRO A 153 LYS A 154
SITE 1 AC5 12 ASN A 137 ASP A 165 ARG A 168 HIS A 192
SITE 2 AC5 12 GLY A 193 ASP A 194 ALA A 237 TYR A 238
SITE 3 AC5 12 ILE A 241 GLY A 245 THR A 247 NAD A 401
SITE 1 AC6 23 GLY B 28 ALA B 29 VAL B 30 ASP B 51
SITE 2 AC6 23 VAL B 52 ILE B 53 THR B 94 ALA B 95
SITE 3 AC6 23 GLY B 96 ARG B 98 ILE B 115 ILE B 119
SITE 4 AC6 23 VAL B 135 ASN B 137 LEU B 164 HIS B 192
SITE 5 AC6 23 ILE B 251 GN0 B 404 HOH B 502 HOH B 504
SITE 6 AC6 23 HOH B 518 HOH B 538 HOH B 539
SITE 1 AC7 7 ARG B 170 HIS B 185 HOH B 536 HOH B 546
SITE 2 AC7 7 HOH B 562 LEU D 182 HIS D 185
SITE 1 AC8 3 TRP B 147 PRO B 153 LYS B 154
SITE 1 AC9 13 ARG B 98 ASN B 137 LEU B 164 ASP B 165
SITE 2 AC9 13 ARG B 168 HIS B 192 GLY B 193 ALA B 237
SITE 3 AC9 13 TYR B 238 ILE B 241 GLY B 245 THR B 247
SITE 4 AC9 13 NAD B 401
SITE 1 AD1 21 GLY C 28 ALA C 29 VAL C 30 ASP C 51
SITE 2 AD1 21 VAL C 52 ILE C 53 THR C 94 ALA C 95
SITE 3 AD1 21 GLY C 96 ARG C 98 ILE C 119 VAL C 135
SITE 4 AD1 21 ASN C 137 HIS C 192 THR C 247 GN0 C 403
SITE 5 AD1 21 HOH C 507 HOH C 511 HOH C 520 HOH C 526
SITE 6 AD1 21 HOH C 557
SITE 1 AD2 4 TRP C 147 PRO C 153 LYS C 154 HOH C 543
SITE 1 AD3 13 ARG C 98 ASN C 137 LEU C 164 ASP C 165
SITE 2 AD3 13 ARG C 168 HIS C 192 GLY C 193 ALA C 237
SITE 3 AD3 13 TYR C 238 ILE C 241 THR C 247 NAD C 401
SITE 4 AD3 13 HOH C 573
SITE 1 AD4 23 GLY D 28 ALA D 29 VAL D 30 ASP D 51
SITE 2 AD4 23 VAL D 52 ILE D 53 THR D 94 ALA D 95
SITE 3 AD4 23 GLY D 96 ILE D 115 PHE D 118 ILE D 119
SITE 4 AD4 23 VAL D 135 ASN D 137 SER D 160 HIS D 192
SITE 5 AD4 23 THR D 247 GN0 D 403 HOH D 510 HOH D 522
SITE 6 AD4 23 HOH D 529 HOH D 534 HOH D 538
SITE 1 AD5 6 LEU B 182 HIS B 185 ARG D 170 HIS D 185
SITE 2 AD5 6 HOH D 543 HOH D 564
SITE 1 AD6 14 GLN D 99 ASN D 137 ASP D 165 ARG D 168
SITE 2 AD6 14 HIS D 192 GLY D 193 ASP D 194 ALA D 237
SITE 3 AD6 14 TYR D 238 ILE D 241 GLY D 245 THR D 247
SITE 4 AD6 14 NAD D 401 HOH D 541
CRYST1 79.164 81.288 102.470 90.00 98.31 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 0.012632 0.000000 0.001846 0.00000
SCALE2 0.000000 0.012302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009863 0.00000
(ATOM LINES ARE NOT SHOWN.)
END